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Conserved domains on  [gi|1586137908|gb|QBJ82337|]
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glycoside hydrolase family 43 protein [Bacillus subtilis subsp. subtilis]

Protein Classification

glycoside hydrolase family 43 protein( domain architecture ID 14406677)

glycoside hydrolase family 43 protein is an inverting enzyme that has an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orientation of the catalytic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
5-303 0e+00

Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


:

Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 624.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGGVWAPCLSYSDGKF 84
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  85 WLIYTDVKVVDGAWKDCHNYLVTCETINGDWSEPITLNSSGFDASLFHDKDGKKYLLNMLWDHRIDRHSFGGIVIQEYSD 164
Cdd:cd09000    81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 KEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSWHDPGNPLQ 244
Cdd:cd09000   161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 245 KCGHASIVQTHTDEWYLAHLTGRPIHPdddsifqqRGYCPLGRETAIQKLYWK-DEWPYV 303
Cdd:cd09000   241 KAGHGSLVETPDGEWYLAHLCGRPLPG--------RGRCPLGRETAIQKVEWTdDGWPRL 292
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
331-531 1.06e-76

Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.


:

Pssm-ID: 436093  Cd Length: 203  Bit Score: 240.25  E-value: 1.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 331 DEFEDSTLNINFQTLRIPFTNELGSLTQAPNHLRLFGHESLTSTFTQAFVARRWQSLHFEAETAVEFYPENFQQAAGLVN 410
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 411 YYNTENWTALQVTHDEELGRILELTICDNFSFSQPL-NNKIVIPREVKYVYLRVNIEKDKYYYFYSFNKEDWHKIDIALE 489
Cdd:pfam17851  82 YYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELaEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPELD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1586137908 490 SKKLSDDYIRGGGfFTGAFVGMQCQDTSGNH-IPADFRYFRYK 531
Cdd:pfam17851 162 ASILSDEYAAGGG-FTGAFVGLYATDNGKGSsGYADFDWFEYE 203
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
5-303 0e+00

Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 624.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGGVWAPCLSYSDGKF 84
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  85 WLIYTDVKVVDGAWKDCHNYLVTCETINGDWSEPITLNSSGFDASLFHDKDGKKYLLNMLWDHRIDRHSFGGIVIQEYSD 164
Cdd:cd09000    81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 KEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSWHDPGNPLQ 244
Cdd:cd09000   161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 245 KCGHASIVQTHTDEWYLAHLTGRPIHPdddsifqqRGYCPLGRETAIQKLYWK-DEWPYV 303
Cdd:cd09000   241 KAGHGSLVETPDGEWYLAHLCGRPLPG--------RGRCPLGRETAIQKVEWTdDGWPRL 292
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
3-301 3.38e-124

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 365.10  E-value: 3.38e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   3 ITNPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSggvWAPCLSYSDG 82
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  83 KFWLIYTDVKvvdgawkdCHNYLVTCETINGDWSEPITL--NSSGFDASLFHDKDGKKYLLNMLWDHridRHSFGGIVIQ 160
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLksGGGGIDPSLFHDDDGKKYLVWGGWDP---RHGHGGIYLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 161 EYSDKEQKLIGKP-KVIFEGTDR---KLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSW 236
Cdd:pfam04616 147 ELDNDGLKLVGPVtKLIYPGTRWvggKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586137908 237 HDPgNPLQKCGHASIVQTHTDEWYLAHLTGRPihpdddsifqQRGYCPLGRETAIQKLYWK-DEWP 301
Cdd:pfam04616 227 SPE-NPIYGPGHASLVETPDGEWWIVYHAGRP----------GDGGYGLGRETRIQPVEWRaDGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
2-347 7.41e-112

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 336.15  E-value: 7.41e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   2 KITNPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLdmkGNPNSGGVWAPCLSYSD 81
Cdd:COG3507    21 TYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  82 GKFWLIYTdvkVVDGAWKDCHNYLVTCETINGDWSEPITL---NSSGFDASLFHDKDGKKYLLNMLWDHridrhsfgGIV 158
Cdd:COG3507    98 GKYYLYYT---AVDGGKNRSGIGVATADDPEGPWSDPGPLvcpGGNGIDPSVFVDDDGKAYLVYGSGGG--------GIY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 159 IQEYSDKEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYE-HAATIARSANIEGPYEVHPDNPILTSWH 237
Cdd:COG3507   167 VAELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTCNSgYAVRVARSKSPTGPYEDAPGNPILTQRS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 238 DpgNPLQKCGHASIVQTHTDEWYLAHLTGRPIHpdddsifqqrgycPLGRETAIQKLYW-KDEWPYVVGGKEgslevdap 316
Cdd:COG3507   247 D--GGIQGPGHGSLVETPDGEWYLVYHAYRPPG-------------GLGRETFLDPVTWnEDGWPVVGPGTG-------- 303
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1586137908 317 sipETIFEATYPEVDEFeDSTLNINFQ--TLRI 347
Cdd:COG3507   304 ---EPPQPLPAPESDDF-DGPLGLQWSlgYLRL 332
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
331-531 1.06e-76

Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.


Pssm-ID: 436093  Cd Length: 203  Bit Score: 240.25  E-value: 1.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 331 DEFEDSTLNINFQTLRIPFTNELGSLTQAPNHLRLFGHESLTSTFTQAFVARRWQSLHFEAETAVEFYPENFQQAAGLVN 410
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 411 YYNTENWTALQVTHDEELGRILELTICDNFSFSQPL-NNKIVIPREVKYVYLRVNIEKDKYYYFYSFNKEDWHKIDIALE 489
Cdd:pfam17851  82 YYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELaEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPELD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1586137908 490 SKKLSDDYIRGGGfFTGAFVGMQCQDTSGNH-IPADFRYFRYK 531
Cdd:pfam17851 162 ASILSDEYAAGGG-FTGAFVGLYATDNGKGSsGYADFDWFEYE 203
Ree1 COG3506
Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function ...
389-532 1.48e-04

Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function unknown];


Pssm-ID: 442729  Cd Length: 195  Bit Score: 42.96  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 389 FEAETAVEF-YPENFQQAaGLVNYYNTENW--TALQVTHDEELGriLELTICDNFS-FSQPlnnkiVIPREVKYVYLRVN 464
Cdd:COG3506    58 FTFEVKVTGdFKELYDQA-GLMVRVDEENWikAGIEYVPDGVPR--LGSVVTNGYSdWSTG-----PVPGDPKSVWLRLS 129
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586137908 465 IEKDKYYYFYSFNKEDWHKIDIAleskKLSDDyirgggffTGAFVGMQCQDTSGNHIPADFRYFRYKE 532
Cdd:COG3506   130 RRGDALRIQYSLDGKTWTLLRLA----PLPPA--------APVKVGLMACSPTGEGFTVRFSDFSLTP 185
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
5-303 0e+00

Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 624.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGGVWAPCLSYSDGKF 84
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  85 WLIYTDVKVVDGAWKDCHNYLVTCETINGDWSEPITLNSSGFDASLFHDKDGKKYLLNMLWDHRIDRHSFGGIVIQEYSD 164
Cdd:cd09000    81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 KEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSWHDPGNPLQ 244
Cdd:cd09000   161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 245 KCGHASIVQTHTDEWYLAHLTGRPIHPdddsifqqRGYCPLGRETAIQKLYWK-DEWPYV 303
Cdd:cd09000   241 KAGHGSLVETPDGEWYLAHLCGRPLPG--------RGRCPLGRETAIQKVEWTdDGWPRL 292
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
5-297 2.26e-156

Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350103 [Multi-domain]  Cd Length: 272  Bit Score: 446.81  E-value: 2.26e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGGVWAPCLSYSDGKF 84
Cdd:cd08989     1 NPVLPGFHPDPSVVRVGDDYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQLDLTGGPDGGGIWAPDISYHDGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  85 WLIYTDVKVVdGAWKDCHNYLVTCETINGDWSEPITLNSSGFDASLFHDKDGKKYLLNMLwdhridrhsfGGIVIQEYSD 164
Cdd:cd08989    81 YIYYTVVLNV-GSWKGRRNYLVTSEDPEGPWSEPVWLDEGGIDPSLFVDDDGKHYMLLNP----------GGIRLAELNP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 KEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTsWHDPGNPLQ 244
Cdd:cd08989   150 DCTKQIGEPKRIWEGTGGRAPEGPHLYKKDGYYYLLTAEGGTGYGHAITIARSKTIYGPYEPCPYNPILR-QQDPQAPLQ 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1586137908 245 KCGHASIVQTHTDEWYLAHLTGRPIHPdddsifqqrGYCPLGRETAIQKLYWK 297
Cdd:cd08989   229 RCGHGKLVETPDGEWWMVYLCGRPLPG---------GYCPLGRETALAPVEWT 272
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
3-301 3.38e-124

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 365.10  E-value: 3.38e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   3 ITNPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSggvWAPCLSYSDG 82
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  83 KFWLIYTDVKvvdgawkdCHNYLVTCETINGDWSEPITL--NSSGFDASLFHDKDGKKYLLNMLWDHridRHSFGGIVIQ 160
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLksGGGGIDPSLFHDDDGKKYLVWGGWDP---RHGHGGIYLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 161 EYSDKEQKLIGKP-KVIFEGTDR---KLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSW 236
Cdd:pfam04616 147 ELDNDGLKLVGPVtKLIYPGTRWvggKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586137908 237 HDPgNPLQKCGHASIVQTHTDEWYLAHLTGRPihpdddsifqQRGYCPLGRETAIQKLYWK-DEWP 301
Cdd:pfam04616 227 SPE-NPIYGPGHASLVETPDGEWWIVYHAGRP----------GDGGYGLGRETRIQPVEWRaDGWP 281
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
5-303 2.34e-120

Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350129 [Multi-domain]  Cd Length: 285  Bit Score: 355.28  E-value: 2.34e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGGVWAPCLSYSDGKF 84
Cdd:cd18617     1 NPILPGFYPDPSICRVGDDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQLDLRGVPSSGGIFAPTIRYHDGRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  85 WLIYTDvkVVDGAWKdchNYLVTCETINGDWSEPITLNSSGFDASLFHDKDGKKYLLNMLWDHRIDRHSfGGIVIQEYSD 164
Cdd:cd18617    81 YIITTN--VSTDGRG---NFIVTADDPAGPWSDPVWLDGPGIDPSLFFDDDGKVYLTGTGPPPDPYEGH-GGIWQQEIDL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 KEQKLIGKPKVIFE-GTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSWHDPGNPL 243
Cdd:cd18617   155 ETGKLLGEPKVLWNgGTGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGPYEPCPNNPILTHRHLGSNPV 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 244 QKCGHASIVQTHTDEWYLAHLTGRPihpdddsifQQRGYCPLGRETAIQKLYWKDEWPYV 303
Cdd:cd18617   235 QNTGHADLVEDPDGSWWAVFLGVRP---------YGGGFHNLGRETFLAPVEWEDGWPVV 285
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
2-347 7.41e-112

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 336.15  E-value: 7.41e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   2 KITNPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLdmkGNPNSGGVWAPCLSYSD 81
Cdd:COG3507    21 TYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  82 GKFWLIYTdvkVVDGAWKDCHNYLVTCETINGDWSEPITL---NSSGFDASLFHDKDGKKYLLNMLWDHridrhsfgGIV 158
Cdd:COG3507    98 GKYYLYYT---AVDGGKNRSGIGVATADDPEGPWSDPGPLvcpGGNGIDPSVFVDDDGKAYLVYGSGGG--------GIY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 159 IQEYSDKEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYE-HAATIARSANIEGPYEVHPDNPILTSWH 237
Cdd:COG3507   167 VAELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTCNSgYAVRVARSKSPTGPYEDAPGNPILTQRS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 238 DpgNPLQKCGHASIVQTHTDEWYLAHLTGRPIHpdddsifqqrgycPLGRETAIQKLYW-KDEWPYVVGGKEgslevdap 316
Cdd:COG3507   247 D--GGIQGPGHGSLVETPDGEWYLVYHAYRPPG-------------GLGRETFLDPVTWnEDGWPVVGPGTG-------- 303
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1586137908 317 sipETIFEATYPEVDEFeDSTLNINFQ--TLRI 347
Cdd:COG3507   304 ---EPPQPLPAPESDDF-DGPLGLQWSlgYLRL 332
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
331-531 1.06e-76

Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.


Pssm-ID: 436093  Cd Length: 203  Bit Score: 240.25  E-value: 1.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 331 DEFEDSTLNINFQTLRIPFTNELGSLTQAPNHLRLFGHESLTSTFTQAFVARRWQSLHFEAETAVEFYPENFQQAAGLVN 410
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 411 YYNTENWTALQVTHDEELGRILELTICDNFSFSQPL-NNKIVIPREVKYVYLRVNIEKDKYYYFYSFNKEDWHKIDIALE 489
Cdd:pfam17851  82 YYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELaEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPELD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1586137908 490 SKKLSDDYIRGGGfFTGAFVGMQCQDTSGNH-IPADFRYFRYK 531
Cdd:pfam17851 162 ASILSDEYAAGGG-FTGAFVGLYATDNGKGSsGYADFDWFEYE 203
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
5-301 1.27e-72

Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl); This glycosyl hydrolase family 43 (GH43) subgroup includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a characterized bifunctional enzyme with beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) activities. This subgroup belongs to the GH43_XybB subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_XybB subgroup includes enzymes having beta-1,4-xylosidase and alpha-L-arabinofuranosidase activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43_XybB subgroup includes Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350154  Cd Length: 292  Bit Score: 232.91  E-value: 1.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGED---YYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMK---GNPNSGGVWAPCLS 78
Cdd:cd18833     1 NPIIPGFHPDPSCIFVPEWdgtFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSQLPELattGTGQQGGIWAPTLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  79 YSDGKFWLIYTDVKVVDGAWKDCHNYLVTCETI--NGDWSEPITLNSSGFDASLFHDKDGKKYLLnMLWDHRidrhSFGG 156
Cdd:cd18833    81 YHDGTFYVITTLVFPDKTDASRWDNLLFTTTDPysDSAWSDPIRFDFPGYDPDLFWDDDGTAYVQ-GAHYWR----VRPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 157 IVIQEYSDKEQKLIGkPKVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSw 236
Cdd:cd18833   156 IQQQEIDLKTGESLS-PSPIWNGTGGSAPEGPHMYKKDGWYYLLIAEGGTGLGHSVTIARSRSIWGPYESYPSNPVLTN- 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586137908 237 HDPGNPLQKCGHASIVQTHTDEWYLAHLTGRPIHPDDDSifqqrgycPLGRETAIQKLYW-KDEWP 301
Cdd:cd18833   234 ANTSEYFQTVGHADLFQDANGNWWGVALATRSGPEYEIY--------PMGRETVLYPVTWeEGEWP 291
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
13-265 1.02e-70

Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350092 [Multi-domain]  Cd Length: 251  Bit Score: 226.55  E-value: 1.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  13 PDPSICRVGEDYYIAVSTFEW--FPGVQIHHSKDLVNWHLVAHPLQRvsqlDMKGNPNSGGVWAPCLSYS-DGKFWLIYT 89
Cdd:cd08978     1 ADPSILKDNGRYYIYATTDDTgtGTGIVVWKSKDLVNWKEEGTVLSR----GKSKSWGTGNLWAPEVYYFnSGKWYLYYS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  90 DVKvvdgAWKDCHNYLVTCETINGDWSEP-----ITLNSSGFDASLFHDKDGKKYLLNMLWDHridrhsFGGIVIQEYSD 164
Cdd:cd08978    77 AVP----NGGGGRIYVATSDSPEGPFTPIvsgklGDRGSGSIDPTVFVDDDGKLYLYYGDEDD------SGDIYVAELDP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 KEQKLIGKPK-----VIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAATIARSANIEGPYEVHPDNPILtsWHDP 239
Cdd:cd08978   147 DLLTIKGDVTlligeVVGSGFRGNYFEGPAVFKRNGYYYLIYSAGGTDGGYAIGYATSDSPLGPWEKASHNPGL--QTSG 224
                         250       260
                  ....*....|....*....|....*.
gi 1586137908 240 GNPLQKCGHASIVQTHTDEWYLAHLT 265
Cdd:cd08978   225 ATGIYGPGHGSIFQDEGDRWYIVYHA 250
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
4-303 7.04e-61

Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase; This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350115 [Multi-domain]  Cd Length: 270  Bit Score: 201.59  E-value: 7.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   4 TNPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDM-----KGNPNSGGVWAPCLS 78
Cdd:cd09001     3 TNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAyyledGKNAYGKGIWAPSLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  79 YSDGKFWLIYTDvkvVDGAWkdchnYLVTCETINGDWSEPITLNSSGFDASLFHDKDGKKYLLnmlwdhridrHSFGGIV 158
Cdd:cd09001    83 YHNGKFYVYFCT---NTGGT-----YVYTADDPAGPWSRPALIGKGYHDPSLLFDDDGKAYLV----------YGNGEIR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 159 IQEYSDKEQKLIGKPKVIFEGTDRKLT-EAPHLYHIGNYYYLLTAEGG--TRYEhaaTIARSANIEGPYEVHpdnPILts 235
Cdd:cd09001   145 LTELSPDGTGVGGEGRVIIDGTEEGLGaEGSHLYKINGYYYIFNIEWGggGRTQ---VVLRSKSLYGPYEGR---VVL-- 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586137908 236 wHDPGNPLQKCGH-ASIVQTHTDEWYLAHltgrpihpdddsiFQQRGycPLGRETAIQKLYWKDEWPYV 303
Cdd:cd09001   217 -DDGSGTGDNGPHqGGLVDTPDGEWWFML-------------FQDRG--AVGRIPVLVPVTWKDGWPVI 269
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
4-303 5.36e-52

Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350116 [Multi-domain]  Cd Length: 271  Bit Score: 178.19  E-value: 5.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   4 TNPVLKGFNPDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVsqldmkgnpnSGGVWAPCLSYSDGK 83
Cdd:cd09002     2 LNPILAGDYPDPSILRDGDDYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAALTEY----------IGTVWAPDLIKHDGR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  84 FWlIYtdvkvvdGAWKDCHNYLVTCETINGDWSEPITLN-SSGFDASLFHDKDGKKYLLnmlwdhridrhsFGGIVIQEY 162
Cdd:cd09002    72 YY-IY-------FPAKGGTNYVITADDIAGPWSEPIDLKvGSGIDPGHVVDEDGKRYLF------------LSGGRRVRL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 163 SDKEQKLIGKPKVIFEG--------TDRKLTEAPHLYHIGNYYYLLTAEGGTR---YEHAATIARSANIEGPYEVHPDNP 231
Cdd:cd09002   132 TDDGLSVAGPPEKVYDGwrypdewdVECFCLEGPKLFRRGGYYYLTTAQGGTAgppTSHMVVSARSKSPHGPWENSPYNP 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586137908 232 ILTSWhDPGNPLQKCGHASIVQTHTDEWYLahltgrpihpdddsIFQ--QRGYCPLGRETAIQKLYW-KDEWPYV 303
Cdd:cd09002   212 LVRTQ-SREEKWWSKGHGTLVEGPDGKWWM--------------VYHgyENGYRTLGRQTLLEPVEWtADGWFRI 271
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
5-302 9.05e-33

Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350113 [Multi-domain]  Cd Length: 284  Bit Score: 126.49  E-value: 9.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYiAVSTFEWFPGVQIHHSKDLVNWHLVAH-PLQRVSqldmKGNPNSGGVWAPCLSY-SDG 82
Cdd:cd08999     1 NPVIDGDFPDPSVIRVGGTYY-AFATNSGGKNVQVATSTDLVTWTLLGGdALPDLP----AWAAAGGNTWAPDVVRrPDG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  83 KFWLIYTdvkvvdgAWKDCHNYLV----TCETING---DWSEPITLNSSGF---DASLFHDKDGKKYLLnmlWdhRIDRH 152
Cdd:cd08999    76 KYVMYYS-------ARLKSSGKHCigvaTSDSPLGpftPVGEPPLCPLDQGgaiDPSGFVDPDGKRYLV---Y--KVDGN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 153 SFGG---IVIQEYSDKEQKLIGKPKVIFEGT---DRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAAT-IARSANIEGPYE 225
Cdd:cd08999   144 SIGVptpIMLQELSADGLTLVGEPVELLLNDgpwDGPLVEAPSLVKRDGTYYLFYSSNCYCSPSYAVgYATSKSITGPYT 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 226 VHPDNPILTSwhdpGNPLQKCGHASIVQTHTDEWYLAHltgrpihpdddsifqqrGYCP-----LGRETAIQKLYWKDEW 300
Cdd:cd08999   224 KAGEPLLLTG----DGGLTGPGGADVVEDDGGDWMVFH-----------------AWDGgddvgGGRAMYTAELTWEGGW 282

                  ..
gi 1586137908 301 PY 302
Cdd:cd08999   283 PV 284
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
13-305 5.89e-20

Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350105 [Multi-domain]  Cd Length: 283  Bit Score: 89.93  E-value: 5.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  13 PDPSICRVGEDYYIAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVsqldmkGNPNSGGVWAPCLSYSDGKFWLIYTdvk 92
Cdd:cd08991     1 ADPFVLKHNGTYYLYGTGGDDGRGFKVYVSDDLVNWEYPGGALEEP------GLWGTKGFWAPEVFYYNGKFYMYYS--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  93 vVDGAWKDCHNYLVTCETING--DWSEPITLNSSGF--DASLFHDKDGKKYLLNMLWDHriDRHSFGGIVIQEYSDkEQK 168
Cdd:cd08991    72 -ANGGDHGEHIAVAVSDSPLGpfRDKGKLLIPAGGFsiDAHVFIDDDGKWYLYYVRDDL--GGEPGNRIYVAELED-DLS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 169 LIGKPKVIF-----------EGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYEHAAT-IARSANIEGPYEVHPDNPILTSw 236
Cdd:cd08991   148 LIGEPTLVLcptaderweygEGRDWHTTEGPTVLKHNGTYYLTYSANHFRSPDYAVgYATADSPLGPWTKYEGNPILSR- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586137908 237 hdPGNPLQKCGHASIVQTHTDEWYLAHLTgrpiHPDDDSIFQqrgycplgRETAIQKLYWKDEWPYVVG 305
Cdd:cd08991   227 --NDGGVNGPGHNSVFKDPDGDLYIVYHT----HDSDETVEP--------RKMRIDRLRFDGDKLSVLG 281
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
14-299 2.75e-19

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350118 [Multi-domain]  Cd Length: 266  Bit Score: 87.67  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVST--FEWFPGVQIH--HSKDLVNW--HLVAHPLQRVSQldmkgnPNSGGVWAPCLSYSDGKFWLI 87
Cdd:cd09004     2 DPDIVVFGGRYYIYPTTdgPPGWSSTSFHvfSSTDLVNWtdHGIILDLANDVW------WANKGAWAPAVAERNGKYYFY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  88 YT-----DVKVVD---GAWKDCHNYLVTCETINGdwsEPItlnssgfDASLFHDKDGKKYLLnmlwdhridrhsFGG--I 157
Cdd:cd09004    76 FSagsqiGVAVSDsptGPFTDLGRPLVTGGDYGG---QAI-------DPMVFVDDDGQAYLY------------WGNgtA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 158 VIQEYSDKEQKLIGKPKVIFEGTDrkLTEAPHLYHIGNYYYLLTAEGGTRYE----HAATiarSANIEGPYEVHPDNPIL 233
Cdd:cd09004   134 YVARLNDDMVSFDGEVVVSITPPN--FREGPFVHKRNGIYYLSWSENDTRDPdyrvRYAT---SDSPLGPWTYRGVGLLL 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586137908 234 tswhDPGNPLQKCGHASIVQT-HTDEWYLA-HLTGRPiHPDDDSifqqrgycplgRETAIQKLYWKDE 299
Cdd:cd09004   209 ----DSAGGIKGTGHHSIVQVpGTDEWYIAyHRFAVP-GGDGYH-----------REVAIDRLEFDAD 260
GH43_F5-8_typeC-like cd18608
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ...
14-264 5.25e-19

Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 domain; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), xylanase (EC 3.2.1.8), and beta-galactosidase (EC 3.2.1.145) activities, and some as F5/8 type C domain (also known as the discoidin (DS) domain)-containing proteins. Most contain a F5/8 type C domain C-terminal to the GH43 domain. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350120 [Multi-domain]  Cd Length: 276  Bit Score: 86.95  E-value: 5.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVSTFEWFPGV----QIHHSKDLVNWHL--VAHPLQRVSQLDMkgnpnsggVWAPCLSY-SDGKFWL 86
Cdd:cd18608     3 DPSIVKFGGTYYLYATTDGWGGFNsgepVVWKSKDFVNWKFegLNWPTKAASGDSK--------VWAPSVVKgKDGKYYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  87 IYTD-----VKVVD---GAWKDchnylvtcetINGDWSEPITLNSS----GFDASLFHDKDGKKYllnMLWdhRIDRHSF 154
Cdd:cd18608    75 YVSVgseiyVGVADsplGPWKN----------ANGDGPPIIPGDGKpnyhMIDAEPFIDDDGKAY---LYW--GSGLHVN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 155 GGIVIQEYSDKEQKLIGKpkVIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGTRYE----HAATiarSANIEGPYEVHPDN 230
Cdd:cd18608   140 GHCFAAKLNPDMVTFDGS--EPTIVTPRDYFEAPFMFKRNGIYYLMYSGGGCWDEtynvRYAV---SDNPLGPFEEGENS 214
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1586137908 231 PILTSwhDPGNPLQKCGHASIVQtHTDEWYLAHL 264
Cdd:cd18608   215 PILQT--DEAKGIFGPGHHSVFE-EGGQYYILYH 245
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
14-263 1.02e-18

Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350112 [Multi-domain]  Cd Length: 278  Bit Score: 86.45  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVSTFewfPGVQIHHSKDLVNWHLVAHPL-QRVSQLDMKGNPNSGGVWAPCLSYSDGKFWLIY---- 88
Cdd:cd08998     3 DPSIIKDDGGTYYVFSTG---AGIQIRTSKDLVNWEFVGTVFpEGPAWAAAEVPGGAGGLWAPDVVYVNGRYYLYYsast 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  89 -----------TDVKVVDGAWKDcHNyLVTCETINGDWSePItlnssgfDASLFHDKDGKKYLlnmlwdhridrhSFG-- 155
Cdd:cd08998    80 fgsnrsaiglaTSTTLDDGPWTD-QG-LVVSSSPGDDYN-AI-------DPNVFVDADGRLWL------------AYGsf 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 156 --GIVIQEYSDKEqkliGKPKVIFEGTD--RKLT-----EAPHLYHIGNYYYLLTAEG------GTRYEhaATIARSANI 220
Cdd:cd08998   138 wgGIKLVELDPAT----GKLRPGSTGTSiaSRPGgpgaiEAPYIIYRGGYYYLFVSYGsccrgaNSTYN--IRVGRSTSI 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1586137908 221 EGPYEvhpDN-----------PILTS---WHDPgnplqkcGHASIVQTHtDEWYLAH 263
Cdd:cd08998   212 TGPYV---DRngvdmlegggtLLLGGhgrWIGP-------GHNSVFRDG-DGDYLVY 257
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
5-235 2.71e-18

Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350128 [Multi-domain]  Cd Length: 291  Bit Score: 85.32  E-value: 2.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGFNPDPSICRVGEDYYIAVSTFE-WFPG-----VQIHHSKDLVNWHLVA-------HPLqrvsqldmkgNPNSGG 71
Cdd:cd18616     1 NPVFEPTFADPTVIRGDDGYFYAYATEDpWGDGggfrlVPILRSKDLVNWEYVGdaftskpRWK----------WDPGGG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  72 VWAPCLSYSDGKFWLIYTDVKVV---------------DGAWKDcHNYLVTCETINGDWSepitlnssgFDASLFHDkDG 136
Cdd:cd18616    71 LWAPDIRYIDGKYVLYYSLSDWGadpnpgigvatadspAGPFTD-QGKLFDSNEIGVRNS---------IDPFVFED-DG 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 137 KKYllnMLWDhridrhSFGGIVIQEYSDKEQKLIGKPKVIFEGTDRkltEAPHLYHIGNYYYLLTAEGG------TRYEh 210
Cdd:cd18616   140 KKY---LFWG------SFYGIYAVELTADGLALKPGEKVQIAGDRY---EGPYIVKRDGYYYLFGSAGSccegpnSTYR- 206
                         250       260
                  ....*....|....*....|....*
gi 1586137908 211 aATIARSANIEGPYEVHPDNPILTS 235
Cdd:cd18616   207 -VVVGRSESLLGPYVDRDGRSLLDS 230
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
14-224 4.03e-16

Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350100 [Multi-domain]  Cd Length: 257  Bit Score: 78.42  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVST----FEWFP--GVQIHHSKDLVNWHLVAHP----------LQRVSQLDMKGNPnsGGVWAPCL 77
Cdd:cd08986     4 DPYITLGPDGYYYLTGTtggpDWWGVndGIRLWRSKDLKDWEYLGLVwdlekdgwwqWEPQWWTPDSKNK--RALWAPEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  78 SYSDGKFWLIYTdvkVVDGawkdCHNYLV-TCETINGDWSEPITLN-SSGFDASLFHDKDGKKYLLnmlwdhridrhsFG 155
Cdd:cd08986    82 HYINGTWYITHS---MNGG----GTGLLKsTTGKPEGPYVDPMGGPlGKGIDPSLFEDDDGTVYLV------------WG 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586137908 156 GIVIQEYSDKEQKLIGKPKVIFEGTDRKL-TEAPHLYHIGNYYYLLTAEGGTRYEHAAT----IARSANIEGPY 224
Cdd:cd08986   143 NGQIARLKKDMSGFAEEPRKIDPSGNREIgHEGAFIFKIGGKYVLFGAAWSTDKMRKGTydlyYATSDSIYGPY 216
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
13-224 1.30e-14

Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350102 [Multi-domain]  Cd Length: 277  Bit Score: 74.09  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  13 PDPSICRVGEDYYiAVSTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGG-VWAPCLSYSDGKFWLIYTdv 91
Cdd:cd08988     1 HDPSIIKEGGTYY-AFGTGTDGFGIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGnLWAPDISQHKGKYYLYYS-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  92 kVVD-GAWKDCHNyLVTCETINGDW--SEPITLNSSG------FDASLFHDKDGKKYLLNMLWdhridrhsFGGIVIQEY 162
Cdd:cd08988    78 -VSDnGSNTSAIG-LATANNPQGPFkdEGPAKPVVTSdnagnaIDPDLFQDEDGQNWLLYGSF--------WGGIWLQKL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586137908 163 sDKEQKLIGKPKVIFEGTDRKLT--EAPHLYHIGNYYYLLTAEG----GTRYEHAATIARSANIEGPY 224
Cdd:cd08988   148 -DKNGLVVNPPGNGKSIAVLYYVsiEAPYITYAGGYYYLFVSAGsccdGGNSTYHTRVGRSKKVTGPY 214
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
14-295 1.34e-10

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675); This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350149 [Multi-domain]  Cd Length: 283  Bit Score: 62.29  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVST--FEWFPGVQIH--HSKDLVNWHLVAHPLQRVSQLDMKGNPnsGGVWAPCLSYSDGKFWLIY- 88
Cdd:cd18828     2 DPDIAYFDGKYYIYPTTdgFPGWSGTQFHvfSSDDLVTWKDEGVILDLKNDQVVPWAT--GNAWAPTIEERDGKYYFYFc 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  89 ---------TDVKVVD---GAWKDCHNYLVTCETINGDWSEPItlnssgfDASLFHD-KDGKKYLlnmLWDHridrhsfG 155
Cdd:cd18828    80 gknpdgrsqIGVAVADsptGPFTAQGSPLITHEMARVTMGQAI-------DPSVFTDpVDGKYYL---YWGN-------G 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 156 GIVIQEYSDKEQKLIGKPKVIFEGtDRKLTEAPHLYHIGNYYYLLTAEGGTRYE--HAAtIARSANIEGPYEVHpdNPIL 233
Cdd:cd18828   143 YAAIAELNDDMISIKPGTLVNLDG-LTDFREAVTVLYRDGLYHFTWSCDDTGSEnyHVN-YGTSDSPYGPITYR--GVIL 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586137908 234 TSwhDPGNPLQKCGHASIVQ-THTDEWYLA-HLTGRPIHPDDDSifqqRGYcplGRETAIQKLY 295
Cdd:cd18828   219 QK--DPSKGILGTGHHSILQvPGTDEWYIAyHRFATPLGIYGSG----LGY---HRETCIDRLT 273
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
42-298 1.94e-10

Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase; This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350104 [Multi-domain]  Cd Length: 269  Bit Score: 61.46  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  42 SKDLVNWHLVAHPLQrvsqLDMKGNPNSGGVWAPCLSYSDGKFWLIY----------TDVKVVD---GAWKDCHNYLVTC 108
Cdd:cd08990    37 STDLVNWTDHGEILP----PDDVFWWASGNAWAPDAVYKNGKYYFYFpvgqasdgfgIGVAVSDspaGPFKDALGKPLIP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 109 ETINGDWsepitlnssGFDASLFHDKDGKKYllnMLWdhridrHSFGGIVIQEYSDKEQKLIGKPKVIFEGTDRKLTEAP 188
Cdd:cd08990   113 EGLNGIE---------GIDPAVFVDDDGRAY---LYF------GGGGGYYVAKLKDDMISLAGEPQKIKNGGLKGFFEAP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 189 HLYHIGNYYYLLTAEGGTRYEHAATiARSANIEGPYE----VHPDNPILTSwhdpgnplqkcgHASIVQTHtDEWYLAHL 264
Cdd:cd08990   175 WVFKRNGTYYLSYAGGWAYPAEIAY-STADSPLGPYTyrgvILDPVGSGTN------------HGSIVEFK-GQWYLFYH 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1586137908 265 TGrpihpDDDSIFQQRgycplgRETAIQKLYWKD 298
Cdd:cd08990   241 TA-----DLSGGGDFR------RSVCIDYLHYNA 263
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
14-225 9.58e-10

Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated as having endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase (AbnA;BSU28810) (Arb43A). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the arabinofuranosidase (ABF; EC 3.2.1.55) enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350150 [Multi-domain]  Cd Length: 273  Bit Score: 59.68  E-value: 9.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYiavsTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGG--VWAPCLSYSDGKFWLIY--- 88
Cdd:cd18829     3 DPSIIKEGSTWW----TFSTGDGIPVKYSSDGLNWTQGPPIFGSPLSWWKTYVPANTTndVWAPDVHYYNGKYWLYYais 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  89 ---TDVKVVDgawkdchnyLVTCETI-NGDWSEP---ITLNSS----GFDASLFHDKDGKKYLlnmlwdhridrhSFG-- 155
Cdd:cd18829    79 tfgSNTSAIG---------LASASSIaAGNWTDEglvLRSTSAdnynAIDPNLVIDASGNPWL------------VFGsf 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586137908 156 --GIVIQEYSDKEQKLIGKPKVIFEGTDRKLtEAPHLYHIGNYYYLLTAEG----GTRYEHAATIARSANIEGPYE 225
Cdd:cd18829   138 wsGIKITRLDKATMKPTGSIYSIASRPSGGI-EGPFIVYRDGYYYLFVSIDkccrGVNSTYKIAYGRSTSITGPYL 212
GH43_AnAbnA-like cd18831
Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); ...
14-224 2.66e-08

Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities such as Aspergillus niger AbnA, Aspergillus niveus AbnA, and Chrysosporium lucknowense Abn1. It belongs to the GH43_Arb43a subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_Arb43a subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. The GH43_Arb43a subgroup includes many enzymes such as Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, and are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350152 [Multi-domain]  Cd Length: 286  Bit Score: 55.29  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVSTFewfPGVQIHHSKDLVN-WHLVAHPLQRVSQLDMKGNPNsggVWAPCLSYSDGKFWLIY---- 88
Cdd:cd18831     3 DPSIIRREDGTYFRFSTG---GGIRIATAPSLTGpWTYVGSVLPGGSSIDLAGNDD---LWAPDVHYVNGTYYCYYsvst 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  89 -----------TDVKVVDGAWKDcHNYLVTceTINGDwsepitlNSSGFDASLFHDKDGKKYLlnmlwdhridrhSFG-- 155
Cdd:cd18831    77 fgsqdsaigvaTSPTMEPGSWTD-HGAVIR--SSSGD-------PYNAIDPNLIVDDDGTPYL------------TFGsy 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 156 --GIVIQEYSDKEQKLIGKPK---VIFEGTDRKLTEAPHLYHIGNYYYLLTAEGGT-RY---------EHAATIARSANI 220
Cdd:cd18831   135 wqGIFQVPLTDPLLSPAAGPPpthLAYNPSGNHPEEGSFMYKHGGYYYLFFSSGICcGYdpslpapgeEYKIRVCRSTSP 214

                  ....
gi 1586137908 221 EGPY 224
Cdd:cd18831   215 TGPF 218
GH43_GsAbnA-like cd18832
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ...
14-238 9.15e-08

Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350153 [Multi-domain]  Cd Length: 332  Bit Score: 54.18  E-value: 9.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVStfewfpgvqihH-----SKDLVNWhlvahplQRVSQLDMKGNPN-------------------- 68
Cdd:cd18832     3 DPSIVKDDGTYYVFGS-----------HlaaakSTDLMNW-------TQFTNGVTTDNPLlfnlfdstawelaedfnwag 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  69 SGGVWAPCLSY--SDGKfWLIYTDVkvvdgawkdCHNY------LVTCETINGDWSEPITLNSSGF-------------- 126
Cdd:cd18832    65 GGNLWAPDVIYnkAMGK-YCMYYSV---------SGDDspsaigLATADNIEGPYTYKGTVLKSGFtgstsadadvyltg 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 127 ------------DASLFHDKDGKKYLLNMLWdhridrhsFGGIVIQE---------YSDKEQKLIGKP----KVIfeGTD 181
Cdd:cd18832   135 gkynnnyhpnaiDPCVFYDKDGKLWMVYGSW--------SGGIFLLEldpktglrdYSVETDGNLPDQyygkKIA--GGY 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586137908 182 RKLTEAPHLYHIGN--YYYL------LTAEGG--TRyehaatIARSANIEGPY-EVHPDNPILTSWHD 238
Cdd:cd18832   205 HASGEGPYILYDKDtgYYYLfvsyggLDANGGynIR------VFRSKNPDGPYvDAAGNDAIYTSGND 266
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
19-201 1.19e-07

Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350143  Cd Length: 266  Bit Score: 53.01  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  19 RVGEDYYiavsTFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNpnSGGVWAPCLSY--SDGKFwliytdvkVVDG 96
Cdd:cd18822    17 WYGENRD----NNNGFNGVSLYSSTDLVNWEFRNTVLTRDTCSASELA--SCKIERPKVIYnpKTGKF--------VMWA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  97 AWKDCHNY------LVTCETINGDWS-----EPITLNSsgFDASLFHDKDGKKYLL---NMLWDHRIDRHSfggiviQEY 162
Cdd:cd18822    83 HWENGKDYglaraaVATSDTPDGDYTfhgsfRPLGYDS--RDMTLFVDDDGTAYLIsaaNDNADLNIYRLT------PDY 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1586137908 163 SDKEQKLigkpKVIFEGTDRkltEAPHLYHIGNYYYLLT 201
Cdd:cd18822   155 LSVDSLV----ATLFKGQHR---EAPALVKRNGYYYLFT 186
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
42-299 5.63e-07

Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350148 [Multi-domain]  Cd Length: 277  Bit Score: 51.12  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  42 SKDLVNWHLVAHPLqrvsqlDMKGNPNSG-GVWAPCLSYSDGKFWLIYT-------------DVKVVD---GAWKDCHNY 104
Cdd:cd18827    33 SPDLVHWTKHERIL------DMADVPWANrAVWAPSVIEKNGKYYLYFAandiqsddegggiGVAVADrpeGPFKDALGK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 105 LVTCETINGdwSEPItlnssgfDASLFHDKDGKKYLLNMLWDH----RI--DRHSFGGiviqeYSDKEQKLIGKPKvife 178
Cdd:cd18827   107 PLIGEFHNG--AQPI-------DQHVFKDDDGQAYLYYGGWGHcnvaKLndDMTSLVP-----FDDGETFKEITPE---- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 179 gtdrKLTEAPHLYHIGNYYYLLTAEGG-TRYEHAATIARSANIEGPYE-----VHPDNPILTSwhdpgnplqkCGHASIV 252
Cdd:cd18827   169 ----GYVEGPFMFKRNGKYYFMWSEGGwTGPDYSVAYAVADSPLGPFKrigkiLQQDPAIATG----------AGHHSVV 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1586137908 253 QT-HTDEWYLA-HLtgRPIHPDDdsifqqrgycPLGRETAIQKLYWKDE 299
Cdd:cd18827   235 NVpGTDDWYIVyHR--RPLGETD----------GNHRVVCIDRMEFNED 271
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
14-264 1.02e-05

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350091 [Multi-domain]  Cd Length: 257  Bit Score: 47.21  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVSTFEWFPGVQIHH--SKDLVNWHLVAHPLQRVSqldmKGNPNSGGVWAPCLSYSDGKFWLIYTDV 91
Cdd:cd08772     2 DPSVVPYNGEYHLFFTIGPKNTRPFLGHarSKDLIHWEEEPPAIVARG----GGSYDTSYAFDPEVVYIEGTYYLTYCSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  92 KVVDGAWKDCHNYLVTCETINGDW----------SEPITLNSSgfDASLFHDKDGKKYLLNMLWDHRIDRhsFGGIVIQE 161
Cdd:cd08772    78 DLGDILRHGQHIGVAYSKDPKGPWtrkdapliepPNAYSPKNR--DPVLFPRKIGKYYLLNVPSDNGHTR--FGKIAIAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 162 ySDKEQKLIGKPKVIFEGTDRKLTEAPHLYHIGNYYYL-LTAEGGTRYEHAATIARSANIEGPYEVHPDNPILTSWHDPG 240
Cdd:cd08772   154 -SPD*LHWINHSFVYNYNEQGKVGEGPSLWKTKGGWYLiYHANTLTGYGYGFGYALGDLDDPSKVLYRSRPEEEYETVGF 232
                         250       260
                  ....*....|....*....|....
gi 1586137908 241 NPLQKCGHASIVQTHTDEWYLAHL 264
Cdd:cd08772   233 KPNVVAPAAFLCDSTGIVAIIGHA 256
GH43-like cd08982
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
14-253 1.10e-05

Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350096 [Multi-domain]  Cd Length: 308  Bit Score: 47.56  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIAVSTFE--WfpgvqihHSKDLVNWHLVAhplqrvsqldMKGNPNSGgvWAPCLSYSDGKFWLIytdv 91
Cdd:cd08982     7 DPTVVLFKGKYYLFASKSGgyW-------HSDDLVNWKFIP----------TNGLPIED--YAPTVVEINGTLYFT---- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  92 kvvdgAWKDCHNYLVTCETINGDWSE-PITLNSSGFDASLFHDKDGKKYL------LNMLWDHRIDRHSFggiviqeysd 164
Cdd:cd08982    64 -----ASGGPGPIYRTDDPLGGKWELvAESGPFGFWDPALFVDDDGRLYLywgcsnKDPIYGVELDPNTG---------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 165 keQKLIGKPKVIFEGTDRKL-----------------TEAPHLYHIGNYYYLLTAEGGTRYEHAAT-IARSANIEGPYEV 226
Cdd:cd08982   129 --FRPIGEPVPLISFDPDKHgwerfgednedpglapwIEGAWMTKHNGKYYLQYAAPGTEFKTYADgVYVSDSPLGPFTY 206
                         250       260
                  ....*....|....*....|....*..
gi 1586137908 227 HPDNPILtswHDPGNPLQKCGHASIVQ 253
Cdd:cd08982   207 APNNPFS---YKPGGFITGAGHGSTFQ 230
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
34-223 1.41e-05

Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350142 [Multi-domain]  Cd Length: 262  Bit Score: 46.84  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  34 FPGVQIHHSKDLVNWHLVAHPLQRVSQLDMkgNPNSgGVWAPCLSYSD--GKFWL-IYTDvkvvDGAWKDCHNYLVTCET 110
Cdd:cd18821    29 FQGVSCYSSTDLVNWTFEGLALPPQESGDL--GPNR-VVERPKVIYNPstGKYVMwMHID----SSNYGDARVGVATSDT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 111 INGDWSEPITLNSSGF---DASLFHDKDGKKYLL--NMLWDHRIDRHSfggiviQEYSDKEqkligkpKVIFEGTDRKLt 185
Cdd:cd18821   102 VTGPYTYVGSFRPLGYesrDIGVFQDDDGTAYLLfeDRDNGLRIYRLS------DDYLSVV-------ELVYTFIAAGL- 167
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1586137908 186 EAPHLYHIGNYYYLLtAEGGTRYEHAATIARSA-NIEGP 223
Cdd:cd18821   168 EAPAMFKVDGTYYLL-GSHLTGWRPNDNVYFTAtSLSGP 205
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
14-224 2.26e-05

Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A); This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes the bifunctional Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350151 [Multi-domain]  Cd Length: 291  Bit Score: 46.50  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  14 DPSICRVGEDYYIavstFEWFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPN-SGGVWAPCLSYSDGKFWLIYT--- 89
Cdd:cd18830     3 DPVMAREGGTYYL----FSTGPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGfNGHIWAPDISFHNGRYYLYYScsa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  90 ----------------DVKVVDGAWKDcHNYLVTCETINGDWsepitlnsSGFDASLFHDKDGKKYLlnmlwdhridrhS 153
Cdd:cd18830    79 fgkntsaigvatnktlDPDSPDYKWED-HGMVVQSVPGRDLW--------NAIDPNVIVDEKGTPWL------------S 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 154 FG----GIVIQEYSD--------KEQKLIGKPKVIFEGTDRKL----TEAPHLYHIGNYYYLLTAEG----GTRYEHAAT 213
Cdd:cd18830   138 FGsfwgGIKLVKLDPdlkslaepQEWHTIARRERTFKLTDSEAgpgaIEAPFIFKKGGYYYLFVSWDyccrGVNSTYKVV 217
                         250
                  ....*....|.
gi 1586137908 214 IARSANIEGPY 224
Cdd:cd18830   218 VGRSKNVTGPY 228
GH43_CtGH43-like cd18825
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
114-231 4.00e-05

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350146 [Multi-domain]  Cd Length: 285  Bit Score: 45.67  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 114 DWSEPITLNSSGFDA---SLFHDKDGKKYLLnmlwdhridrHSFGG---IVIQEYSDKEQKLIGKPKVIFEGTDRkltEA 187
Cdd:cd18825   123 NAGEKNRDFSNGQMSrdmTLFVDDDGKAYLI----------YSSEEnktLYIAKLTDDYTGVTGDYARILIGQSR---EA 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1586137908 188 PHLYHIGNYYYLLTAeGGTRYE-HAATIARSANIEGPYEVHpDNP 231
Cdd:cd18825   190 PAVFKHDGKYYMITS-GCTGWApNAARYAVADSIFGPWKEI-GNP 232
Ree1 COG3506
Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function ...
389-532 1.48e-04

Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function unknown];


Pssm-ID: 442729  Cd Length: 195  Bit Score: 42.96  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 389 FEAETAVEF-YPENFQQAaGLVNYYNTENW--TALQVTHDEELGriLELTICDNFS-FSQPlnnkiVIPREVKYVYLRVN 464
Cdd:COG3506    58 FTFEVKVTGdFKELYDQA-GLMVRVDEENWikAGIEYVPDGVPR--LGSVVTNGYSdWSTG-----PVPGDPKSVWLRLS 129
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586137908 465 IEKDKYYYFYSFNKEDWHKIDIAleskKLSDDyirgggffTGAFVGMQCQDTSGNHIPADFRYFRYKE 532
Cdd:COG3506   130 RRGDALRIQYSLDGKTWTLLRLA----PLPPA--------APVKVGLMACSPTGEGFTVRFSDFSLTP 185
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
4-75 3.72e-04

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655; This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350097  Cd Length: 262  Bit Score: 42.22  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   4 TNPVLKGFNP-----DPSICRVGED--YYIAVSTFEWFPGVQIH--------HSKDLVNWhlvahplQRVSQLDMKGNPN 68
Cdd:cd08983     5 GNPVLTSTVGtkgvrDPFIIRGPEDgkFYLVATDLWIAGGAQWNgsrgigvwESTDLVNW-------SEQRLVKMVSPPN 77

                  ....*..
gi 1586137908  69 SGGVWAP 75
Cdd:cd08983    78 AGNAWAP 84
GH43_CtGH43-like cd18826
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
33-237 3.78e-04

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350147 [Multi-domain]  Cd Length: 269  Bit Score: 42.23  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  33 WFPGVQIHHSKDLVNWH---LVAHPlqrvsQLDMKGNPnsggvWAPClSYSD----------GKF--WLiytdvKVVDGa 97
Cdd:cd18826    32 WHWGVRCYSSTDLYNWEdegLIIPP-----DPDDPSSP-----LHPT-RIMDrphiiynektGKYvcWL-----KLYPG- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  98 WKDCHNYLVTCETINGdwsePITL---------NSSGfDASLFHDKDGKKYLLnmlwdhrIDR-HSfgGIVIQEYSDKEQ 167
Cdd:cd18826    95 GDVQYFGVLTADSPTG----PYTYvhkflgplgMGAG-DFDLVVDPDGKAYLY-------FERvHK--EVVCADLTDDYT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586137908 168 KLIGKPKVIFEGTDRKL-TEAPHLYHIGNYYYLLTAeGGTRY-EHAATIARSANIEGPYEV----HPDNPILTSWH 237
Cdd:cd18826   161 DVTGEYSTHFPGLGPPFaREAPAVFKRGGKHYLLTS-GTTGYfPNPSEVAVADSYHGPWTVlgnpHVGDGSETSFN 235
GH43_LbAraf43-like cd18820
Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis ...
13-141 6.43e-04

Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350141 [Multi-domain]  Cd Length: 258  Bit Score: 41.74  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  13 PDPSICRVGEDYYiavSTFEWFPGVQIHHSKDLVNWHlvAHPLQRVSQldMKGNPNSGGVWAPCLSYSDGKFWLIYTdvk 92
Cdd:cd18820     1 ADPWVVYHDGYYY---LTFTTGDRITIWKSKTLTGLG--TAEPKVVWT--PPDPSRSCNIWAPELHFIDGRWYIYYA--- 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1586137908  93 VVDGAWKDCHNYLV---TCETINGDWSE--PITLNSSGF--DASLFhDKDGKKYLL 141
Cdd:cd18820    71 ADDGDNANHRMYVLesaSDDPPLGPYTFkgRLADPTDKWaiDGTVL-EHNGKLYFV 125
COG3940 COG3940
Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism];
5-197 1.07e-03

Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism];


Pssm-ID: 443140 [Multi-domain]  Cd Length: 309  Bit Score: 41.34  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908   5 NPVLKGfNPDPSICRVGEDYYIAVSTfeWFPGVQIHHSKDLVNWhlvAHPLQRVSQLDMKGNPNSGGVWAPCLSYSDGKF 84
Cdd:COG3940     1 NPLIEQ-GADPWVYKHDGYYYFTATV--EYDRIVLRRSKTLAGL---ATAEPVVVWTPPASGPMSKNIWAPELHFIDGKW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  85 WLIYTDVKVVDGAWkDCHNYLVTCET---INGDWSE--PITLNSSGF--DASLFhDKDGKKYLLNMLWDHRIDRHSfgGI 157
Cdd:COG3940    75 YIYFAAGDGEDNNF-NHRMYVLENASadpLTGPWTEkgQIKTPWDSWaiDATVF-EHNGKLYLVWSGWEGDINGNQ--NL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1586137908 158 VIQEYSD-----KEQKLIGKPKVIFEGTDRKLTEAPH-LYHIGNYY 197
Cdd:COG3940   151 YIAEMSNpwtlsGPRVLLSKPEYDWEKIGFKVNEGPAvLKHNGKVF 196
GH43_RcAra43A-like cd18823
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ...
33-235 2.31e-03

Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis arabinanase Ara43A and Fibrobacter succinogenes subsp. succinogenes S85 Fisuc_1994 / FSU_2517. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350144 [Multi-domain]  Cd Length: 289  Bit Score: 40.03  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  33 WFPGVQIHHSKDLVNWHLVAHPLQRVSQLDMKGNPNSGGvWA--PCLSY--SDGKFWLIytdVKVVDGAWKDCHNYLVTC 108
Cdd:cd18823    39 SFKSVTLYSSTDLVNWTFEGNVLTASGAVDTAGDFAGAG-WVgrPGVAYnsATGKYVLL---IQWGSTGNGRNGVLFATS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 109 ETING--------DWSEPITLNSSGfDASLFHDKDGKKYLLNMLwdhridRHSFGGIVIQEY-SDKEQKLIGKPKVIFEG 179
Cdd:cd18823   115 DSPTGpftyqrvqPMIDNVGTNNTG-DQTSFFDDDGKAYLVYSN------DRGRGSLYIAKLrSDYLGIEPAVRIDNYVG 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1586137908 180 TDRkltEAPHLYHIGNYYYLLTAEggTRYEHA-AT-IARSANIEGPYEvhPDNPILTS 235
Cdd:cd18823   188 PGR---EGNALFKYGGTYYLCASD--LHGWNAsQTyYMVATSLTGPYS--PSNVLETT 238
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
34-242 7.02e-03

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350145 [Multi-domain]  Cd Length: 282  Bit Score: 38.55  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908  34 FPGVQIHHSKDLVNWHL--VAHPLQRvsqldmkGNPNSGGVWAPCLSYS--DGKFWLIYTDVKVVDGawkdchnYLV-TC 108
Cdd:cd18824    34 FCGFVVYSSVDLVNWTYrgVLFDPNT-------CAGSPGVCFRPHVVYNarTGRYVLWYNAYDGSSG-------YAVaTS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586137908 109 ETINGDWSE--PITLNSSGF---DASLFHDKDGKKYLLNMLWDHridrhsFGGIVIQEYSDkeqKLIGKPKVIFEGTDRK 183
Cdd:cd18824   100 STPTGPFVTvpDPVLAPAGLqagDFSLFVDDDGTGYLAYTTIDF------PQSIVVEQLTD---DYLNTTGEYVRDLIDQ 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586137908 184 LTEAPHLYHIGNYYYLLTAEGGTRYEHAATIA--RSANIEGPYEVHPDNPILTSWHDPGNP 242
Cdd:cd18824   171 EAEAPSIFKRNGIYYILASNTCCGCCQGTGARvyRATSPLGPWTRQIDINSCAGALFPPSD 231
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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