CAZypedia - User contributions [en-ca]

Carbohydrate Binding Module Family 101

2024-01-02T13:43:06Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM101.html
|}
</div>


== Ligand specificities ==

[[File:Figure.png|thumb|'''Figure 1. Carbohydrate array assays of WfCBM101. ''' The binding of WfCBM101 to agarose and other galactans in red algae (A), and several other polysaccharides (B) was evaluated. κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from ''Ascophyllum nodosum''. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Three parallels were conducted for each polysaccharide.''' ]]

The first characterized member in the CBM101 family is WfCBM101 <cite>Mei2023</cite>. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose <cite>Chi2012</cite>. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of WfCBM101 as a tool in the ''in situ'' investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The ''in situ'' visualization of agarose in red alga ''Gelidium amansii'' was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e<sup>-5</sup>). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.

== Family Firsts ==
;First Identified
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<sup>T</sup> <cite>Chen2016</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=38010608
#Chi2012 pmid=22526785
#Chen2016 pmid=27220912
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM101]]

Carbohydrate Binding Module Family 99

2024-01-02T13:34:55Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from ''Ascophyllum nodosum''. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10<sup>-4</sup> M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the ''in situ'' investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The ''in situ'' visualization of porphyran in red alga ''Porphyra haitanensis'' was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium ''Flammeovirga sp''. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 101

2024-01-02T13:25:56Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM101.html
|}
</div>


== Ligand specificities ==

[[File:Figure.png|thumb|'''Figure 1. Carbohydrate array assays of WfCBM101. ''' The binding of WfCBM101 to agarose and other galactans in red algae (A), and several other polysaccharides (B) was evaluated. κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from ''Ascophyllum nodosum''. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Three parallels were conducted for each polysaccharide.''' ]]

The first characterized member in the CBM101 family is WfCBM101 <cite>Mei2023</cite>. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose <cite>Chi2012</cite>. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of WfCBM101 as a tool in the ''in situ'' investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The in situ visualization of agarose in red alga Gelidium amansii was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e<sup>-5</sup>). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.

== Family Firsts ==
;First Identified
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<sup>T</sup> <cite>Chen2016</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=38010608
#Chi2012 pmid=22526785
#Chen2016 pmid=27220912
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM101]]

Carbohydrate Binding Module Family 99

2024-01-02T13:23:23Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from ''Ascophyllum nodosum''. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10<sup>-4</sup> M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga ''Porphyra haitanensis'' was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium ''Flammeovirga sp''. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T13:22:56Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10<sup>-4</sup> M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga ''Porphyra haitanensis'' was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium ''Flammeovirga sp''. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T13:21:42Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10 <sup>-4</sup> M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 101

2024-01-02T13:20:19Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM101.html
|}
</div>


== Ligand specificities ==

[[File:Figure.png|thumb|'''Figure 1. Carbohydrate array assays of WfCBM101. ''' The binding of WfCBM101 to agarose and other galactans in red algae (A), and several other polysaccharides (B) was evaluated. κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Three parallels were conducted for each polysaccharide.''' ]]

The first characterized member in the CBM101 family is WfCBM101 <cite>Mei2023</cite>. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose <cite>Chi2012</cite>. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of WfCBM101 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The in situ visualization of agarose in red alga Gelidium amansii was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e-5). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.

== Family Firsts ==
;First Identified
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium Wenyingzhuangia fucanilytica CZ1127T <cite>Chen2016</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=38010608
#Chi2012 pmid=22526785
#Chen2016 pmid=27220912
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM101]]

File:Figure.png

2024-01-02T13:19:22Z

Xuanwei Mei:

Carbohydrate array assays of WfCBM101

Carbohydrate Binding Module Family 101

2024-01-02T13:16:53Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM101.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM101 family is WfCBM101 <cite>Mei2023</cite>. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose <cite>Chi2012</cite>. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of WfCBM101 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The in situ visualization of agarose in red alga Gelidium amansii was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e-5). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.

== Family Firsts ==
;First Identified
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium Wenyingzhuangia fucanilytica CZ1127T <cite>Chen2016</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=38010608
#Chi2012 pmid=22526785
#Chen2016 pmid=27220912
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM101]]

Carbohydrate Binding Module Family 101

2024-01-02T13:15:37Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM101.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM101 family is WfCBM101 [1]. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose [2]. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of WfCBM101 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The in situ visualization of agarose in red alga Gelidium amansii was realized by utilizing the fluorescent probe [1].
Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e-5). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.

== Family Firsts ==
;First Identified
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium Wenyingzhuangia fucanilytica CZ1127T [3].
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=38010608
#Chi2012 pmid=22526785
#Chen2016 pmid=27220912
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM101]]

File:Figure1.png

2024-01-02T13:03:43Z

Xuanwei Mei: Xuanwei Mei uploaded a new version of File:Figure1.png

Carbohydrate array assay results of FvCBM99.

File:Figure1.png

2024-01-02T13:01:35Z

Xuanwei Mei: Xuanwei Mei uploaded a new version of File:Figure1.png

Carbohydrate array assay results of FvCBM99.

Carbohydrate Binding Module Family 99

2024-01-02T12:55:17Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:54:54Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure . Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:54:25Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:53:11Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1. Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:52:22Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb|'''Figure 1.Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:50:50Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|'''Figure 1.Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:49:40Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb]]'''Figure 1.Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from Ascophyllum nodosum. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:40:49Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:35:50Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:34:18Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==

[[File:Figure1.png|thumb]]

The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:33:31Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.
[[File:Figure1.png|thumb]]
== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

File:Figure1.png

2024-01-02T12:33:17Z

Xuanwei Mei:

Carbohydrate array assay results of FvCBM99.

Carbohydrate Binding Module Family 99

2024-01-02T12:29:13Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 <cite>Liu2015</cite>.
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:26:56Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM99 family is FvCBM99 [1]. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran [2], it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe [1].
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 [3].
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid=37769778
#Chi2012 pmid=22526785
#Liu2015 pmid=25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:25:07Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM99 family is FvCBM99 [1]. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran [2], it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe [1].
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 [3].
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid= 37769778
#Chi2012 pmid= 22526785
#Liu2015 pmid= 25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:24:12Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023.
The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 [3].
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid= 37769778
#Chi2012 pmid= 22526785
#Liu2015 pmid= 25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

Carbohydrate Binding Module Family 99

2024-01-02T12:23:30Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM99.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10-4 M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.

== Structural Features ==
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold.

== Functionalities ==
To evaluate the feasibility of FvCBM99 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The in situ visualization of porphyran in red alga Porphyra haitanensis was realized by utilizing the fluorescent probe <cite>Mei2023.
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran.

== Family Firsts ==
;First Identified
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium Flammeovirga sp. OC4 [3].
;First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2023 pmid= 37769778
#Chi2012 pmid= 22526785
#Liu2015 pmid= 25683442
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM099]]

File:Xuanwei Mei.jpg

2023-04-20T00:40:19Z

Xuanwei Mei: Xuanwei Mei uploaded a new version of File:Xuanwei Mei.jpg

Xuanwei Mei

User:Xuanwei Mei

2023-04-20T00:39:22Z

Xuanwei Mei:

[[File:Xuanwei Mei.jpg|thumb]]
Xuanwei Mei is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. His research focuses on the gene-mining and characterization of carbohydrate-binding modules. So far, he discovered and characterized five CBMs:

*CBM16: ABP_Wf (alginate-binding CBM) [1]
*CBM47: WfCBM47 (sulfated fucan-binding CBM) [2]
*CBM70: SrCBM70 (hyaluronic acid-binding CBM) [3]
*CBM92: Cgk16A-CBM92 (carrageenan-binding CBM; the first member of the CBM92 family) [4]
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [5]

== References ==
<biblio>
#Mei2020 pmid=32747278
#Mei2022a pmid=34893209
#Mei2022b pmid=36395930
#Mei2022c pmid=35830544
#Mei2023 pmid=36924869
</biblio>


[[Category:Contributors|Mei,Xuanwei]]

User:Xuanwei Mei

2023-04-20T00:38:53Z

Xuanwei Mei:

File:Xuanwei Mei.jpg

2023-04-20T00:38:44Z

Xuanwei Mei:

Xuanwei Mei

User:Xuanwei Mei

2023-04-20T00:37:50Z

Xuanwei Mei:

[[Image:Blank_user-200px.png|200px|right]]
Xuanwei Mei is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. His research focuses on the gene-mining and characterization of carbohydrate-binding modules. So far, he discovered and characterized five CBMs:

*CBM16: ABP_Wf (alginate-binding CBM) [1]
*CBM47: WfCBM47 (sulfated fucan-binding CBM) [2]
*CBM70: SrCBM70 (hyaluronic acid-binding CBM) [3]
*CBM92: Cgk16A-CBM92 (carrageenan-binding CBM; the first member of the CBM92 family) [4]
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [5]

== References ==
<biblio>
#Mei2020 pmid=32747278
#Mei2022a pmid=34893209
#Mei2022b pmid=36395930
#Mei2022c pmid=35830544
#Mei2023 pmid=36924869
</biblio>


[[Category:Contributors|Mei,Xuanwei]]

User:Xuanwei Mei

2023-04-20T00:36:37Z

Xuanwei Mei:

[[Image:Blank_user-200px.png|200px|right]]
Xuanwei Mei is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. His research focuses on the gene-mining and characterization of carbohydrate-binding modules. So far, he discovered and characterized five CBMs:

*CBM16: ABP_Wf (alginate-binding CBM)[1]
*CBM47: WfCBM47 (sulfated fucan-binding CBM)[2]
*CBM70: SrCBM70 (hyaluronic acid-binding CBM)[3]
*CBM92: Cgk16A-CBM92 (carrageenan-binding CBM; the first member of the CBM92 family)[4]
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM)[5]

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Mei,Xuanwei]]

User:Xuanwei Mei

2023-04-20T00:35:39Z

Xuanwei Mei:

[[Image:Blank_user-200px.png|200px|right]]
Xuanwei Mei is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. His research focuses on the gene-mining and characterization of carbohydrate-binding modules. So far, he discovered and characterized five CBMs:

CBM16: ABP_Wf (alginate-binding CBM) [1]
CBM47: WfCBM47 (sulfated fucan-binding CBM) [2]
CBM70: SrCBM70 (hyaluronic acid-binding CBM) [3]
CBM92: Cgk16A-CBM92 (carrageenan-binding CBM; the first member of the CBM92 family) [4]
CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [5]

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Mei,Xuanwei]]

Carbohydrate Binding Module Family 92

2023-04-13T06:52:50Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is the Cgk16A-CBM92 from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The Cgk16A-CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. '''The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (viz., Cgk16A-CBM92; 378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids).''' ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:43:11Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is the Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The Cgk16A-CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. '''The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (viz., Cgk16A-CBM92; 378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids).''' ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:40:39Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The Cgk16A-CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. '''The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (viz., Cgk16A-CBM92; 378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids).''' ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

File:Figure 1.png

2023-04-13T06:39:51Z

Xuanwei Mei: Blanked the page

Carbohydrate Binding Module Family 92

2023-04-13T06:36:32Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The Cgk16A-CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. '''The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids).''' ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:13:09Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. '''The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids).''' ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:12:19Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids). ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:11:01Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. ''''''The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids)''''''. ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:05:10Z

Xuanwei Mei: Undo revision 17166 by Xuanwei Mei (talk)

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb|300px|right|'''Figure 1. Domain architecture of the κ-carrageenase Cgk16A. The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids). ]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T06:00:32Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T05:58:09Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
[[File:Figure 1.png|thumb]]

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

File:Figure 1.png

2023-04-13T05:57:52Z

Xuanwei Mei:

Domain architecture of the κ-carrageenase Cgk16A. The enzyme consists of a signal peptide (1-20 amino acids), a GH16 domain (21-347 amino acids), a CBM92 domain (378-490 amino acids) and a C-terminal Sorting domain (516-581 amino acids).

Carbohydrate Binding Module Family 92

2023-04-13T05:56:11Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==

In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]

Carbohydrate Binding Module Family 92

2023-04-13T05:50:12Z

Xuanwei Mei:

{{UnderConstruction}}
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]

* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM92.html
|}
</div>


== Ligand specificities ==
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium ''Wenyingzhuangia aestuarii'' OF219 <cite>Mei2022</cite>. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran <cite>Mei2022</cite>. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans <cite>Mei2022</cite>. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.

== Structural Features ==
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs <cite>Mei2022</cite>, which might be critical for the ligand binding of this CBM.

== Functionalities ==
In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>.

Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., [[GH16]]_17, [[GH5]]_54, [[GH19]], and [[GH95]]. According to the [http://www.cazy.org/CBM92.html CAZy database], these GH families comprise enzymes with various substrate specificities, including κ-carrageenase ([[GH16]]_17), chitinase ([[GH19]]), fucosidase ([[GH95]]), and galactosidase ([[GH95]]). It indicated that functional diversity might be present within the CBM92 family.

== Family Firsts ==
;First Identified: The first characterized CBM92 member <cite>Mei2022</cite> is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite>, which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219.
;First Structural Characterization: No three-dimensional structure has been solved in this CBM family at present.

== References ==
<biblio>
#Mei2022 pmid=35830544
#Shen2018 pmid=29355636
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM092]]