Carbohydrate Binding Module Family 74 - Revision history

Amanda Photenhauer at 00:39, 23 May 2023

2023-05-23T00:39:35Z

Amanda Photenhauer at 00:38, 23 May 2023

2023-05-23T00:38:21Z

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:14:24Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Amanda Photenhauer at 01:36, 10 November 2021

2021-11-10T01:36:50Z

Amanda Photenhauer at 01:36, 10 November 2021

2021-11-10T01:36:21Z

Amanda Photenhauer at 05:44, 7 December 2020

2020-12-07T05:44:02Z

Amanda Photenhauer at 05:42, 7 December 2020

2020-12-07T05:42:33Z

Amanda Photenhauer at 19:17, 23 October 2020

2020-10-23T19:17:41Z

Harry Brumer: Replaced CAZyDBlink template

2020-03-30T21:22:28Z

Replaced CAZyDBlink template

Amanda Photenhauer at 23:52, 29 March 2020

2020-03-29T23:52:19Z

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 :1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.
-::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.
+::In some cases CBM74 is not appended to any GH13 domain. For example, Sas6 from the bacterium ''Ruminococcus bromii'' has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a GH13-containing protein.
 :2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.
-:3. FNIII or Bacterial Ig-like2
+:3. FNIII (FN3) or Bacterial Ig-like2 (BIG2)
 == Family Firsts ==
 ;First Identified

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 :1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.
-::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.
+::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.
 :2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.
 :3. FNIII or Bacterial Ig-like2

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{UnderConstruction}}
-* [[Author]]: ^^^Amanda Photenhauer^^^
+* [[Author]]: [[User:Amanda Photenhauer|Amanda Photenhauer]]
-* [[Responsible Curator]]:  ^^^Nicole Koropatkin^^^
+* [[Responsible Curator]]:  [[User:Nicole Koropatkin|Nicole Koropatkin]]
 ----
 CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis for binding remains unknown.

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 * [[Responsible Curator]]:  ^^^Nicole Koropatkin^^^
 ----
-CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis remains unknown.
+CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis for binding remains unknown.
 <!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 <div style="float:right">

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 * [[Responsible Curator]]:  ^^^Nicole Koropatkin^^^
 ----
+CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis remains unknown.
 <!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 <div style="float:right">
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 == Structural Features ==
-CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined and has not been modeled with high confidence by protein structure prediction tools. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.
+CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.
 == Functionalities ==

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 == Ligand specificities ==
-The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite>
+The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type<cite> Valk2016 </cite>.
 == Structural Features ==
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 == Functionalities ==
-''Content in this section should include, in paragraph form, a description of:''
 * '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed.
 * '''Most Common Associated Modules:'''

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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/CBM74.html
+| colspan="2" |{{CAZyDBlink}}CBM74.html
 |}
 </div>

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 <biblio>
 #Valk2016 pmid=27101946
 </biblio>
 [[Category:Carbohydrate Binding Module Families|CBM074]]