1CYG,1DTU,1QHO,1ITC,1ACZ


Conserved Protein Domain Family
CBM20

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cd05467: CBM20 
Click on image for an interactive view with Cn3D
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
Statistics
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PSSM-Id: 119437
Aligned: 47 rows
Threshold Bit Score: 67.7078
Created: 25-Apr-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
starch-bindingstarch-binding
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:starch-binding site 1 [chemical binding site]
Evidence:
  • Comment:Site 1 is small relative to site 2 and exhibits minimal structural changes upon ligand binding. It acts as an initial starch recognition site.
  • Structure:1ACZ_A; Aspergillus niger glucoamylase CBM20 domain starch binding site 1 binds beta-cyclodextrin; defined at 4A contacts.
    View structure with Cn3D
  • Citation:PMID 9195884
  • Structure:1DTU_A; Bacillus circulans CGTase CBM20 domain starch binding site 1 binds maltopentaose inhibitor; defined at 4A contacts.
    View structure with Cn3D
  • Citation:PMID 8672460

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                    #                                         #         
1CYG_A       581 SVRFVVNnatTNLGQNIYIVGNVYELGNWDtsKAIGpMFNqvv-ysyPTWYIDVSVpe------gKTIEFKFIKKdsq-- 651  Geobacillus st...
1ACZ_A         8 AVTFDLTa-tTTYGENIYLVGSISQLGDWEtsDGIA-LSAdkytssdPLWYVTVTLpa------gESFEYKFIRIesd-- 77   Aspergillus niger
XP_001609560   6 SVHFRCQg-nLDFGRRLAVVGDHPSLGNWDi-NACHeLQRist--vdDVWTSRTPAslp----lkERREYRYVVLndlg- 76   Babesia bovis ...
NP_484213    541 IVRVQLNgvhTQPGETIVVVGDCPELGNWDisKAYP-LEYin----sNTWFAEIPFdes----agKLISYKYAMWreg-- 609  Nostoc sp. PCC...
NP_923319    544 IVRIQVNgfrTQPGEVVAVIGDCPELGDWDlsRAFR-LEYin----dNTWFGEIPFnks----anQIVAYKYVIFren-- 612  Gloeobacter vi...
ZP_01079704  513 IVKFQINnffTRPGERIAVTGDVPELGCWDlhKSAA-LEYin----gDTWFNEIPFdes----vgQPICFKFVVLkega- 582  Synechococcus ...
XP_001310739  11 IVHFHVRv-sTSYGQEVRVCGNIPELGIWDakKAIK-MQFen---nlDFWSADIKLpks---nedRTIEYKYVIVndd-- 80   Trichomonas va...
XP_001025376  43 IVNWQISy-qTNYGERLAIVGNIHELGNWKkeEALN-LQWnn----nNIWNGQIIInlngssnvqKILEYKYILIdekn- 115  Tetrahymena th...
NP_062539      5 QVAFEIRg-tLLPGEVFAICGSCDALGNWNpqNAVA-LLPendtgesMLWKATIVLsr------gVSVQYRYFKGyflep 76   human
YP_213214      2 IVTFHIEy-rTSWGEEVRILGSVPELGKNNpeQAVA-LTTvd----gIHWSNEISIqlp----aeGVVEYSYHIYrdgk- 70   Bacteroides fr...
Feature 1                     ##        #                      
1CYG_A       652 ---------gnvTWESGs-----NHVYt-TPTn----tTGKIIVDW 678  Geobacillus stearothermophilus
1ACZ_A        78 ---------dsvEWESDp-----NREYt-VPQacg-tsTATVTDTW 107  Aspergillus niger
XP_001609560  77 ---------gfvQWHEDs-----IRHV--EPTg----qNMIVEDDY 102  Babesia bovis T2Bo
NP_484213    610 ---------rspLRENIl-----NRRW--VVAke---gTVKWRDTW 636  Nostoc sp. PCC 7120
NP_923319    613 ---------gppINENRt----sRRRF--VPDk----sIAKWRDVW 639  Gloeobacter violaceus PCC 7421
ZP_01079704  583 ---------edpAWEARyenvlhRRFL--LPAs----gRVKLEFDW 613  Synechococcus sp. RS9917
XP_001310739  81 ---------nseQWEPEq-----NHKLv-FGAind-dcVINIEDHF 110  Trichomonas vaginalis G3
XP_001025376 116 ---------qkvQWEEGq-----NRFYyySQIlaesqeKENILFRN 147  Tetrahymena thermophila SB210
NP_062539     77 ktiggpcqvivhKWETHl----qPRSI--TPLe-----SEIIIDDG 111  human
YP_213214     71 --------airtEWNSFp-----RRIY--LPAdv--kkSLRINDCW 99   Bacteroides fragilis NCTC 9343

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