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Conserved domains on  [gi|556491238|ref|WP_023338964|]
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MULTISPECIES: glycoside hydrolase family 43 protein [Enterobacter cloacae complex]

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 ...
5-305 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: 547.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGGIWAPCLSYADGKF 84
Cdd:cd09000    1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYTDVKIVDSPWKNGRNYLVTAPSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYRPWGPRHHSNPHNTIVMQAFDP 164
Cdd:cd09000   81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTSWHLPENPLQ 244
Cdd:cd09000  161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556491238 245 KSGHGSLLQTHTGEWYMAYLTSRPLRlpgvpllasgGRGYCPLGRETGIARIEWR-DGWPYV 305
Cdd:cd09000  241 KAGHGSLVETPDGEWYLAHLCGRPLP----------GRGRCPLGRETAIQKVEWTdDGWPRL 292
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
332-534 6.30e-86

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: 264.13  E-value: 6.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  332 RDDFDASSLDPELQTLRIPFDDTLGSLTARPGYLRLYGNDSLNSTFTQSTVARRWQHFTFRAETRMQFSPVHFQQSAGLT 411
Cdd:pfam17851   1 RDDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  412 CYYNSKNWSYCFVDYEEGQGRTIKVLQLDHNVPSWPLHEQPIPVPESAQSVWLRVDVDTLVYRYSYSFDGETWHTVPVTY 491
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 556491238  492 EAWKLSDDYiGGRGFFTGAFVGLHCEDI-SGDGCHADFDYFTYE 534
Cdd:pfam17851 161 DASILSDEY-AAGGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
5-305 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: 547.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGGIWAPCLSYADGKF 84
Cdd:cd09000    1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYTDVKIVDSPWKNGRNYLVTAPSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYRPWGPRHHSNPHNTIVMQAFDP 164
Cdd:cd09000   81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTSWHLPENPLQ 244
Cdd:cd09000  161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556491238 245 KSGHGSLLQTHTGEWYMAYLTSRPLRlpgvpllasgGRGYCPLGRETGIARIEWR-DGWPYV 305
Cdd:cd09000  241 KAGHGSLVETPDGEWYLAHLCGRPLP----------GRGRCPLGRETAIQKVEWTdDGWPRL 292
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
3-303 2.78e-118

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: 350.08  E-value: 2.78e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238    3 ITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSggiWAPCLSYADG 82
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   83 KFWLLYTDVKivdspwknGRNYLVTAPSIEGPWSEPIPM--GNGGFDPSLFHDDDGRKYYLYRPWGPRHhsnPHNTIVMQ 160
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLksGGGGIDPSLFHDDDGKKYLVWGGWDPRH---GHGGIYLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  161 AFDPQTGTLSPERKTLFTG----TPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTSW 236
Cdd:pfam04616 147 ELDNDGLKLVGPVTKLIYPgtrwVGGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556491238  237 HlPENPLQKSGHGSLLQTHTGEWYMAYLTSRPlrlpgvpllasgGRGYCPLGRETGIARIEWR-DGWP 303
Cdd:pfam04616 227 S-PENPIYGPGHASLVETPDGEWWIVYHAGRP------------GDGGYGLGRETRIQPVEWRaDGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
3-415 1.74e-107

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 324.98  E-value: 1.74e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   3 ITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLdmkGNPDSGGIWAPCLSYADG 82
Cdd:COG3507   22 YTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHNG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  83 KFWLLYTDvkiVDSPWKNGRNYLVTAPSIEGPWSEPIPM---GNGGFDPSLFHDDDGRKYYLYrpwgprhhSNPHNTIVM 159
Cdd:COG3507   99 KYYLYYTA---VDGGKNRSGIGVATADDPEGPWSDPGPLvcpGGNGIDPSVFVDDDGKAYLVY--------GSGGGGIYV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 160 QAFDPQTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGT-SYEHAVVVLRSKTIDGPYELHPEVTMMTSWHl 238
Cdd:COG3507  168 AELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTcNSGYAVRVARSKSPTGPYEDAPGNPILTQRS- 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 239 pENPLQKSGHGSLLQTHTGEWYMAYLTSRPLRlpgvpllasggrgycPLGRETGIARIEWR-DGWPYVEGGKHaqltvkg 317
Cdd:COG3507  247 -DGGIQGPGHGSLVETPDGEWYLVYHAYRPPG---------------GLGRETFLDPVTWNeDGWPVVGPGTG------- 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 318 pqiaEQPAAVQHSWRDDFDaSSLDPELQTlripfddtlgsltarpGYLRLYGndslnstftqstvarrwqhfTFRAETRM 397
Cdd:COG3507  304 ----EPPQPLPAPESDDFD-GPLGLQWSL----------------GYLRLTR--------------------QFTATTKL 342
                        410
                 ....*....|....*...
gi 556491238 398 QfspvhfqqsAGLTCYYN 415
Cdd:COG3507  343 R---------AGLVLYGN 351
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
332-534 6.30e-86

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: 264.13  E-value: 6.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  332 RDDFDASSLDPELQTLRIPFDDTLGSLTARPGYLRLYGNDSLNSTFTQSTVARRWQHFTFRAETRMQFSPVHFQQSAGLT 411
Cdd:pfam17851   1 RDDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  412 CYYNSKNWSYCFVDYEEGQGRTIKVLQLDHNVPSWPLHEQPIPVPESAQSVWLRVDVDTLVYRYSYSFDGETWHTVPVTY 491
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 556491238  492 EAWKLSDDYiGGRGFFTGAFVGLHCEDI-SGDGCHADFDYFTYE 534
Cdd:pfam17851 161 DASILSDEY-AAGGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
Ree1 COG3506
Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function ...
391-535 2.73e-10

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


Pssm-ID: 442729  Cd Length: 195  Bit Score: 59.91  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 391 FRAETRMQFSPVH-FQQsAGLTCYYNSKNWSYCFVDYE-EGQGRTIKVLQLDHNvpSWPLHeqpiPVPESAQSVWLRVDV 468
Cdd:COG3506   58 FTFEVKVTGDFKElYDQ-AGLMVRVDEENWIKAGIEYVpDGVPRLGSVVTNGYS--DWSTG----PVPGDPKSVWLRLSR 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556491238 469 DTLVYRYSYSFDGETWHTVPVTYeawkLSDDyiggrgffTGAFVGLHCEDISGDGCHADFDYFTYEP 535
Cdd:COG3506  131 RGDALRIQYSLDGKTWTLLRLAP----LPPA--------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 ...
5-305 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: 547.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGGIWAPCLSYADGKF 84
Cdd:cd09000    1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYTDVKIVDSPWKNGRNYLVTAPSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYRPWGPRHHSNPHNTIVMQAFDP 164
Cdd:cd09000   81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTSWHLPENPLQ 244
Cdd:cd09000  161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556491238 245 KSGHGSLLQTHTGEWYMAYLTSRPLRlpgvpllasgGRGYCPLGRETGIARIEWR-DGWPYV 305
Cdd:cd09000  241 KAGHGSLVETPDGEWYLAHLCGRPLP----------GRGRCPLGRETAIQKVEWTdDGWPRL 292
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
5-298 1.88e-118

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: 350.12  E-value: 1.88e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGGIWAPCLSYADGKF 84
Cdd:cd08989    1 NPVLPGFHPDPSVVRVGDDYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQLDLTGGPDGGGIWAPDISYHDGKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYTDVKIVDSpWKNGRNYLVTAPSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYRPwgprhhsnphNTIVMQAFDP 164
Cdd:cd08989   81 YIYYTVVLNVGS-WKGRRNYLVTSEDPEGPWSEPVWLDEGGIDPSLFVDDDGKHYMLLNP----------GGIRLAELNP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEvTMMTSWHLPENPLQ 244
Cdd:cd08989  150 DCTKQIGEPKRIWEGTGGRAPEGPHLYKKDGYYYLLTAEGGTGYGHAITIARSKTIYGPYEPCPY-NPILRQQDPQAPLQ 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556491238 245 KSGHGSLLQTHTGEWYMAYLTSRPLrlpgvpllasgGRGYCPLGRETGIARIEW 298
Cdd:cd08989  229 RCGHGKLVETPDGEWWMVYLCGRPL-----------PGGYCPLGRETALAPVEW 271
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
5-305 2.56e-118

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: 350.27  E-value: 2.56e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGGIWAPCLSYADGKF 84
Cdd:cd18617    1 NPILPGFYPDPSICRVGDDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQLDLRGVPSSGGIFAPTIRYHDGRF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYTDVKIVdspwkNGRNYLVTAPSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYRPWGPRHHsNPHNTIVMQAFDP 164
Cdd:cd18617   81 YIITTNVSTD-----GRGNFIVTADDPAGPWSDPVWLDGPGIDPSLFFDDDGKVYLTGTGPPPDPY-EGHGGIWQQEIDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTGTLSPERKTLFT-GTPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTSWHLPENPL 243
Cdd:cd18617  155 ETGKLLGEPKVLWNgGTGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGPYEPCPNNPILTHRHLGSNPV 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556491238 244 QKSGHGSLLQTHTGEWYMAYLTSRPlrlpgvpllasGGRGYCPLGRETGIARIEWRDGWPYV 305
Cdd:cd18617  235 QNTGHADLVEDPDGSWWAVFLGVRP-----------YGGGFHNLGRETFLAPVEWEDGWPVV 285
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
3-303 2.78e-118

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: 350.08  E-value: 2.78e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238    3 ITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSggiWAPCLSYADG 82
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   83 KFWLLYTDVKivdspwknGRNYLVTAPSIEGPWSEPIPM--GNGGFDPSLFHDDDGRKYYLYRPWGPRHhsnPHNTIVMQ 160
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLksGGGGIDPSLFHDDDGKKYLVWGGWDPRH---GHGGIYLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  161 AFDPQTGTLSPERKTLFTG----TPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTSW 236
Cdd:pfam04616 147 ELDNDGLKLVGPVTKLIYPgtrwVGGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556491238  237 HlPENPLQKSGHGSLLQTHTGEWYMAYLTSRPlrlpgvpllasgGRGYCPLGRETGIARIEWR-DGWP 303
Cdd:pfam04616 227 S-PENPIYGPGHASLVETPDGEWWIVYHAGRP------------GDGGYGLGRETRIQPVEWRaDGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
3-415 1.74e-107

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 324.98  E-value: 1.74e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   3 ITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLdmkGNPDSGGIWAPCLSYADG 82
Cdd:COG3507   22 YTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHNG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  83 KFWLLYTDvkiVDSPWKNGRNYLVTAPSIEGPWSEPIPM---GNGGFDPSLFHDDDGRKYYLYrpwgprhhSNPHNTIVM 159
Cdd:COG3507   99 KYYLYYTA---VDGGKNRSGIGVATADDPEGPWSDPGPLvcpGGNGIDPSVFVDDDGKAYLVY--------GSGGGGIYV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 160 QAFDPQTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGT-SYEHAVVVLRSKTIDGPYELHPEVTMMTSWHl 238
Cdd:COG3507  168 AELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTcNSGYAVRVARSKSPTGPYEDAPGNPILTQRS- 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 239 pENPLQKSGHGSLLQTHTGEWYMAYLTSRPLRlpgvpllasggrgycPLGRETGIARIEWR-DGWPYVEGGKHaqltvkg 317
Cdd:COG3507  247 -DGGIQGPGHGSLVETPDGEWYLVYHAYRPPG---------------GLGRETFLDPVTWNeDGWPVVGPGTG------- 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 318 pqiaEQPAAVQHSWRDDFDaSSLDPELQTlripfddtlgsltarpGYLRLYGndslnstftqstvarrwqhfTFRAETRM 397
Cdd:COG3507  304 ----EPPQPLPAPESDDFD-GPLGLQWSL----------------GYLRLTR--------------------QFTATTKL 342
                        410
                 ....*....|....*...
gi 556491238 398 QfspvhfqqsAGLTCYYN 415
Cdd:COG3507  343 R---------AGLVLYGN 351
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
332-534 6.30e-86

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: 264.13  E-value: 6.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  332 RDDFDASSLDPELQTLRIPFDDTLGSLTARPGYLRLYGNDSLNSTFTQSTVARRWQHFTFRAETRMQFSPVHFQQSAGLT 411
Cdd:pfam17851   1 RDDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  412 CYYNSKNWSYCFVDYEEGQGRTIKVLQLDHNVPSWPLHEQPIPVPESAQSVWLRVDVDTLVYRYSYSFDGETWHTVPVTY 491
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 556491238  492 EAWKLSDDYiGGRGFFTGAFVGLHCEDI-SGDGCHADFDYFTYE 534
Cdd:pfam17851 161 DASILSDEY-AAGGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
5-303 3.89e-64

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: 210.95  E-value: 3.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGED---YYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMK---GNPDSGGIWAPCLS 78
Cdd:cd18833    1 NPIIPGFHPDPSCIFVPEWdgtFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSQLPELattGTGQQGGIWAPTLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  79 YADGKFWLLYTDVKIVDSPWKNGRNYLVTA--PSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYRpwgprHHSNPHNT 156
Cdd:cd18833   81 YHDGTFYVITTLVFPDKTDASRWDNLLFTTtdPYSDSAWSDPIRFDFPGYDPDLFWDDDGTAYVQGA-----HYWRVRPE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 157 IVMQAFDPQTG-TLSPERKTLFTGTPlcYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVTMMTS 235
Cdd:cd18833  156 IQQQEIDLKTGeSLSPSPIWNGTGGS--APEGPHMYKKDGWYYLLIAEGGTGLGHSVTIARSRSIWGPYESYPSNPVLTN 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556491238 236 WHLPENpLQKSGHGSLLQTHTGEWYMAYLTSRplrlpgvpllasGGRGYC--PLGRETGIARIEW-RDGWP 303
Cdd:cd18833  234 ANTSEY-FQTVGHADLFQDANGNWWGVALATR------------SGPEYEiyPMGRETVLYPVTWeEGEWP 291
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
4-305 2.48e-57

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: 192.34  E-value: 2.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   4 TNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPD-----SGGIWAPCLS 78
Cdd:cd09001    3 TNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAYYLEDgknayGKGIWAPSLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  79 YADGKFWLLYTDVkivdspwkNGRNYLVTAPSIEGPWSEPIPMGNGGFDPSLFHDDDGRKYYLYrpwgprhhsnPHNTIV 158
Cdd:cd09001   83 YHNGKFYVYFCTN--------TGGTYVYTADDPAGPWSRPALIGKGYHDPSLLFDDDGKAYLVY----------GNGEIR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 159 MQAFDPQTGTLSPERKTLFTGTPLCYT-EGAHLYRHAGWYYLMVAEGGtSYEHAVVVLRSKTIDGPYELHPEVtmmtswH 237
Cdd:cd09001  145 LTELSPDGTGVGGEGRVIIDGTEEGLGaEGSHLYKINGYYYIFNIEWG-GGGRTQVVLRSKSLYGPYEGRVVL------D 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 238 LPENPLQKSGH-GSLLQTHTGEWY-MAYLtsrplrlpgvpllasgGRGycPLGRETGIARIEWRDGWPYV 305
Cdd:cd09001  218 DGSGTGDNGPHqGGLVDTPDGEWWfMLFQ----------------DRG--AVGRIPVLVPVTWKDGWPVI 269
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
13-265 3.82e-54

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: 183.41  E-value: 3.82e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  13 PDPSLCRQGEDYYIATSTFEW--FPGVRIYHSRDLKNWSLVSTPLDRvsmlDMKGNPDSGGIWAPCLSY-ADGKFWLLYT 89
Cdd:cd08978    1 ADPSILKDNGRYYIYATTDDTgtGTGIVVWKSKDLVNWKEEGTVLSR----GKSKSWGTGNLWAPEVYYfNSGKWYLYYS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  90 DVkivdSPWKNGRNYLVTAPSIEGPWSEPIPM-----GNGGFDPSLFHDDDGRKYYLYRPWgprhhsNPHNTIVMQAFDP 164
Cdd:cd08978   77 AV----PNGGGGRIYVATSDSPEGPFTPIVSGklgdrGSGSIDPTVFVDDDGKLYLYYGDE------DDSGDIYVAELDP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTGTLSPERKTLF-----TGTPLCYTEGAHLYRHAGWYYLMVAEGGTSYEHAVVVLRSKTIDGPYELHPEVtmMTSWHLP 239
Cdd:cd08978  147 DLLTIKGDVTLLIgevvgSGFRGNYFEGPAVFKRNGYYYLIYSAGGTDGGYAIGYATSDSPLGPWEKASHN--PGLQTSG 224
                        250       260
                 ....*....|....*....|....*.
gi 556491238 240 ENPLQKSGHGSLLQTHTGEWYMAYLT 265
Cdd:cd08978  225 ATGIYGPGHGSIFQDEGDRWYIVYHA 250
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
4-305 4.22e-51

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: 175.88  E-value: 4.22e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   4 TNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWSLVSTPLDRVsmldmkgnpdSGGIWAPCLSYADGK 83
Cdd:cd09002    2 LNPILAGDYPDPSILRDGDDYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAALTEY----------IGTVWAPDLIKHDGR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  84 FWLLYtdvkivdsPWKNGRNYLVTAPSIEGPWSEPIPMG-NGGFDPSLFHDDDGRKyYLYRPWGPRHHSNPHNTIVmqAF 162
Cdd:cd09002   72 YYIYF--------PAKGGTNYVITADDIAGPWSEPIDLKvGSGIDPGHVVDEDGKR-YLFLSGGRRVRLTDDGLSV--AG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 163 DPQTgTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGT---SYEHAVVVLRSKTIDGPYELHPEVTMMTSWHlP 239
Cdd:cd09002  141 PPEK-VYDGWRYPDEWDVECFCLEGPKLFRRGGYYYLTTAQGGTagpPTSHMVVSARSKSPHGPWENSPYNPLVRTQS-R 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556491238 240 ENPLQKSGHGSLLQTHTGEWYMAYLTSRplrlpgvpllasggRGYCPLGRETGIARIEW-RDGWPYV 305
Cdd:cd09002  219 EEKWWSKGHGTLVEGPDGKWWMVYHGYE--------------NGYRTLGRQTLLEPVEWtADGWFRI 271
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
5-304 5.87e-25

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: 104.53  E-value: 5.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYiATSTFEWFPGVRIYHSRDLKNWSLVST-PLDRVSmldmKGNPDSGGIWAPCLSY-ADG 82
Cdd:cd08999    1 NPVIDGDFPDPSVIRVGGTYY-AFATNSGGKNVQVATSTDLVTWTLLGGdALPDLP----AWAAAGGNTWAPDVVRrPDG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  83 KFWLLYTdvkivdSPWKNGRNYLV---TAPSIEGPW---SEP--IPMGNGG-FDPSLFHDDDGRKYYLYRPWGPrhhSNP 153
Cdd:cd08999   76 KYVMYYS------ARLKSSGKHCIgvaTSDSPLGPFtpvGEPplCPLDQGGaIDPSGFVDPDGKRYLVYKVDGN---SIG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 154 HNT-IVMQAFDPQTGTLSPERKTLFTGT-----PLcyTEGAHLYRHAGWYYLMVAEG---GTSYehAVVVLRSKTIDGPY 224
Cdd:cd08999  147 VPTpIMLQELSADGLTLVGEPVELLLNDgpwdgPL--VEAPSLVKRDGTYYLFYSSNcycSPSY--AVGYATSKSITGPY 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 225 ELHPEVTMMTS---WHLPenplqksGHGSLLQThTGEWYMAYLTSRPLRLPGvpllasGGRG-YcplgretgIARIEWRD 300
Cdd:cd08999  223 TKAGEPLLLTGdggLTGP-------GGADVVED-DGGDWMVFHAWDGGDDVG------GGRAmY--------TAELTWEG 280

                 ....
gi 556491238 301 GWPY 304
Cdd:cd08999  281 GWPV 284
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
14-304 2.30e-24

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: 102.30  E-value: 2.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYI--ATSTFEWFPGVR--IYHSRDLKNWSLVSTPLDrvsmLDMKGNPDSGGIWAPCLSYADGKFWLLYT 89
Cdd:cd09004    2 DPDIVVFGGRYYIypTTDGPPGWSSTSfhVFSSTDLVNWTDHGIILD----LANDVWWANKGAWAPAVAERNGKYYFYFS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  90 -DVKIvdspwknGrnyLVTAPSIEGPW---SEPI----PMGNGGFDPSLFHDDDGRkYYLYrpWGprhhsnpHNTIVMQA 161
Cdd:cd09004   78 aGSQI-------G---VAVSDSPTGPFtdlGRPLvtggDYGGQAIDPMVFVDDDGQ-AYLY--WG-------NGTAYVAR 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 162 FDPQTGTLSPERKTLFTgtPLCYTEGAHLYRHAGWYYLMVAEGGT-SYEHAVVVLRSKTIDGPYELHPEVTMMTswhlPE 240
Cdd:cd09004  138 LNDDMVSFDGEVVVSIT--PPNFREGPFVHKRNGIYYLSWSENDTrDPDYRVRYATSDSPLGPWTYRGVGLLLD----SA 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556491238 241 NPLQKSGHGSLLQT-HTGEWYMAYltsrpLRLPGVpllasGGRGYcplGRETGIARIEWR-DGWPY 304
Cdd:cd09004  212 GGIKGTGHHSIVQVpGTDEWYIAY-----HRFAVP-----GGDGY---HREVAIDRLEFDaDGTIR 264
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
14-261 3.82e-24

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: 101.54  E-value: 3.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIATST----FEWFP--GVRIYHSRDLKNWSLVSTPLD----------RVSMLDMKGNPdsGGIWAPCL 77
Cdd:cd08986    4 DPYITLGPDGYYYLTGTtggpDWWGVndGIRLWRSKDLKDWEYLGLVWDlekdgwwqwePQWWTPDSKNK--RALWAPEI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  78 SYADGKFWLLYTdvkivdSPWKNGRNYLVTAPSIEGPWSEPI--PMGNGgFDPSLFHDDDGRKYYLYrpwgprhhsnpHN 155
Cdd:cd08986   82 HYINGTWYITHS------MNGGGTGLLKSTTGKPEGPYVDPMggPLGKG-IDPSLFEDDDGTVYLVW-----------GN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 156 TIVMQAFDPQTGTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVA------EGGTSYEHAVVVlrSKTIDGPYelHPE 229
Cdd:cd08986  144 GQIARLKKDMSGFAEEPRKIDPSGNREIGHEGAFIFKIGGKYVLFGAawstdkMRKGTYDLYYAT--SDSIYGPY--SER 219
                        250       260       270
                 ....*....|....*....|....*....|..
gi 556491238 230 VTMMTswHLpenplqksGHGSLLQTHTGEWYM 261
Cdd:cd08986  220 RFAGP--HG--------GHGTPFKDKDGQWWC 241
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 4.57e-22

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: 96.20  E-value: 4.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIATSTFEWF------PGVriYHSRDLKNWSL--VSTPLDRVSMLDMkgnpdsggIWAPCLSYA-DGKF 84
Cdd:cd18608    3 DPSIVKFGGTYYLYATTDGWGgfnsgePVV--WKSKDFVNWKFegLNWPTKAASGDSK--------VWAPSVVKGkDGKY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYT-DVKIvdspwkngrnYLVTAPSIEGPW------SEPIPMGN-----GGFDPSLFHDDDGrKYYLYrpWGPRHHSN 152
Cdd:cd18608   73 YMYVSvGSEI----------YVGVADSPLGPWknangdGPPIIPGDgkpnyHMIDAEPFIDDDG-KAYLY--WGSGLHVN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 153 PHNTIVMQAFDpqtgTLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMVAEGGTSYE-HAVVVLRSKTIDGPYELHPEVT 231
Cdd:cd18608  140 GHCFAAKLNPD----MVTFDGSEPTIVTPRDYFEAPFMFKRNGIYYLMYSGGGCWDEtYNVRYAVSDNPLGPFEEGENSP 215
                        250       260       270
                 ....*....|....*....|....*....|...
gi 556491238 232 MMTSwhLPENPLQKSGHGSLLQtHTGEWYMAYL 264
Cdd:cd18608  216 ILQT--DEAKGIFGPGHHSVFE-EGGQYYILYH 245
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
5-263 1.54e-21

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: 94.95  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGFNPDPSLCRQGEDYYIATSTFE-WFPG-----VRIYHSRDLKNWSLVSTPLDRVsmlDMKGNPDSGGIWAPCLS 78
Cdd:cd18616    1 NPVFEPTFADPTVIRGDDGYFYAYATEDpWGDGggfrlVPILRSKDLVNWEYVGDAFTSK---PRWKWDPGGGLWAPDIR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  79 YADGKFWLLYTdvkivDSPWKNGRNY---LVTAPSIEGPW--------SEPIPMGNgGFDPSLFHDDDgrKYYLYrpWGp 147
Cdd:cd18616   78 YIDGKYVLYYS-----LSDWGADPNPgigVATADSPAGPFtdqgklfdSNEIGVRN-SIDPFVFEDDG--KKYLF--WG- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 148 rhhsNPHNTIVMQafdpqtgtLSPERKTLFTGTP--LCYT--EGAHLYRHAGWYYLMVAEGG------TSYEhaVVVLRS 217
Cdd:cd18616  147 ----SFYGIYAVE--------LTADGLALKPGEKvqIAGDryEGPYIVKRDGYYYLFGSAGSccegpnSTYR--VVVGRS 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556491238 218 KTIDGPYELHPEVTMMT--SWHLPENpLQKS------GHGSLLQTHTGEWYMAY 263
Cdd:cd18616  213 ESLLGPYVDRDGRSLLDsgGGGTPVV-LQNGnrfvgpGHNAVITDDAGQDWMLY 265
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
14-224 1.34e-20

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: 91.84  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIATSTFewfPGVRIYHSRDLKNWSLVSTPLDRV-SMLDMKGNPDSGGIWAPCLSYADGKFWLLYtdvk 92
Cdd:cd08998    3 DPSIIKDDGGTYYVFSTG---AGIQIRTSKDLVNWEFVGTVFPEGpAWAAAEVPGGAGGLWAPDVVYVNGRYYLYY---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  93 ivdSPWKNGRN----YLVTAPSIE-GPWSE--PIPMGNGGF-----DPSLFHDDDGRKYYLYRPWgprhhsnpHNTIVMQ 160
Cdd:cd08998   76 ---SASTFGSNrsaiGLATSTTLDdGPWTDqgLVVSSSPGDdynaiDPNVFVDADGRLWLAYGSF--------WGGIKLV 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556491238 161 AFDPQTGTLSPERktlfTGTPLCYT-------EGAHLYRHAGWYYLMVAEG------GTSYEhaVVVLRSKTIDGPY 224
Cdd:cd08998  145 ELDPATGKLRPGS----TGTSIASRpggpgaiEAPYIIYRGGYYYLFVSYGsccrgaNSTYN--IRVGRSTSITGPY 215
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
13-224 7.03e-20

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: 89.88  E-value: 7.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  13 PDPSLCRQGEDYYI-ATSTFEWfpGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGG-IWAPCLSYADGKFWLLYtd 90
Cdd:cd08988    1 HDPSIIKEGGTYYAfGTGTDGF--GIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGnLWAPDISQHKGKYYLYY-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  91 vkivdSPWKNGRNY----LVTAPSIEGP-WSEPIPMGN-------GGFDPSLFHDDDGRKYYLYRPWgprhhsnpHNTIV 158
Cdd:cd08988   77 -----SVSDNGSNTsaigLATANNPQGPfKDEGPAKPVvtsdnagNAIDPDLFQDEDGQNWLLYGSF--------WGGIW 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556491238 159 MQAFDPQTG-TLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLMV-----AEGGTSYEHaVVVLRSKTIDGPY 224
Cdd:cd08988  144 LQKLDKNGLvVNPPGNGKSIAVLYYVSIEAPYITYAGGYYYLFVsagscCDGGNSTYH-TRVGRSKKVTGPY 214
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
13-307 3.01e-19

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: 88.00  E-value: 3.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  13 PDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDLKNWslvsTPLDRVsmLDMKGNPDSGGIWAPCLSYADGKFWLLYTdvk 92
Cdd:cd08991    1 ADPFVLKHNGTYYLYGTGGDDGRGFKVYVSDDLVNW----EYPGGA--LEEPGLWGTKGFWAPEVFYYNGKFYMYYS--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  93 iVDSPWKNGRNYLVTAPSIEGP--WSEPIPMGNGGF--DPSLFHDDDGrKYYLY---RPWGprhhSNPHNTIVMQAF-DP 164
Cdd:cd08991   72 -ANGGDHGEHIAVAVSDSPLGPfrDKGKLLIPAGGFsiDAHVFIDDDG-KWYLYyvrDDLG----GEPGNRIYVAELeDD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 165 QTG--------TLSPERKTLFTGTPLCYT-EGAHLYRHAGWYYLMVAEGGTSYEH-AVVVLRSKTIDGPYElhpevtmmt 234
Cdd:cd08991  146 LSLigeptlvlCPTADERWEYGEGRDWHTtEGPTVLKHNGTYYLTYSANHFRSPDyAVGYATADSPLGPWT--------- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 235 swHLPENPLQKS--------GHGSLLQTHTGEWYMAYLTSRPLRLPGvpllasggrgycplGRETGIARIEWRDGWPYVE 306
Cdd:cd08991  217 --KYEGNPILSRndggvngpGHNSVFKDPDGDLYIVYHTHDSDETVE--------------PRKMRIDRLRFDGDKLSVL 280

                 .
gi 556491238 307 G 307
Cdd:cd08991  281 G 281
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
35-300 3.56e-17

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: 81.49  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  35 PGVRIYHSRDLKNWSLVSTPLDrvsmLDMKGNPDSGGIWAPCLSYADGKFWLlYTDVKIVDSPWKNGrnyLVTAPSIEGP 114
Cdd:cd08990   30 DDWHVFSSTDLVNWTDHGEILP----PDDVFWWASGNAWAPDAVYKNGKYYF-YFPVGQASDGFGIG---VAVSDSPAGP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 115 W-----SEPIPMGNGG---FDPSLFHDDDGRkYYLYrpWGPRHH-------SNphntivMQAFDPQTgtlsperKTLFTG 179
Cdd:cd08990  102 FkdalgKPLIPEGLNGiegIDPAVFVDDDGR-AYLY--FGGGGGyyvaklkDD------MISLAGEP-------QKIKNG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 180 TPLCYTEGAHLYRHAGWYYLMVAeGGTSYEHAVVVLRSKTIDGPYElHPEVTMmtswhlpENPLQKSGHGSLLQTHtGEW 259
Cdd:cd08990  166 GLKGFFEAPWVFKRNGTYYLSYA-GGWAYPAEIAYSTADSPLGPYT-YRGVIL-------DPVGSGTNHGSIVEFK-GQW 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 556491238 260 YMAYLTSrplrlpgvplLASGGRGYcplGRETGIARIEWRD 300
Cdd:cd08990  236 YLFYHTA----------DLSGGGDF---RRSVCIDYLHYNA 263
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
14-302 1.81e-13

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: 70.77  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIATSTfEWFPG-----VRIYHSRDLKNWSlvstplDRVSMLDMKGNPDS----GGIWAPCLSYADGKF 84
Cdd:cd18828    2 DPDIAYFDGKYYIYPTT-DGFPGwsgtqFHVFSSDDLVTWK------DEGVILDLKNDQVVpwatGNAWAPTIEERDGKY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  85 WLLYTDVKivdspwKNGRNYL--VTAPSIEGPWS-EPIPM---------GNGGFDPSLFHDDDGRKYYLYrpWGprhhsN 152
Cdd:cd18828   75 YFYFCGKN------PDGRSQIgvAVADSPTGPFTaQGSPLithemarvtMGQAIDPSVFTDPVDGKYYLY--WG-----N 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 153 PHNTIVMQAFDpqtgTLSPERKTLFTGTPLC-YTEGAHLYRHAGWYYLMVAEGGTSYE-HAVVVLRSKTIDGPYELHPEV 230
Cdd:cd18828  142 GYAAIAELNDD----MISIKPGTLVNLDGLTdFREAVTVLYRDGLYHFTWSCDDTGSEnYHVNYGTSDSPYGPITYRGVI 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556491238 231 tmmtswhLPENPLQK---SGHGSLLQ-THTGEWYMAYLTSRPlrlpgvPLLA-SGGRGYcplGRETGIARIEW-RDGW 302
Cdd:cd18828  218 -------LQKDPSKGilgTGHHSILQvPGTDEWYIAYHRFAT------PLGIyGSGLGY---HRETCIDRLTFdADGL 279
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
40-269 1.25e-11

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: 65.38  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  40 YHSRDLKNWslvsTPLDRVsmLDMKGNP-DSGGIWAPCLSYADGKFWLLYT--DVKIVDSPwknGRNYLVTAPSIEGPW- 115
Cdd:cd18827   31 FSSPDLVHW----TKHERI--LDMADVPwANRAVWAPSVIEKNGKYYLYFAanDIQSDDEG---GGIGVAVADRPEGPFk 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 116 --------------SEPIpmgnggfDPSLFHDDDGRkYYLYrpWGPRHHSNphntiVMQAFDPQTGTLSPERKTLFTG-T 180
Cdd:cd18827  102 dalgkpligefhngAQPI-------DQHVFKDDDGQ-AYLY--YGGWGHCN-----VAKLNDDMTSLVPFDDGETFKEiT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 181 PLCYTEGAHLYRHAGWYYLMVAEGG-TSYEHAVVVLRSKTIDGPYE-----LHPEVTMMTSwhlpenplqkSGHGSLLQT 254
Cdd:cd18827  167 PEGYVEGPFMFKRNGKYYFMWSEGGwTGPDYSVAYAVADSPLGPFKrigkiLQQDPAIATG----------AGHHSVVNV 236
                        250
                 ....*....|....*.
gi 556491238 255 -HTGEWYMAYlTSRPL 269
Cdd:cd18827  237 pGTDDWYIVY-HRRPL 251
GH43-like cd08982
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
40-263 1.55e-11

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: 65.28  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  40 YHSRDLKNWSLVSTPldrvsmldmkGNPDSGgiWAPCLSYADGKFWLLytdvkivdSPWKNGRNYLVTAPsiEGPWSEPI 119
Cdd:cd08982   28 WHSDDLVNWKFIPTN----------GLPIED--YAPTVVEINGTLYFT--------ASGGPGPIYRTDDP--LGGKWELV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 120 PMG--NGGFDPSLFHDDDGRkYYLYrpWGprhhSNPHNTIVMQAFDPQTGTLSP-ERKTLFTGTPLC------------- 183
Cdd:cd08982   86 AESgpFGFWDPALFVDDDGR-LYLY--WG----CSNKDPIYGVELDPNTGFRPIgEPVPLISFDPDKhgwerfgednedp 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 184 ----YTEGAHLYRHAGWYYLMVAEGGT---SYEHAVVVlrSKTIDGPYELHpevtmmtswhlPENPL--------QKSGH 248
Cdd:cd08982  159 glapWIEGAWMTKHNGKYYLQYAAPGTefkTYADGVYV--SDSPLGPFTYA-----------PNNPFsykpggfiTGAGH 225
                        250
                 ....*....|....*
gi 556491238 249 GSLLQTHTGEWYMAY 263
Cdd:cd08982  226 GSTFQDKYGNYWHFG 240
GH43_AnAbnA-like cd18831
Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); ...
14-224 4.98e-11

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: 63.77  E-value: 4.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIATSTFewfPGVRIYHSRDLKN-WSLVSTPLDRVSMLDMKGNPDsggIWAPCLSYADGKFWLLYTdVK 92
Cdd:cd18831    3 DPSIIRREDGTYFRFSTG---GGIRIATAPSLTGpWTYVGSVLPGGSSIDLAGNDD---LWAPDVHYVNGTYYCYYS-VS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  93 IVDSpwKNGRNYLVTAPSIE-GPWS---EPIPMGNG----GFDPSLFHDDDGRKYYLYRPWGprhhsnphNTIVMQAF-- 162
Cdd:cd18831   76 TFGS--QDSAIGVATSPTMEpGSWTdhgAVIRSSSGdpynAIDPNLIVDDDGTPYLTFGSYW--------QGIFQVPLtd 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556491238 163 DPQTGTLSPERKTL-FTGTPLCYTEGAHLYRHAGWYYLMVAEGGTSY----------EHAVVVLRSKTIDGPY 224
Cdd:cd18831  146 PLLSPAAGPPPTHLaYNPSGNHPEEGSFMYKHGGYYYLFFSSGICCGydpslpapgeEYKIRVCRSTSPTGPF 218
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
14-260 1.39e-10

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: 62.29  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIatstFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPD-SGGIWAPCLSYADGKFWLLYtdvk 92
Cdd:cd18830    3 DPVMAREGGTYYL----FSTGPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGfNGHIWAPDISFHNGRYYLYY---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  93 ivdSPWKNGRNY----LVTAPSIeGPWSEPIPMGNGG--------------FDPSLFHDDDGRKY--------------- 139
Cdd:cd18830   75 ---SCSAFGKNTsaigVATNKTL-DPDSPDYKWEDHGmvvqsvpgrdlwnaIDPNVIVDEKGTPWlsfgsfwggiklvkl 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 140 ---YLYRPWGPRHHS--NPHNTIVMQAFDPQTGTLsperktlftgtplcytEGAHLYRHAGWYYLMVA-----EGGTSYE 209
Cdd:cd18830  151 dpdLKSLAEPQEWHTiaRRERTFKLTDSEAGPGAI----------------EAPFIFKKGGYYYLFVSwdyccRGVNSTY 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556491238 210 HaVVVLRSKTIDGPYELHPEVTMMtswhlpenplqkSGHGSLLQTHTGEWY 260
Cdd:cd18830  215 K-VVVGRSKNVTGPYLDKDGKSML------------QGGGTLVVGGNKRWA 252
Ree1 COG3506
Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function ...
391-535 2.73e-10

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


Pssm-ID: 442729  Cd Length: 195  Bit Score: 59.91  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 391 FRAETRMQFSPVH-FQQsAGLTCYYNSKNWSYCFVDYE-EGQGRTIKVLQLDHNvpSWPLHeqpiPVPESAQSVWLRVDV 468
Cdd:COG3506   58 FTFEVKVTGDFKElYDQ-AGLMVRVDEENWIKAGIEYVpDGVPRLGSVVTNGYS--DWSTG----PVPGDPKSVWLRLSR 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556491238 469 DTLVYRYSYSFDGETWHTVPVTYeawkLSDDyiggrgffTGAFVGLHCEDISGDGCHADFDYFTYEP 535
Cdd:COG3506  131 RGDALRIQYSLDGKTWTLLRLAP----LPPA--------APVKVGLMACSPTGEGFTVRFSDFSLTP 185
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
14-259 1.68e-09

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: 58.91  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYiatsTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGG--IWAPCLSYADGKFWLLYtdv 91
Cdd:cd18829    3 DPSIIKEGSTWW----TFSTGDGIPVKYSSDGLNWTQGPPIFGSPLSWWKTYVPANTTndVWAPDVHYYNGKYWLYY--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  92 kivdSPWKNGRNY----LVTAPSIE-GPWSEP---IPMGNG----GFDPSLFHDDDGRKYYLYRPWgprhhsnpHNTIVM 159
Cdd:cd18829   76 ----AISTFGSNTsaigLASASSIAaGNWTDEglvLRSTSAdnynAIDPNLVIDASGNPWLVFGSF--------WSGIKI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 160 QAFDPQT--GTLSPERKTLFTGTPLcytEGAHLYRHAGWYYLMVAEG----GTSYEHAVVVLRSKTIDGPYELHPEVTMM 233
Cdd:cd18829  144 TRLDKATmkPTGSIYSIASRPSGGI---EGPFIVYRDGYYYLFVSIDkccrGVNSTYKIAYGRSTSITGPYLDKNGKDML 220
                        250       260
                 ....*....|....*....|....*.
gi 556491238 234 tswhlpenplqkSGHGSLLQTHTGEW 259
Cdd:cd18829  221 ------------NGGGTVLDSGNSRW 234
GH43_GsAbnA-like cd18832
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ...
14-224 1.81e-09

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: 59.19  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  14 DPSLCRQGEDYYIATStfewfpgvriyH-----SRDLKNWSLVSTPL--DRVSMLDMKGNPD-----------SGGIWAP 75
Cdd:cd18832    3 DPSIVKDDGTYYVFGS-----------HlaaakSTDLMNWTQFTNGVttDNPLLFNLFDSTAwelaedfnwagGGNLWAP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  76 CLSY--ADGKFWLLYTdvkiVDSPWKNGRNYLVTAPSIEGPW----------------SEPIPMGNGG----------FD 127
Cdd:cd18832   72 DVIYnkAMGKYCMYYS----VSGDDSPSAIGLATADNIEGPYtykgtvlksgftgstsADADVYLTGGkynnnyhpnaID 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 128 PSLFHDDDGRKYYLYRPW--GprhhsnphntIVMQAFDPQTG----TLSPERKTL--FTGTPL---CYT--EGAH-LY-R 192
Cdd:cd18832  148 PCVFYDKDGKLWMVYGSWsgG----------IFLLELDPKTGlrdySVETDGNLPdqYYGKKIaggYHAsgEGPYiLYdK 217
                        250       260       270
                 ....*....|....*....|....*....|....
gi 556491238 193 HAGWYYLMVAEGGTSYE--HAVVVLRSKTIDGPY 224
Cdd:cd18832  218 DTGYYYLFVSYGGLDANggYNIRVFRSKNPDGPY 251
GH43_Xsa43E-like cd18618
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ...
31-266 3.09e-09

Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), 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. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. 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: 350130 [Multi-domain]  Cd Length: 275  Bit Score: 58.00  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  31 FEWfpgvRIYHSRDLKNWSLVSTPLdrvSMLDMKGNpdSGGIWAPCLSYADGKFWLLYTdvkiVDSPWKNGRNYLV-TAP 109
Cdd:cd18618   33 NDW----RVFSTTDMVNWTDHGAVL---SLKDFSWA--KGDAWAGQVIERNGKFYWYVP----VHHKTNGGFAIGVaVSD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 110 SIEGPWSEPI-------------PMGNGGFDPSLFHDDDGRKYyLYrpWGprhhsNPHNTIV-----MQAFDPQTGTLSP 171
Cdd:cd18618  100 SPTGPFKDALgkplitndmtgttNHSWDDIDPTVFIDDDGQAY-LY--WG-----NPELYYVklkedMISLDGEIGTIDI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 172 ERKTLFTgtplcytEGAHLYRHAGWYYLMVAEGG---TSYEhavvvlRSKTIDGPYElHPEVTMMTSWHLPENplqksgH 248
Cdd:cd18618  172 SGLPDFT-------EAPWVHKRNGLYYLSYAAGFpekIAYA------TSDSPTGPWT-YKGVIMDPAGNSFTN------H 231
                        250
                 ....*....|....*...
gi 556491238 249 GSLLQTHtGEWYMAYLTS 266
Cdd:cd18618  232 PAIIEFK-GQSYFFYHNG 248
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
34-223 7.22e-08

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: 53.78  E-value: 7.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  34 FPGVRIYHSRDLKNWSLVSTPLDRVSMLDMkgNPDSGGiWAPCLSYAD--GKFWLLytdVKIVDSPWKNGRNYLVTAPSI 111
Cdd:cd18821   29 FQGVSCYSSTDLVNWTFEGLALPPQESGDL--GPNRVV-ERPKVIYNPstGKYVMW---MHIDSSNYGDARVGVATSDTV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 112 EGPWS---EPIPMGNGGFDPSLFHDDDGRKYYLYrpwgprhHSNPHNTIVMQAFDpqtGTLSPERKT-LFTGTPLcytEG 187
Cdd:cd18821  103 TGPYTyvgSFRPLGYESRDIGVFQDDDGTAYLLF-------EDRDNGLRIYRLSD---DYLSVVELVyTFIAAGL---EA 169
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 556491238 188 AHLYRHAGWYYLMVAeGGTSYEH-AVVVLRSKTIDGP 223
Cdd:cd18821  170 PAMFKVDGTYYLLGS-HLTGWRPnDNVYFTATSLSGP 205
DUF1349 pfam07081
Protein of unknown function (DUF1349); This family consists of several hypothetical bacterial ...
391-535 8.32e-08

Protein of unknown function (DUF1349); This family consists of several hypothetical bacterial proteins but contains one sequence from Saccharomyces cerevisiae. Members of this family are typically around 200 residues in length. The function of this family is unknown.


Pssm-ID: 462084  Cd Length: 168  Bit Score: 52.18  E-value: 8.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  391 FRAETRMQFSPVHFQQSAGLTCYYNSKNWSYCFVDYEEGQGRTIKVLQLDHnvPSWPLheQPIPVPESAQSVWLRVDVDT 470
Cdd:pfam07081  40 FTAEVKVSGDFKELYDQAGLMVRVDEENWIKAGIEYNDGVQRLGSVVTNGY--SDWST--SPLPSEWDPKEVWLRVSRRG 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556491238  471 LVYRYSYSFDGETWHTVPVTYeawkLSDDyiggrgffTGAFVGLHCEDISGDGCHADFDYFTYEP 535
Cdd:pfam07081 116 DAFTIEYSTDGEKWTLLRLAH----LPAA--------EEVQVGLYACSPTGEGFTVTFDEFRLTP 168
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
21-200 6.09e-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: 51.08  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  21 GEDYYiatsTFEWFPGVRIYHSRDLKNWSLVSTPLDRVSMldmkGNPDSGG--IWAPCLSY--ADGKF--WLlytdvkiv 94
Cdd:cd18822   19 GENRD----NNNGFNGVSLYSSTDLVNWEFRNTVLTRDTC----SASELASckIERPKVIYnpKTGKFvmWA-------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  95 dsPWKNGRNY------LVTAPSIEGPWS---EPIPMGNGGFDPSLFHDDDGRKYYLyrpwgprhHSNPHNT-IVMQAFDP 164
Cdd:cd18822   83 --HWENGKDYglaraaVATSDTPDGDYTfhgSFRPLGYDSRDMTLFVDDDGTAYLI--------SAANDNAdLNIYRLTP 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 556491238 165 QTGTLSPERKTLFTGTplcYTEGAHLYRHAGWYYLM 200
Cdd:cd18822  153 DYLSVDSLVATLFKGQ---HREAPALVKRNGYYYLF 185
GH43_XylA-like cd18620
Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium ...
44-263 1.33e-06

Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), 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. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) 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.


Pssm-ID: 350132 [Multi-domain]  Cd Length: 274  Bit Score: 49.90  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  44 DLKNWSLVSTPLDrvSMLDMKGNPDSGGI-WAPCLSYADGKFWLLYT-------DVKIVDSPWKNGRNYlvtapsieGPW 115
Cdd:cd18620   40 DLSNWRYHGVIFR--SDQDPDEVPPGKGLlYAPDVVKGPGRYYLYYClskgsveGVAVSDSPAGPFEYL--------GPV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 116 SEPIPMGNGGFDPSLFHDDDGRkYYLYrpWGprhhsnphntivmqAFDPQTGTLSPERKTLFTGT----PLCYTEGAHLY 191
Cdd:cd18620  110 KYPRKGDIFQIDPAVLVDDDGR-VYLY--WG--------------QGGSKGAELDPDMLTIKPETivdvPAGITFEGHGF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 192 RHA-------GWYYL----MVAEGGTSYEHAVvvlrSKTIDGPYE----LHPEVTMMTSWhlpENplqksGHGSLLQTHt 256
Cdd:cd18620  173 FEGssirkinGIYYLvyssISRGRPTELCYAT----SKSPLGPFTyggvIIDNGGCDPPS---GN-----NHGSIVEIN- 239

                 ....*..
gi 556491238 257 GEWYMAY 263
Cdd:cd18620  240 GQWYIFY 246
GH43_CtGH43-like cd08985
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
33-224 4.09e-06

Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; 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 (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: 350099 [Multi-domain]  Cd Length: 273  Bit Score: 48.48  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  33 WFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPDSGGIWAPCLSY--ADGKFWLLYTdvkivdspWKNGRNYLV---- 106
Cdd:cd08985   30 LSHGINCYSSTDLYNWRFEGLVLPASGVEVVRDISPGYVIERPKVLYnaRTRKYVMWFH--------LDNPNYGFAavgv 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 107 -TAPSIEGPWS---EPIPMGNGGFDPSLFHDDDGRKYYLYRPWgprhhsNPHNTIVMQAFDPQTGTLSpeRKTLFTGTPl 182
Cdd:cd08985  102 aTSDTPTGPFTfvrSFRPDGYPSRDMTLFQDPDGTAYLVRSTD------HNTDIGISRLSDDYLDTTG--ASSTFKGPK- 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 556491238 183 cyTEGAHLYRHAGWYYLMvAEGGTSYEHAVVVL-RSKTIDGPY 224
Cdd:cd08985  173 --REAPALFKRGGTYYLI-TSGLTGWNPNPSRLaRADSPLGPW 212
GH43_XynD-like cd09003
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ...
10-142 4.96e-06

Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as 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. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. 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: 350117 [Multi-domain]  Cd Length: 315  Bit Score: 48.41  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  10 GFNPDPSLCRQGEDYYIATStfewfpgVRIYHSRDLKNWSlvstplDRVSMLDMKGNPDS---GGIWAPCLSY----ADG 82
Cdd:cd09003   29 DQQYNANGKKKDNSYYNINS-------LTVISSDDMVNWT------DHGEIPVAGPNGIAkwaGNSWAPSVAYkninGKD 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556491238  83 KFWLLYTDvkivdspwkNGRNY-LVTAPSIEGPWSEPI--PM------GNGG----FDPSLFHDDDGRKyYLY 142
Cdd:cd09003   96 KFYLYFAN---------GGGGIgVLTADSPTGPWTDPLgkPLitrstpGCAGvvwlFDPAVFIDDDGQG-YLY 158
COG3940 COG3940
Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism];
5-152 1.94e-05

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


Pssm-ID: 443140 [Multi-domain]  Cd Length: 309  Bit Score: 46.73  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   5 NPILTGfNPDPSLCRQGEDYYIATSTfeWFPGVRIYHSRDLKNWSlvsTPLDRVSMLDMKGNPDSGGIWAPCLSYADGKF 84
Cdd:COG3940    1 NPLIEQ-GADPWVYKHDGYYYFTATV--EYDRIVLRRSKTLAGLA---TAEPVVVWTPPASGPMSKNIWAPELHFIDGKW 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556491238  85 WLLYTDVKIVDSPWkNGRNYLVTAPS---IEGPWSE--PIPMGNGGF--DPSLFhDDDGRKYYLYRPW--GPRHHSN 152
Cdd:COG3940   75 YIYFAAGDGEDNNF-NHRMYVLENASadpLTGPWTEkgQIKTPWDSWaiDATVF-EHNGKLYLVWSGWegDINGNQN 149
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
42-144 2.45e-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: 46.05  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  42 SRDLKNWSLVSTPLDRVSmldmKGNPDSGGIWAPCLSYADGKFWLLYTDVKIVDSPWKNGRNYLVTAPSIEGPW--SEPI 119
Cdd:cd08772   32 SKDLIHWEEEPPAIVARG----GGSYDTSYAFDPEVVYIEGTYYLTYCSDDLGDILRHGQHIGVAYSKDPKGPWtrKDAP 107
                         90       100       110
                 ....*....|....*....|....*....|.
gi 556491238 120 PMGNGGF------DPSLFHDDDGRKYYLYRP 144
Cdd:cd08772  108 LIEPPNAyspknrDPVLFPRKIGKYYLLNVP 138
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
4-142 2.60e-05

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: 46.07  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238   4 TNPILTGFNP-----DPSLCRQGED---YYIAT-------STFEWFPGVRIYHSRDLKNWSlvstpldRVSMLDMKGNPD 68
Cdd:cd08983    5 GNPVLTSTVGtkgvrDPFIIRGPEDgkfYLVATdlwiaggAQWNGSRGIGVWESTDLVNWS-------EQRLVKMVSPPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  69 SGGIWAPCLSY--ADGK---FW--------------LLYT----------------------DVKIVdspWKNGRNYLV- 106
Cdd:cd08983   78 AGNAWAPEAIYdpETGQyvvYWssslygdggggnhrIYYAttkdfktfsepkvlfdpgfnviDTTIV---KDGGTYYRFy 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556491238 107 ------------TAPSIEGPWSEPIPMGNGGFD-----PSLFHDDDGRKYYLY 142
Cdd:cd08983  155 kdettgkgirlaTSDSLTGPWTTVTTGGGAGTGggvegPTVFKLNDGGKWYLY 207
GH43_CoXyl43_like cd18619
Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase ...
73-224 9.71e-05

Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), 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. Included in this subfamily is the metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43, which 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: 350131 [Multi-domain]  Cd Length: 313  Bit Score: 44.60  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  73 WAPCLSYADGKFWLlYTDVKIVDSPWKNGrnyLVTAPSIEGPW---SEPIPmGNGGFDPSLFHDDDGrKYYLYRP--WGP 147
Cdd:cd18619   78 WAPDAAEKDGKYYL-YFPAKDKDGIFRIG---VAVSDKPEGPFkpePEPIK-GSYSIDPAVFVDDDG-SYYLYFGgiWGG 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 148 RHHSNPHNTIVMQAFD-PQTGT---------LSPERKTLFT-----------GTPLC-------YTEGAHLYRHAGWYYL 199
Cdd:cd18619  152 QLQRWQTGSYVSGDGDePQDDEpalgpriakLSPDMLSFAEppreivildedGKPLLagdhdrrFFEGPWMHKYNGKYYL 231
                        170       180
                 ....*....|....*....|....*
gi 556491238 200 MVAEGGTsyeHAVVVLRSKTIDGPY 224
Cdd:cd18619  232 SYSTGDT---HLLVYATSDNPYGPF 253
GH43_LbAraf43-like cd18820
Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis ...
13-145 5.08e-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: 42.13  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  13 PDPSLCRQGEDYYIATSTFewfPGVRIYHSRDLKNWS-----LVSTPldrvsmldmKGNPDSGGIWAPCLSYADGKFWLL 87
Cdd:cd18820    1 ADPWVVYHDGYYYLTFTTG---DRITIWKSKTLTGLGtaepkVVWTP---------PDPSRSCNIWAPELHFIDGRWYIY 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556491238  88 YT-DvkivDSPWKNGRNYLV---TAPSIEGPWSE--PIPMGNGGF--DPSLFhDDDGRKYYLYRPW 145
Cdd:cd18820   69 YAaD----DGDNANHRMYVLesaSDDPPLGPYTFkgRLADPTDKWaiDGTVL-EHNGKLYFVWSGW 129
GH43_RcAra43A-like cd18823
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ...
20-224 7.34e-04

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: 41.57  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  20 QGEDYYIATSTFE--WFPGVRIYHSRDLKNWSLVSTPLDRVSMLDMKGNPdSGGIWA--PCLSY-ADGKFWLLYTDVKiv 94
Cdd:cd18823   24 GAVTYAANTKKNSdtSFKSVTLYSSTDLVNWTFEGNVLTASGAVDTAGDF-AGAGWVgrPGVAYnSATGKYVLLIQWG-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  95 DSPWKNGRNYLVTAPSIEGP--WSEPIPM-----GNGGFDPSLFHDDDGRKYYLYrpwgprhhSNPHNTIVMQAFDPQTG 167
Cdd:cd18823  101 STGNGRNGVLFATSDSPTGPftYQRVQPMidnvgTNNTGDQTSFFDDDGKAYLVY--------SNDRGRGSLYIAKLRSD 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556491238 168 TLSPERKTLFTGTPLCYTEGAHLYRHAGWYYLmvAEGGTSYEHAVV--VLRSKTIDGPY 224
Cdd:cd18823  173 YLGIEPAVRIDNYVGPGREGNALFKYGGTYYL--CASDLHGWNASQtyYMVATSLTGPY 229
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
34-225 3.33e-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: 39.70  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238  34 FPGVRIYHSRDLKNWSLVSTPLDRVSmldmkGNPDSGGIWAP--CLSYADGKFWLLYtdvkivDSPWKNGRNYLVTAPSI 111
Cdd:cd18824   34 FCGFVVYSSVDLVNWTYRGVLFDPNT-----CAGSPGVCFRPhvVYNARTGRYVLWY------NAYDGSSGYAVATSSTP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556491238 112 EGPW---SEPIPMGNGGF--DPSLFHDDDGRKYYLYRPWgprhhsnphntivmqafdPQTGTLSPERKT--LFTGTPLCY 184
Cdd:cd18824  103 TGPFvtvPDPVLAPAGLQagDFSLFVDDDGTGYLAYTTI------------------DFPQSIVVEQLTddYLNTTGEYV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556491238 185 -------TEGAHLYRHAGWYYLMVAE------GGTSyehaVVVLRSKTIDGPYE 225
Cdd:cd18824  165 rdlidqeAEAPSIFKRNGIYYILASNtccgccQGTG----ARVYRATSPLGPWT 214
 
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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