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Conserved domains on  [gi|1467206167|gb|RGP23054|]
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glycoside hydrolase family 43 protein [Bacteroides sp. AF39-10AT]

Protein Classification

glycoside hydrolase family 43 protein( domain architecture ID 14440559)

glycoside hydrolase family 43 (GH43) protein such as alpha-L-arabinofuranosidase and beta-D-xylosidase, which hydrolyzes monosaccaride residues from the non-reducing termini of substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
71-366 9.47e-159

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: 455.04  E-value: 9.47e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTNGeGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGQHVSGGIFAPAISYnpH 150
Cdd:cd18617     1 NPILPGFYPDPSICRVG-DDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQL-DLRGVPSSGGIFAPTIRY--H 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 151 NKTYYMVTTNV---GAGNFFVKTQDPFGEWSDPIMLPEVtGIDPSFFFDEDGKAYLVNNDDAPDNkpeYSGHRTIRVQEF 227
Cdd:cd18617    77 DGRFYIITTNVstdGRGNFIVTADDPAGPWSDPVWLDGP-GIDPSLFFDDDGKVYLTGTGPPPDP---YEGHGGIWQQEI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 228 DVNADKTVGPRKILVNKGarpeDKPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQRQ 307
Cdd:cd18617   153 DLETGKLLGEPKVLWNGG----TGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGPYEPCPNNPILTHRH 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 308 LDAerpNPVTCAGHADLVQTREGDWWAVFLACRPINNTFENLGRETFMMPVKWSEDGFP 366
Cdd:cd18617   229 LGS---NPVQNTGHADLVEDPDGSWWAVFLGVRPYGGGFHNLGRETFLAPVEWEDGWPV 284
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
399-576 2.64e-43

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: 153.58  E-value: 2.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 399 DGFDGQTLGMEWMTLRAPATG-LYSLSQTPGYLTLKCDSvSASEKKVPAFICRRLQHHKFECSTRMLFCPQSKAEQAGIL 477
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDEsWYSLTERPGYLRLYGRE-SLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 478 LFKDEKHQYFLAVGRDDQGE-CISLRQIGDGESKML---ASVRLDDGGVLTDLKVVSRGTHYDFYYARQEAVWNVLCRNV 553
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGrVLRLVRCDNGELTEElaeEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180
                  ....*....|....*....|....*
gi 1467206167 554 DAGYLST--ATAGGFTGTTIGMYAT 576
Cdd:pfam17851 161 DASILSDeyAAGGGFTGAFVGLYAT 185
 
Name Accession Description Interval E-value
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
71-366 9.47e-159

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: 455.04  E-value: 9.47e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTNGeGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGQHVSGGIFAPAISYnpH 150
Cdd:cd18617     1 NPILPGFYPDPSICRVG-DDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQL-DLRGVPSSGGIFAPTIRY--H 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 151 NKTYYMVTTNV---GAGNFFVKTQDPFGEWSDPIMLPEVtGIDPSFFFDEDGKAYLVNNDDAPDNkpeYSGHRTIRVQEF 227
Cdd:cd18617    77 DGRFYIITTNVstdGRGNFIVTADDPAGPWSDPVWLDGP-GIDPSLFFDDDGKVYLTGTGPPPDP---YEGHGGIWQQEI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 228 DVNADKTVGPRKILVNKGarpeDKPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQRQ 307
Cdd:cd18617   153 DLETGKLLGEPKVLWNGG----TGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGPYEPCPNNPILTHRH 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 308 LDAerpNPVTCAGHADLVQTREGDWWAVFLACRPINNTFENLGRETFMMPVKWSEDGFP 366
Cdd:cd18617   229 LGS---NPVQNTGHADLVEDPDGSWWAVFLGVRPYGGGFHNLGRETFLAPVEWEDGWPV 284
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
62-410 3.30e-104

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 318.04  E-value: 3.30e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  62 PLPGDDYFYNPILPGWYSDPSICTNGeGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLVNmegqHVSGGIF 141
Cdd:COG3507    15 AAALGNTYTNPVLPGDYPDPSIIRVG-DTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQWAD----PYSGGIW 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 142 APAISYnpHNKTYYMVTTNV-----GAGNFFVKTQDPFGEWSDPIML--PEVTGIDPSFFFDEDGKAYLVNNddapdnkp 214
Cdd:COG3507    90 APDIRY--HNGKYYLYYTAVdggknRSGIGVATADDPEGPWSDPGPLvcPGGNGIDPSVFVDDDGKAYLVYG-------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 215 eySGHRTIRVQEFDVNADKTVGPRKILVNKGarpedKPIWIEGPHLYKINGNYFLMSAEGGTAGW-HSEVIFRGDSPTGK 293
Cdd:COG3507   160 --SGGGGIYVAELDPDTGKLLGEPKTLAPGG-----EGGWIEGPHIYKRNGYYYLFYSEGGTCNSgYAVRVARSKSPTGP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 294 FIPWKNNPILTQRqldaeRPNPVTCAGHADLVQTREGDWWAVFLACRPINntfeNLGRETFMMPVKWSEDGFPYMTQGDD 373
Cdd:COG3507   233 YEDAPGNPILTQR-----SDGGIQGPGHGSLVETPDGEWYLVYHAYRPPG----GLGRETFLDPVTWNEDGWPVVGPGTG 303
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1467206167 374 LVPVIVRREGVkrdesatfgnfemnDGFDGqTLGMEW 410
Cdd:COG3507   304 EPPQPLPAPES--------------DDFDG-PLGLQW 325
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
69-366 9.85e-96

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: 293.84  E-value: 9.85e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  69 FYNPILPGWYSDPSICTNGEgDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGqhvSGGIFAPAISYn 148
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGD-DYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQL-SGRG---SNASWAPDISY- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 149 pHNKTYYMVTTNVGAGNFFVKTQDPFGEWSDPIMLPEVT-GIDPSFFFDEDGKAYLVNNddapdNKPEYSGHRTIRVQEF 227
Cdd:pfam04616  75 -HDGKYYLYYTAVAHGIFVATADSPDGPWSDPGKLKSGGgGIDPSLFHDDDGKKYLVWG-----GWDPRHGHGGIYLQEL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 228 DVNADKTVGPRKILVNKGARPEDkPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQRQ 307
Cdd:pfam04616 149 DNDGLKLVGPVTKLIYPGTRWVG-GKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSRS 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 308 ldaeRPNPVTCAGHADLVQTREGDWWAVFLACRPINNtFENLGRETFMMPVKWSEDGFP 366
Cdd:pfam04616 228 ----PENPIYGPGHASLVETPDGEWWIVYHAGRPGDG-GYGLGRETRIQPVEWRADGWP 281
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
399-576 2.64e-43

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: 153.58  E-value: 2.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 399 DGFDGQTLGMEWMTLRAPATG-LYSLSQTPGYLTLKCDSvSASEKKVPAFICRRLQHHKFECSTRMLFCPQSKAEQAGIL 477
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDEsWYSLTERPGYLRLYGRE-SLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 478 LFKDEKHQYFLAVGRDDQGE-CISLRQIGDGESKML---ASVRLDDGGVLTDLKVVSRGTHYDFYYARQEAVWNVLCRNV 553
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGrVLRLVRCDNGELTEElaeEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180
                  ....*....|....*....|....*
gi 1467206167 554 DAGYLST--ATAGGFTGTTIGMYAT 576
Cdd:pfam17851 161 DASILSDeyAAGGGFTGAFVGLYAT 185
 
Name Accession Description Interval E-value
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
71-366 9.47e-159

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: 455.04  E-value: 9.47e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTNGeGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGQHVSGGIFAPAISYnpH 150
Cdd:cd18617     1 NPILPGFYPDPSICRVG-DDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQL-DLRGVPSSGGIFAPTIRY--H 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 151 NKTYYMVTTNV---GAGNFFVKTQDPFGEWSDPIMLPEVtGIDPSFFFDEDGKAYLVNNDDAPDNkpeYSGHRTIRVQEF 227
Cdd:cd18617    77 DGRFYIITTNVstdGRGNFIVTADDPAGPWSDPVWLDGP-GIDPSLFFDDDGKVYLTGTGPPPDP---YEGHGGIWQQEI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 228 DVNADKTVGPRKILVNKGarpeDKPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQRQ 307
Cdd:cd18617   153 DLETGKLLGEPKVLWNGG----TGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGPYEPCPNNPILTHRH 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 308 LDAerpNPVTCAGHADLVQTREGDWWAVFLACRPINNTFENLGRETFMMPVKWSEDGFP 366
Cdd:cd18617   229 LGS---NPVQNTGHADLVEDPDGSWWAVFLGVRPYGGGFHNLGRETFLAPVEWEDGWPV 284
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
62-410 3.30e-104

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 318.04  E-value: 3.30e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  62 PLPGDDYFYNPILPGWYSDPSICTNGeGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLVNmegqHVSGGIF 141
Cdd:COG3507    15 AAALGNTYTNPVLPGDYPDPSIIRVG-DTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQWAD----PYSGGIW 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 142 APAISYnpHNKTYYMVTTNV-----GAGNFFVKTQDPFGEWSDPIML--PEVTGIDPSFFFDEDGKAYLVNNddapdnkp 214
Cdd:COG3507    90 APDIRY--HNGKYYLYYTAVdggknRSGIGVATADDPEGPWSDPGPLvcPGGNGIDPSVFVDDDGKAYLVYG-------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 215 eySGHRTIRVQEFDVNADKTVGPRKILVNKGarpedKPIWIEGPHLYKINGNYFLMSAEGGTAGW-HSEVIFRGDSPTGK 293
Cdd:COG3507   160 --SGGGGIYVAELDPDTGKLLGEPKTLAPGG-----EGGWIEGPHIYKRNGYYYLFYSEGGTCNSgYAVRVARSKSPTGP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 294 FIPWKNNPILTQRqldaeRPNPVTCAGHADLVQTREGDWWAVFLACRPINntfeNLGRETFMMPVKWSEDGFPYMTQGDD 373
Cdd:COG3507   233 YEDAPGNPILTQR-----SDGGIQGPGHGSLVETPDGEWYLVYHAYRPPG----GLGRETFLDPVTWNEDGWPVVGPGTG 303
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1467206167 374 LVPVIVRREGVkrdesatfgnfemnDGFDGqTLGMEW 410
Cdd:COG3507   304 EPPQPLPAPES--------------DDFDG-PLGLQW 325
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
69-366 9.85e-96

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: 293.84  E-value: 9.85e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  69 FYNPILPGWYSDPSICTNGEgDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGqhvSGGIFAPAISYn 148
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGD-DYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQL-SGRG---SNASWAPDISY- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 149 pHNKTYYMVTTNVGAGNFFVKTQDPFGEWSDPIMLPEVT-GIDPSFFFDEDGKAYLVNNddapdNKPEYSGHRTIRVQEF 227
Cdd:pfam04616  75 -HDGKYYLYYTAVAHGIFVATADSPDGPWSDPGKLKSGGgGIDPSLFHDDDGKKYLVWG-----GWDPRHGHGGIYLQEL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 228 DVNADKTVGPRKILVNKGARPEDkPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQRQ 307
Cdd:pfam04616 149 DNDGLKLVGPVTKLIYPGTRWVG-GKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSRS 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 308 ldaeRPNPVTCAGHADLVQTREGDWWAVFLACRPINNtFENLGRETFMMPVKWSEDGFP 366
Cdd:pfam04616 228 ----PENPIYGPGHASLVETPDGEWWIVYHAGRPGDG-GYGLGRETRIQPVEWRADGWP 281
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
71-368 6.57e-92

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: 284.05  E-value: 6.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTNGEgDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGQHVSGGIFAPAISYnpH 150
Cdd:cd09000     1 NPILPGFNPDPSICRVGD-DYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQL-DMRGNPDSGGIWAPCLSY--A 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 151 NKTYYMVTTNV--------GAGNFFVKTQDPFGEWSDPIMLPEVtGIDPSFFFDEDGKAYLVN--NDDAPDNKPeYSGhr 220
Cdd:cd09000    77 DGKFWLVYTDVksvdgpfkDVHNYLVTAESIEGPWSEPIYLNSS-GFDPSLFHDDDGRKYLVNmlWDHRPGHNR-FAG-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 221 tIRVQEFDVNADKTVGPRKILVnKGArpEDKpiWIEGPHLYKINGNYFLMSAEGGTaGW-HSEVIFRGDSPTGKFIPWKN 299
Cdd:cd09000   153 -IVLQEFDPETKKLVGERKVIF-KGT--ELG--LTEGPHLYKRDGYYYLLTAEGGT-GYeHAVTVARSRNIFGPYEVDPD 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 300 NPILTQRQLDAerpNPVTCAGHADLVQTREGDWWAVFLACRPINNT-FENLGRETFMMPVKWSEDGFPYM 368
Cdd:cd09000   226 NPLLTSWDDPE---NPLQKAGHGSLVETPDGEWYLAHLCGRPLPGRgRCPLGRETAIQKVEWTDDGWPRL 292
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
71-360 4.73e-87

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: 270.77  E-value: 4.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTNGEgDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLvNMEGQHVSGGIFAPAISYnpH 150
Cdd:cd08989     1 NPVLPGFHPDPSVVRVGD-DYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQL-DLTGGPDGGGIWAPDISY--H 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 151 NKTYYMVTTNV-------GAGNFFVKTQDPFGEWSDPIMLpEVTGIDPSFFFDEDGKAYLVNNddapdnkpeysgHRTIR 223
Cdd:cd08989    77 DGKFYIYYTVVlnvgswkGRRNYLVTSEDPEGPWSEPVWL-DEGGIDPSLFVDDDGKHYMLLN------------PGGIR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 224 VQEFDVNADKTVGPRKIL--VNKGARPedkpiwiEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNP 301
Cdd:cd08989   144 LAELNPDCTKQIGEPKRIweGTGGRAP-------EGPHLYKKDGYYYLLTAEGGTGYGHAITIARSKTIYGPYEPCPYNP 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 302 ILTQRQLDAerpnPVTCAGHADLVQTREGDWWAVFLACRPINNTFENLGRETFMMPVKW 360
Cdd:cd08989   217 ILRQQDPQA----PLQRCGHGKLVETPDGEWWMVYLCGRPLPGGYCPLGRETALAPVEW 271
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
71-366 3.29e-84

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: 264.11  E-value: 3.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSiCT---NGEGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQL--VNMEGQHVSGGIFAPAI 145
Cdd:cd18833     1 NPIIPGFHPDPS-CIfvpEWDGTFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSQLpeLATTGTGQQGGIWAPTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 146 SYnpHNKTYYMVTTNVGA--------GNFFVKTQDPF--GEWSDPIMLPeVTGIDPSFFFDEDGKAYLVNNDDApDNKPE 215
Cdd:cd18833    80 RY--HDGTFYVITTLVFPdktdasrwDNLLFTTTDPYsdSAWSDPIRFD-FPGYDPDLFWDDDGTAYVQGAHYW-RVRPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 216 ysghrtIRVQEFDVNADKTVGPRKILVNKGArpedkpIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFI 295
Cdd:cd18833   156 ------IQQQEIDLKTGESLSPSPIWNGTGG------SAPEGPHMYKKDGWYYLLIAEGGTGLGHSVTIARSRSIWGPYE 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1467206167 296 PWKNNPILTQRQLDaerpNPVTCAGHADLVQTREGDWWAVFLACR--PINNTFEnLGRETFMMPVKWSEDGFP 366
Cdd:cd18833   224 SYPSNPVLTNANTS----EYFQTVGHADLFQDANGNWWGVALATRsgPEYEIYP-MGRETVLYPVTWEEGEWP 291
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
71-369 7.97e-61

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


Pssm-ID: 350115 [Multi-domain]  Cd Length: 270  Bit Score: 202.36  E-value: 7.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTNGEgDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPS---QLVNMEGQHV-SGGIFAPAIS 146
Cdd:cd09001     4 NPVLWADYPDPDVIRVGD-TYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDdgdAYYLEDGKNAyGKGIWAPSLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 147 YnpHNKTYYMVTTNVGAGNFFVKTQDPFGEWSDPIMLPEVtGIDPSFFFDEDGKAYLVnnddapdnkpeySGHRTIRVQE 226
Cdd:cd09001    83 Y--HNGKFYVYFCTNTGGTYVYTADDPAGPWSRPALIGKG-YHDPSLLFDDDGKAYLV------------YGNGEIRLTE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 227 FDVNADKTVGPRKILVNKGarpeDKPIWIEGPHLYKINGNYFLMSAEGGtAGWHSEVIFRGDSPTGkfiPWKNNPILtqR 306
Cdd:cd09001   148 LSPDGTGVGGEGRVIIDGT----EEGLGAEGSHLYKINGYYYIFNIEWG-GGGRTQVVLRSKSLYG---PYEGRVVL--D 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1467206167 307 QLDAERPNPVTCAGhadLVQTREGDWWAV-FLACRPInntfenlGRETFMMPVKWsEDGFPYMT 369
Cdd:cd09001   218 DGSGTGDNGPHQGG---LVDTPDGEWWFMlFQDRGAV-------GRIPVLVPVTW-KDGWPVIG 270
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
69-368 3.05e-58

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: 195.52  E-value: 3.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  69 FYNPILPGWYSDPSICTNGEgDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPsqlvnmegqhvSGGIFAPAISYn 148
Cdd:cd09002     1 YLNPILAGDYPDPSILRDGD-DYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAALTEY-----------IGTVWAPDLIK- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 149 pHNKTYYMVTTNVGAGNFFVKTQDPFGEWSDPIMLPEVTGIDPSFFFDEDGKAYL-VNNDDapdnkpeysghrtiRVQef 227
Cdd:cd09002    68 -HDGRYYIYFPAKGGTNYVITADDIAGPWSEPIDLKVGSGIDPGHVVDEDGKRYLfLSGGR--------------RVR-- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 228 dVNAD--KTVGPRKILVNKGARPEDkpiWI------EGPHLYKINGNYFLMSAEGGTAG---WHSEVIFRGDSPTGkfiP 296
Cdd:cd09002   131 -LTDDglSVAGPPEKVYDGWRYPDE---WDvecfclEGPKLFRRGGYYYLTTAQGGTAGpptSHMVVSARSKSPHG---P 203
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1467206167 297 WKN---NPIL-TQRqldaeRPNPVTCAGHADLVQTREGDWWAVFLACRpinNTFENLGRETFMMPVKWSEDGFPYM 368
Cdd:cd09002   204 WENspyNPLVrTQS-----REEKWWSKGHGTLVEGPDGKWWMVYHGYE---NGYRTLGRQTLLEPVEWTADGWFRI 271
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
399-576 2.64e-43

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: 153.58  E-value: 2.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 399 DGFDGQTLGMEWMTLRAPATG-LYSLSQTPGYLTLKCDSvSASEKKVPAFICRRLQHHKFECSTRMLFCPQSKAEQAGIL 477
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDEsWYSLTERPGYLRLYGRE-SLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 478 LFKDEKHQYFLAVGRDDQGE-CISLRQIGDGESKML---ASVRLDDGGVLTDLKVVSRGTHYDFYYARQEAVWNVLCRNV 553
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGrVLRLVRCDNGELTEElaeEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180
                  ....*....|....*....|....*
gi 1467206167 554 DAGYLST--ATAGGFTGTTIGMYAT 576
Cdd:pfam17851 161 DASILSDeyAAGGGFTGAFVGLYAT 185
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
80-338 4.23e-36

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: 135.26  E-value: 4.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTnGEGDYFLAVSTFTYY--PGVPLFHSKDLVNWKQVGHILNRpsqlvNMEGQHVSGGIFAPAISYNPhNKTYYMV 157
Cdd:cd08978     2 DPSILK-DNGRYYIYATTDDTGtgTGIVVWKSKDLVNWKEEGTVLSR-----GKSKSWGTGNLWAPEVYYFN-SGKWYLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 158 TTNVGAG---NFFVKTQD----PFGEW-SDPIMLPEVTGIDPSFFFDEDGKAYLVNNDDapdnkpeySGHRTIRVQEFDV 229
Cdd:cd08978    75 YSAVPNGgggRIYVATSDspegPFTPIvSGKLGDRGSGSIDPTVFVDDDGKLYLYYGDE--------DDSGDIYVAELDP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 230 NADKTVGPRKILVNKGARPEDKPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQR-QL 308
Cdd:cd08978   147 DLLTIKGDVTLLIGEVVGSGFRGNYFEGPAVFKRNGYYYLIYSAGGTDGGYAIGYATSDSPLGPWEKASHNPGLQTSgAT 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1467206167 309 DAERPnpvtcaGHADLVQTREGDWWAVFLA 338
Cdd:cd08978   227 GIYGP------GHGSIFQDEGDRWYIVYHA 250
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
80-365 4.73e-25

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: 104.95  E-value: 4.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSI-CTNGEgdYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPsqlvnmeGQHVSGGIFAPAISYnpHNKTYYMVT 158
Cdd:cd08991     2 DPFVlKHNGT--YYLYGTGGDDGRGFKVYVSDDLVNWEYPGGALEEP-------GLWGTKGFWAPEVFY--YNGKFYMYY 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 159 TNVGAGNFF---VKTQD----PFGEWSDPIMLPEVTGIDPSFFFDEDGKAYL--VNNDDapDNKPEYSghrtIRVQEFDv 229
Cdd:cd08991    71 SANGGDHGEhiaVAVSDsplgPFRDKGKLLIPAGGFSIDAHVFIDDDGKWYLyyVRDDL--GGEPGNR----IYVAELE- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 230 NADKTVGPRKILVNKGA--RPEDKPI----WIEGPHLYKINGNYFLM-SA-----EG---GTAgwhsevifRGDSPTGKF 294
Cdd:cd08991   144 DDLSLIGEPTLVLCPTAdeRWEYGEGrdwhTTEGPTVLKHNGTYYLTySAnhfrsPDyavGYA--------TADSPLGPW 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1467206167 295 IPWKNNPILTQRQLDAERPnpvtcaGHADLVQTREGDWWAVFLAcrpINNTFENLGRETFMMPVKWSEDGF 365
Cdd:cd08991   216 TKYEGNPILSRNDGGVNGP------GHNSVFKDPDGDLYIVYHT---HDSDETVEPRKMRIDRLRFDGDKL 277
GH43-like cd08982
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
80-367 9.66e-23

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: 98.79  E-value: 9.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSIcTNGEGDYFLAVSTFTYYpgvplFHSKDLVNWKQVghilnRPSQLVNMEgqhvsggiFAPAISynPHNKTYYMVTT 159
Cdd:cd08982     7 DPTV-VLFKGKYYLFASKSGGY-----WHSDDLVNWKFI-----PTNGLPIED--------YAPTVV--EINGTLYFTAS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 160 NvGAGNFFvKTQDPFGEW------SDPIMLpevtgIDPSFFFDEDGKAYLvnnddapdnkpeYSGHR---TIRVQEFDVN 230
Cdd:cd08982    66 G-GPGPIY-RTDDPLGGKwelvaeSGPFGF-----WDPALFVDDDGRLYL------------YWGCSnkdPIYGVELDPN 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 231 AD-KTVGPRKILVN----------KGAR---PEDKPiWIEGPHLYKINGNYFLMSAEGGTAG-WHSEVIFRGDSPTGKFI 295
Cdd:cd08982   127 TGfRPIGEPVPLISfdpdkhgwerFGEDnedPGLAP-WIEGAWMTKHNGKYYLQYAAPGTEFkTYADGVYVSDSPLGPFT 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1467206167 296 PWKNNPILtqrqldaERPNP-VTCAGHADLVQTREGDWWAVFLACRPINNTFEnlgRETFMMPVKWSEDGFPY 367
Cdd:cd08982   206 YAPNNPFS-------YKPGGfITGAGHGSTFQDKYGNYWHFGTMVISVNHNFE---RRIGLFPAGFDKDGELY 268
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
77-336 2.30e-22

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: 96.53  E-value: 2.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  77 WYSDPSICTNGEGDYFLAVST-----FTYYPGVPLFHSKDLVNWKQVGHI--LNRPS--QLVNMEGQHVSG---GIFAPA 144
Cdd:cd08986     1 WLRDPYITLGPDGYYYLTGTTggpdwWGVNDGIRLWRSKDLKDWEYLGLVwdLEKDGwwQWEPQWWTPDSKnkrALWAPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 145 ISYNphNKTYYMV-TTNVGAGNFFV-KTQDPFGEWSDPIMLPEVTGIDPSFFFDEDGKAYLVNNDDapdnkpeysghrti 222
Cdd:cd08986    81 IHYI--NGTWYIThSMNGGGTGLLKsTTGKPEGPYVDPMGGPLGKGIDPSLFEDDDGTVYLVWGNG-------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 223 RVQEFDVNADKTVG-PRKILVNKgarpeDKPIWIEGPHLYKINGNYFLMSaeggtAGWHSEVIFRG---------DSPTG 292
Cdd:cd08986   145 QIARLKKDMSGFAEePRKIDPSG-----NREIGHEGAFIFKIGGKYVLFG-----AAWSTDKMRKGtydlyyatsDSIYG 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1467206167 293 kfiPWknnpiltqrqldAERPNPVTCAGHADLVQTREGDWWAVF 336
Cdd:cd08986   215 ---PY------------SERRFAGPHGGHGTPFKDKDGQWWCTA 243
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
71-363 1.11e-21

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: 95.29  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSICTngEGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGH----ILNRPSQlvnmegqhVSGGIFAPAIS 146
Cdd:cd08999     1 NPVIDGDFPDPSVIR--VGGTYYAFATNSGGKNVQVATSTDLVTWTLLGGdalpDLPAWAA--------AGGNTWAPDVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 147 YNPhNKTYYM-----------------VTTNVgagnffvktQDPFGEWSDPIMLPEVTG--IDPSFFFDEDGKAYLVNND 207
Cdd:cd08999    71 RRP-DGKYVMyysarlkssgkhcigvaTSDSP---------LGPFTPVGEPPLCPLDQGgaIDPSGFVDPDGKRYLVYKV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 208 DAPDNkpeysGHRT-IRVQEfdVNAD---KTVGPRKILVNKGarPEDKPIwIEGPHLYKINGNYFLMSAEGGTAGWHSEV 283
Cdd:cd08999   141 DGNSI-----GVPTpIMLQE--LSADgltLVGEPVELLLNDG--PWDGPL-VEAPSLVKRDGTYYLFYSSNCYCSPSYAV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 284 IF-RGDSPTGKFIPWKNNPILTqrqldaeRPNPVTCAGHADLVQTrEGDWWAVFLACRPINNTFenLGRETFMMPVKWSE 362
Cdd:cd08999   211 GYaTSKSITGPYTKAGEPLLLT-------GDGGLTGPGGADVVED-DGGDWMVFHAWDGGDDVG--GGRAMYTAELTWEG 280

                  .
gi 1467206167 363 D 363
Cdd:cd08999   281 G 281
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
80-338 2.43e-16

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: 79.48  E-value: 2.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTngEGDYFLAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLVNMEGQHVSGGIFAPAISYnpHNKTYYMVTT 159
Cdd:cd08988     2 DPSIIK--EGGTYYAFGTGTDGFGIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGNLWAPDISQ--HKGKYYLYYS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 160 NVGAGNFF--------VKTQDPFgeWSDPIMLPEVTG------IDPSFFFDEDGKAYLVNNDDapdnkpeysgHRTIRVQ 225
Cdd:cd08988    78 VSDNGSNTsaiglataNNPQGPF--KDEGPAKPVVTSdnagnaIDPDLFQDEDGQNWLLYGSF----------WGGIWLQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 226 EFDVNADKTVGP---RKILVNKGARpedkpiwIEGPHLYKINGNYFLMS-----AEGGTAGWHSEViFRGDSPTGKFIPW 297
Cdd:cd08988   146 KLDKNGLVVNPPgngKSIAVLYYVS-------IEAPYITYAGGYYYLFVsagscCDGGNSTYHTRV-GRSKKVTGPYLDK 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1467206167 298 KNNPIL-TQRQLDAERPNPVTCAGHADLVQTREGDWWAVFLA 338
Cdd:cd08988   218 GGLDMLeGGGTLLTKGKNQWVGPGHNSIVTGDNGVDYLVLHA 259
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
71-360 1.44e-14

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: 74.53  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYSDPSIcTNGEGDYFLAVSTFTYYPG------VPLFHSKDLVNWKQVGHILNRPSQLVNMEGqhvsGGIFAPA 144
Cdd:cd18616     1 NPVFEPTFADPTV-IRGDDGYFYAYATEDPWGDgggfrlVPILRSKDLVNWEYVGDAFTSKPRWKWDPG----GGLWAPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 145 ISYnpHNKTYYM--VTTNVGAGNFF---VKTQD-PFGEWSDPIML--PEVTG----IDPsFFFDEDGKAYLVnnddapdn 212
Cdd:cd18616    76 IRY--IDGKYVLyySLSDWGADPNPgigVATADsPAGPFTDQGKLfdSNEIGvrnsIDP-FVFEDDGKKYLF-------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 213 kpeYSGHRTIRVQEfdVNADKT--VGPRKILVnKGARpedkpiwIEGPHLYKINGNYFLM-SA----EGGTAGWHSEViF 285
Cdd:cd18616   145 ---WGSFYGIYAVE--LTADGLalKPGEKVQI-AGDR-------YEGPYIVKRDGYYYLFgSAgsccEGPNSTYRVVV-G 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 286 RGDSPTGKFIPWKNNPILTQR----QLDAERPNPVTCAGHADLVQTREGDWWAVFLACRPINNTFENL--GRETFMMPVK 359
Cdd:cd18616   211 RSESLLGPYVDRDGRSLLDSGgggtPVVLQNGNRFVGPGHNAVITDDAGQDWMLYHAYDRNDPYLPGGynRRPLLLDRLD 290

                  .
gi 1467206167 360 W 360
Cdd:cd18616   291 W 291
GH43_F5-8_typeC-like cd18608
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ...
78-304 1.27e-13

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: 71.54  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  78 YSDPSICTNGeGDYFLAVSTFTYY------PGVplFHSKDLVNWKQVGhiLNRPSQLVnmegqhvSGG--IFAPAISYNP 149
Cdd:cd18608     1 FADPSIVKFG-GTYYLYATTDGWGgfnsgePVV--WKSKDFVNWKFEG--LNWPTKAA-------SGDskVWAPSVVKGK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 150 hNKTYYMVTTnVGAGNFFVKTQDPFGEWSD----------PIMLPEVTGIDPSFFFDEDGKAYLVNNDDAPDNkpeysGH 219
Cdd:cd18608    69 -DGKYYMYVS-VGSEIYVGVADSPLGPWKNangdgppiipGDGKPNYHMIDAEPFIDDDGKAYLYWGSGLHVN-----GH 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 220 RtiRVQEFDVNADKTVGPRKILVNkgarpedKPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIFR-GDSPTGKFIPWK 298
Cdd:cd18608   142 C--FAAKLNPDMVTFDGSEPTIVT-------PRDYFEAPFMFKRNGIYYLMYSGGGCWDETYNVRYAvSDNPLGPFEEGE 212

                  ....*.
gi 1467206167 299 NNPILT 304
Cdd:cd18608   213 NSPILQ 218
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
80-270 8.60e-13

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: 68.73  E-value: 8.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTNGEGDYFLavstFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLVNMEGQHVSGGIFAPAISYnpHNKTYYM--- 156
Cdd:cd08998     3 DPSIIKDDGGTYYV----FSTGAGIQIRTSKDLVNWEFVGTVFPEGPAWAAAEVPGGAGGLWAPDVVY--VNGRYYLyys 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 157 VTTNvGAGN---FFVKTQDP-FGEWSDPIMLPEVTG------IDPSFFFDEDGKAYLVnnddapdnkpeY----SGhrtI 222
Cdd:cd08998    77 ASTF-GSNRsaiGLATSTTLdDGPWTDQGLVVSSSPgddynaIDPNVFVDADGRLWLA-----------YgsfwGG---I 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1467206167 223 RVQEFDVN--ADKTVGPRKILVNKGARPEDkpiwIEGPHLYKINGNYFLM 270
Cdd:cd08998   142 KLVELDPAtgKLRPGSTGTSIASRPGGPGA----IEAPYIIYRGGYYYLF 187
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
106-298 1.39e-12

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: 68.01  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 106 LFHSKDLVNWKQVGHILnrPSQLVNMEGqhvSGGIFAPAISYnpHNKTYYMVTTNVGAGNFF---VKTQD-PFGEWSDPI 181
Cdd:cd08990    34 VFSSTDLVNWTDHGEIL--PPDDVFWWA---SGNAWAPDAVY--KNGKYYFYFPVGQASDGFgigVAVSDsPAGPFKDAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 182 -------MLPEVTGIDPSFFFDEDGKAYLVnnddapdnkpeYSGHRTIRVQEFDVNADKTVGPRKILVNKGARPedkpiW 254
Cdd:cd08990   107 gkplipeGLNGIEGIDPAVFVDDDGRAYLY-----------FGGGGGYYVAKLKDDMISLAGEPQKIKNGGLKG-----F 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1467206167 255 IEGPHLYKINGNYFLMSAeGGTAGWHSEVIFRGDSPTGkfiPWK 298
Cdd:cd08990   171 FEAPWVFKRNGTYYLSYA-GGWAYPAEIAYSTADSPLG---PYT 210
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
107-364 1.46e-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: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 107 FHSKDLVNWKQVGHILNrpsqlvnMEGQH-VSGGIFAPAISYnpHNKTYYMVttnVGAGNFFVKTQD----------PFG 175
Cdd:cd18827    31 FSSPDLVHWTKHERILD-------MADVPwANRAVWAPSVIE--KNGKYYLY---FAANDIQSDDEGggigvavadrPEG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 176 EWSD----PIMLPEVTG---IDPSFFFDEDGKAYLVnnddapdnkpeYSGHRTIRVQEfdVNADKT---VGPRKILvNKG 245
Cdd:cd18827    99 PFKDalgkPLIGEFHNGaqpIDQHVFKDDDGQAYLY-----------YGGWGHCNVAK--LNDDMTslvPFDDGET-FKE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 246 ARPEDkpiWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIF-RGDSPTGkfiPWKNNPILTQRQldaerPNPVTCAGHADL 324
Cdd:cd18827   165 ITPEG---YVEGPFMFKRNGKYYFMWSEGGWTGPDYSVAYaVADSPLG---PFKRIGKILQQD-----PAIATGAGHHSV 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1467206167 325 VQTREGDWWAVFLACRPINNTFENLgRETFMMPVKWSEDG 364
Cdd:cd18827   234 VNVPGTDDWYIVYHRRPLGETDGNH-RVVCIDRMEFNEDG 272
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
80-333 2.04e-11

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: 64.55  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTNGeGDYFLavstftyYP---GVP--------LFHSKDLVNWKQVGHILNRpsQLVNMEGQHvsgGIFAPAIsyN 148
Cdd:cd09004     2 DPDIVVFG-GRYYI-------YPttdGPPgwsstsfhVFSSTDLVNWTDHGIILDL--ANDVWWANK---GAWAPAV--A 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 149 PHNKTYYM---VTTNVGagnffVKTQD-PFGEWSD---PImlpeVTG-------IDPSFFFDEDGKAYLvnnddapdnkp 214
Cdd:cd09004    67 ERNGKYYFyfsAGSQIG-----VAVSDsPTGPFTDlgrPL----VTGgdyggqaIDPMVFVDDDGQAYL----------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 215 eYSGHRTIRVQEfdVNADKTVGPRKILVNkgarpEDKPIWIEGPHLYKINGNYFLMSAEGGTAGWHSEVIF-RGDSPTGk 293
Cdd:cd09004   127 -YWGNGTAYVAR--LNDDMVSFDGEVVVS-----ITPPNFREGPFVHKRNGIYYLSWSENDTRDPDYRVRYaTSDSPLG- 197
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1467206167 294 fiPWKNNPILTQRQLDAerpnPVTCAGHADLVQTREGDWW 333
Cdd:cd09004   198 --PWTYRGVGLLLDSAG----GIKGTGHHSIVQVPGTDEW 231
GH43_CtGH43-like cd08985
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
103-302 8.05e-10

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: 60.04  E-value: 8.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 103 GVPLFHSKDLVNWKQVGHILnRPSQLVNMEGQHVSGGIFAPAISYNPHNKTYYMVTTNVGAGNFF----VKTQD----PF 174
Cdd:cd08985    33 GINCYSSTDLYNWRFEGLVL-PASGVEVVRDISPGYVIERPKVLYNARTRKYVMWFHLDNPNYGFaavgVATSDtptgPF 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 175 GEWSDPIMLPEVTGiDPSFFFDEDGKAYLVNNDDAPDNkpeysghrtIRVQEFDVNADKTVGPRKILVNKGArpedkpiw 254
Cdd:cd08985   112 TFVRSFRPDGYPSR-DMTLFQDPDGTAYLVRSTDHNTD---------IGISRLSDDYLDTTGASSTFKGPKR-------- 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1467206167 255 iEGPHLYKINGNYFLMSaeGGTAGW---HSEvIFRGDSPTGKFIPWKNNPI 302
Cdd:cd08985   174 -EAPALFKRGGTYYLIT--SGLTGWnpnPSR-LARADSPLGPWSTWGNLPV 220
GH43_XynD-like cd09003
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ...
71-269 8.60e-10

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: 60.35  E-value: 8.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  71 NPILPGWYS-DPS----------ICTNGEGDYFLAVSTF--TYY--PGVPLFHSKDLVNWKQVGHILNRPSQLVNMEGQH 135
Cdd:cd09003     1 NPIISHRFGaDPTalvyngrvyvYGTNDDQQYNANGKKKdnSYYniNSLTVISSDDMVNWTDHGEIPVAGPNGIAKWAGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 136 vsggIFAPAISYNPHNKT--YYMVTTNVGAGNFFVKTQDPFGEWSDPIMLPEVTG-----------IDPSFFFDEDGKAY 202
Cdd:cd09003    81 ----SWAPSVAYKNINGKdkFYLYFANGGGGIGVLTADSPTGPWTDPLGKPLITRstpgcagvvwlFDPAVFIDDDGQGY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 203 LV---NNDDAPDNKPeysghRTIRVQEfdvnadktVGPRKILVNKGARPEDKPIWIEGPHLYKINGNYFL 269
Cdd:cd09003   157 LYfggGVPGGSEANP-----KTARVIK--------LGDDMISVDGSAVTIDAPYFFEASGINKINGKYYY 213
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
77-320 1.95e-09

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: 58.96  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  77 WYSDPSICTNGEGDYFLAVstftyypGVPLFHSKDLVNWKQVGHILNRPSqlvnmeGQHVSGGIFAPAISYNPHNKTYYM 156
Cdd:cd18824    17 WYGTPYGCGCGSCGFTLFC-------GFVVYSSVDLVNWTYRGVLFDPNT------CAGSPGVCFRPHVVYNARTGRYVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 157 -VTTNVGAGNFFVKTQD----PFGEWSDPIMLPEVTGI-DPSFFFDEDGKAYLVNNDDapdnkpeySGHRTIRVQEFDVN 230
Cdd:cd18824    84 wYNAYDGSSGYAVATSStptgPFVTVPDPVLAPAGLQAgDFSLFVDDDGTGYLAYTTI--------DFPQSIVVEQLTDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 231 ADKTVGPrkilvnkgARPEDKPIWIEGPHLYKINGNYFLMSAE------GGTAGwhseVIFRGDSPTGkfiPWKNNPILT 304
Cdd:cd18824   156 YLNTTGE--------YVRDLIDQEAEAPSIFKRNGIYYILASNtccgccQGTGA----RVYRATSPLG---PWTRQIDIN 220
                         250
                  ....*....|....*...
gi 1467206167 305 QR--QLDAERPNPVTCAG 320
Cdd:cd18824   221 SCagALFPPSDSAYTCGG 238
GH43_RcAra43A-like cd18823
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ...
103-281 2.27e-09

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: 58.90  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 103 GVPLFHSKDLVNWKQVGHILNRPSQLVNMEGQHVSGGIFAPAISYNPHNKTYYMV-----TTNVGAGNFFVKTQDP---- 173
Cdd:cd18823    42 SVTLYSSTDLVNWTFEGNVLTASGAVDTAGDFAGAGWVGRPGVAYNSATGKYVLLiqwgsTGNGRNGVLFATSDSPtgpf 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 174 -FGEWSDPIMLPEVTGI-DPSFFFDEDGKAYLVNNDDapdnkpeySGHRTIRVQEFdvNADKTV---GPRKILVNKGARp 248
Cdd:cd18823   122 tYQRVQPMIDNVGTNNTgDQTSFFDDDGKAYLVYSND--------RGRGSLYIAKL--RSDYLGiepAVRIDNYVGPGR- 190
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1467206167 249 edkpiwiEGPHLYKINGNYFLMSAEggTAGWHS 281
Cdd:cd18823   191 -------EGNALFKYGGTYYLCASD--LHGWNA 214
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
99-279 7.01e-09

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: 56.86  E-value: 7.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  99 TYY------------PGVPLFHSKDLVNWKQVGHILNRpSQLVNMEGQHVsgGIFAPAISYNPHNKTYYMV--------- 157
Cdd:cd18822    14 TYYwygenrdnnngfNGVSLYSSTDLVNWEFRNTVLTR-DTCSASELASC--KIERPKVIYNPKTGKFVMWahwengkdy 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 158 --------TTNVGAGNF-FVKTQDPFGEWSDpimlpevtgiDPSFFFDEDGKAYLV-NNDDAPDNkpeysghrTIrvqeF 227
Cdd:cd18822    91 glaraavaTSDTPDGDYtFHGSFRPLGYDSR----------DMTLFVDDDGTAYLIsAANDNADL--------NI----Y 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1467206167 228 DVNADKT-VGPRKILVNKGARPedkpiwiEGPHLYKINGNYFLMSAegGTAGW 279
Cdd:cd18822   149 RLTPDYLsVDSLVATLFKGQHR-------EAPALVKRNGYYYLFTS--GASGW 192
GH43_Xsa43E-like cd18618
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ...
106-298 1.99e-07

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: 52.61  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 106 LFHSKDLVNWKQVGHILnrpsQLVNMEGqhVSGGIFAPAISYNpHNKTYYMVTTNVGAGNFF---VKTQD-PFGEWSDPI 181
Cdd:cd18618    37 VFSTTDMVNWTDHGAVL----SLKDFSW--AKGDAWAGQVIER-NGKFYWYVPVHHKTNGGFaigVAVSDsPTGPFKDAL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 182 MLPEVTG------------IDPSFFFDEDGKAYLvnnddapdnkpeYSGH---RTIRVQEFDVNADKTVGPRKIlvnkga 246
Cdd:cd18618   110 GKPLITNdmtgttnhswddIDPTVFIDDDGQAYL------------YWGNpelYYVKLKEDMISLDGEIGTIDI------ 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1467206167 247 rpEDKPIWIEGPHLYKINGNYFLMSAeggtAGWHSEVIFR-GDSPTGkfiPWK 298
Cdd:cd18618   172 --SGLPDFTEAPWVHKRNGLYYLSYA----AGFPEKIAYAtSDSPTG---PWT 215
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
99-269 2.00e-07

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: 52.66  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  99 TYY-----PGVPLFHSKDLVNWKQVGHILNRPSQLVNMEGQHVSGGIFAPAISYnpHNKTYYM---------------VT 158
Cdd:cd18830    12 TYYlfstgPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGFNGHIWAPDISF--HNGRYYLyyscsafgkntsaigVA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 159 TNvgagnffvKTQDPFG---EWSDP-IMLPEVTG------IDPSFFFDEDGKAY-----------LVNNDdaPDNKPEYS 217
Cdd:cd18830    90 TN--------KTLDPDSpdyKWEDHgMVVQSVPGrdlwnaIDPNVIVDEKGTPWlsfgsfwggikLVKLD--PDLKSLAE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1467206167 218 GHRTIRVQefdvnadktvgpRKILVNKGARPEDKPIWIEGPHLYKINGNYFL 269
Cdd:cd18830   160 PQEWHTIA------------RRERTFKLTDSEAGPGAIEAPFIFKKGGYYYL 199
GH43_AnAbnA-like cd18831
Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); ...
80-204 4.24e-07

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: 51.83  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTNGEGDYFLavstFTYYPGVPLFHSKDLVN-WKQVGHILNRPSqLVNMEGQhvsGGIFAPAISYnpHNKTYYM-- 156
Cdd:cd18831     3 DPSIIRREDGTYFR----FSTGGGIRIATAPSLTGpWTYVGSVLPGGS-SIDLAGN---DDLWAPDVHY--VNGTYYCyy 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 157 -VTTnVGAGNFFV-----KTQDPfGEWSD-PIMLPEVTG-----IDPSFFFDEDGKAYLV 204
Cdd:cd18831    73 sVST-FGSQDSAIgvatsPTMEP-GSWTDhGAVIRSSSGdpynaIDPNLIVDDDGTPYLT 130
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
99-297 7.29e-07

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: 50.70  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  99 TYYPGVPLFHSKDLVNWKQVGHILNRpsqlvnmegqhVSGGIFA-------PAISYNPHNKTYYM--------------- 156
Cdd:cd18821    27 NLFQGVSCYSSTDLVNWTFEGLALPP-----------QESGDLGpnrvverPKVIYNPSTGKYVMwmhidssnygdarvg 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 157 -VTTNVGAGNF-FVKTQDPFGEWSDpimlpevtgiDPSFFFDEDGKAYLVNNDDapdnkpeysgHRTIRVQEFdvNADKT 234
Cdd:cd18821    96 vATSDTVTGPYtYVGSFRPLGYESR----------DIGVFQDDDGTAYLLFEDR----------DNGLRIYRL--SDDYL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1467206167 235 VGPRKILVNKGARpedkpiwIEGPHLYKINGNYFL-MSaegGTAGWHSE--VIFRGDSPTGkfiPW 297
Cdd:cd18821   154 SVVELVYTFIAAG-------LEAPAMFKVDGTYYLlGS---HLTGWRPNdnVYFTATSLSG---PW 206
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
102-336 7.36e-07

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: 50.67  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 102 PGVPLFHSKDLVNWKQVGhilnrPSQLVNMEGQHVSGGIFAPAISYnpHNKTYYMV--TTNVGAGNFFVKTQ------DP 173
Cdd:cd08772    25 PFLGHARSKDLIHWEEEP-----PAIVARGGGSYDTSYAFDPEVVY--IEGTYYLTycSDDLGDILRHGQHIgvayskDP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 174 FGEWSDPIMLPEVTG-------IDPSFFFDEDGKAYLVnnddapdNKPEYSGHrtIRVQEFDVnADKTVGPRKILVNKGA 246
Cdd:cd08772    98 KGPWTRKDAPLIEPPnayspknRDPVLFPRKIGKYYLL-------NVPSDNGH--TRFGKIAI-AESPD*LHWINHSFVY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 247 RP-EDKPIWiEGPHLYKINGNYFLM-SAEGGTAGWHSEVIFRGDSPTGKFIPWKNNPILTQRQLDAeRPNPVTCAGHADL 324
Cdd:cd08772   168 NYnEQGKVG-EGPSLWKTKGGWYLIyHANTLTGYGYGFGYALGDLDDPSKVLYRSRPEEEYETVGF-KPNVVAPAAFLCD 245
                         250
                  ....*....|..
gi 1467206167 325 vqtREGDWWAVF 336
Cdd:cd08772   246 ---STGIVAIIG 254
GH43_XylA-like cd18620
Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium ...
111-269 1.35e-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: 50.29  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 111 DLVNWKQVGHILNrpSQLVNMEGQHVSGGIFAPAISYnpHNKTYYMVTTNVGAGNFFVKTQD-PFGEWSDPIMLP----- 184
Cdd:cd18620    40 DLSNWRYHGVIFR--SDQDPDEVPPGKGLLYAPDVVK--GPGRYYLYYCLSKGSVEGVAVSDsPAGPFEYLGPVKyprkg 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 185 EVTGIDPSFFFDEDGKAYLvnnddapdnkpeYSGHRTIRVQEFDVNAdKTVGPRKILVNKGARPEDKPIWIEGPHLYKIN 264
Cdd:cd18620   116 DIFQIDPAVLVDDDGRVYL------------YWGQGGSKGAELDPDM-LTIKPETIVDVPAGITFEGHGFFEGSSIRKIN 182

                  ....*
gi 1467206167 265 GNYFL 269
Cdd:cd18620   183 GIYYL 187
GH43_CtGH43-like cd18826
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
103-301 5.15e-05

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


Pssm-ID: 350147 [Multi-domain]  Cd Length: 269  Bit Score: 45.31  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 103 GVPLFHSKDLVNWKQVGHIL-----NRPSQLvnmegqHVSGGIFAPAISYNPHNKTYYMVTTNVGAGN---FFVKTQD-- 172
Cdd:cd18826    35 GVRCYSSTDLYNWEDEGLIIppdpdDPSSPL------HPTRIMDRPHIIYNEKTGKYVCWLKLYPGGDvqyFGVLTADsp 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 173 --PFgEWSDPIMLPEVTGI-DPSFFFDEDGKAYLVN------------NDDAPDNKPEYSGHRTirvqefdvnadkTVGP 237
Cdd:cd18826   109 tgPY-TYVHKFLGPLGMGAgDFDLVVDPDGKAYLYFervhkevvcadlTDDYTDVTGEYSTHFP------------GLGP 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1467206167 238 rkilvnkgarpedkPIWIEGPHLYKINGNYFLMSAegGTAGWH---SEViFRGDSPTGkfiPWK--NNP 301
Cdd:cd18826   176 --------------PFAREAPAVFKRGGKHYLLTS--GTTGYFpnpSEV-AVADSYHG---PWTvlGNP 224
GH43_CtGH43-like cd18825
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
102-372 1.22e-04

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


Pssm-ID: 350146 [Multi-domain]  Cd Length: 285  Bit Score: 44.13  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 102 PGVPLFHSKDLVNWKQVGHILnRPSQLVNMEGQHVSGGIFAPAISYNPHNKTYYMV------------------TTNVGA 163
Cdd:cd18825    33 IGVSCYSSKDLYNWKDEGIVL-DAVDDAPASDLYPNNVVERPKVIYNKKTKKYVMWfhldgpgadysraragvaVSDSPT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 164 GNF-FVKTQDPF-GEWSDPI----MLPEVTgidpsFFFDEDGKAYLVnnddapdnkpeYS--GHRTIRVQEF-DVNADKT 234
Cdd:cd18825   112 GPFkYLGSFRPNaGEKNRDFsngqMSRDMT-----LFVDDDGKAYLI-----------YSseENKTLYIAKLtDDYTGVT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 235 VGPRKILVNKgarpedkpiWIEGPHLYKINGNYFLMSAegGTAGWHSE--VIFRGDSPTGkfiPWKnnpiltqrqldaER 312
Cdd:cd18825   176 GDYARILIGQ---------SREAPAVFKHDGKYYMITS--GCTGWAPNaaRYAVADSIFG---PWK------------EI 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 313 PNPvtCAGHADLVQTregdwwavflacrpinnTFEnlGRETFMMPVKWSEDGFPYMtqGD 372
Cdd:cd18825   230 GNP--CRGPNDDADT-----------------TFG--SQSTFVLPVDGENGKFIYM--GD 266
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
80-274 2.06e-04

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: 43.50  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTNGEGDYflavsTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQ-----LVNMEGQHVsggiFAPAISYnpHNKTY 154
Cdd:cd18829     3 DPSIIKEGSTWW-----TFSTGDGIPVKYSSDGLNWTQGPPIFGSPLSwwktyVPANTTNDV----WAPDVHY--YNGKY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 155 YM---VTT---NVGAGNFFVKTQDPFGEWSDPIMLPEVT------GIDPSFFFDEDGKAYLVnnddapdnkpeYSGHRT- 221
Cdd:cd18829    72 WLyyaISTfgsNTSAIGLASASSIAAGNWTDEGLVLRSTsadnynAIDPNLVIDASGNPWLV-----------FGSFWSg 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1467206167 222 IRVQEFDVNADKTVGPrkiLVNKGARPedkPIWIEGPHLYKINGNYFLMSAEG 274
Cdd:cd18829   141 IKITRLDKATMKPTGS---IYSIASRP---SGGIEGPFIVYRDGYYYLFVSID 187
Glyco_hydro_32N pfam00251
Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal ...
68-220 2.64e-04

Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.


Pssm-ID: 425557  Cd Length: 308  Bit Score: 43.39  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  68 YFYNPIL---PGWYS----DPSICTNGEGDYF--LAVSTFTYYPGVPLFHSKDLVNWKQVGHILNRPSQLVNM------- 131
Cdd:pfam00251 114 YPNNPVIinlPAGYTkhfrDPKVAWYEDGKWYmvLGAQDNDKKGKILLYKSDDLKNWTFVGELLHSNDGGGYMwecpdlf 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 132 --------EGQHVSggIFAPA-ISYNPHNKTYYMVTTNVGAGNFFvkTQDPFGEWSDpimlpevTGID---PSFFFDEDG 199
Cdd:pfam00251 194 pldgkdgeKWKHVL--KFSPQgLSYDNIYQDYYFIGSFDLDGDKF--TPDGEFLRLD-------YGFDfyaPQTFNDPDG 262
                         170       180
                  ....*....|....*....|....
gi 1467206167 200 KAYLV---NNDDAPDNKPEYSGHR 220
Cdd:pfam00251 263 RRILIgwmGNWDSEANDYPTKGWA 286
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
80-270 1.40e-03

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: 40.68  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  80 DPSICTNGEGDYFLAVST---------FTYYPGVPLFHSKDLVNWKQVGHI-LNRPSQLVNMegqhvsggiFAPAISYNP 149
Cdd:cd08983    20 DPFIIRGPEDGKFYLVATdlwiaggaqWNGSRGIGVWESTDLVNWSEQRLVkMVSPPNAGNA---------WAPEAIYDP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 150 HNKTYY-----MVTTNVGAGNF---FVKTQDpFGEWSDPIML--PEVTGIDpSFFFDEDGKAYLVNNDDapdnkpeySGH 219
Cdd:cd08983    91 ETGQYVvywssSLYGDGGGGNHriyYATTKD-FKTFSEPKVLfdPGFNVID-TTIVKDGGTYYRFYKDE--------TTG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1467206167 220 RTIRVQefdvNADKTVGPRKILVNKGarPEDKPIWIEGPHLYKINGN--YFLM 270
Cdd:cd08983   161 KGIRLA----TSDSLTGPWTTVTTGG--GAGTGGGVEGPTVFKLNDGgkWYLY 207
GH43_62_32_68_117_130-like cd08994
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
146-303 1.71e-03

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: 350108 [Multi-domain]  Cd Length: 294  Bit Score: 40.71  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 146 SYNPHNKT----------YYMVTTNVGAGNFFVK----TQ--------DPFGEWSD---PIMLPEVTGID------PSFF 194
Cdd:cd08994    77 GDTTHNPTikkfdgkyylYYIGNTGPGPDPPLWWghrnNQrigvavadSPNGPWKRfdkPILDPRPRSWDdlitsnPAVL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167 195 FDEDGKAYLVNNDDAPDNKpeysGHRTIRVqefdVNADKTVGPRKILVNKGARPEDKPIWIEGPHLYKINGNYFLMS--- 271
Cdd:cd08994   157 KRPDGSYLLYYKGGKKNPG----GNRKHGV----AVSDSPEGPYTKLSDPPVYEPGVNGQTEDPFIWYDKGQYHLIVkdm 228
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1467206167 272 AEGGTAGWHSEVIFRgdSPTGkfIPWKNNPIL 303
Cdd:cd08994   229 GGIFTGEGGGGALLR--SKDG--INWKLAPGL 256
GH43_Bt1873-like cd08981
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This ...
88-204 6.71e-03

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as 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 GH43 enzymes in this family may 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: 350095 [Multi-domain]  Cd Length: 289  Bit Score: 38.66  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467206167  88 EGDYFLAVSTFTYY-----PGVPLFHSKDLVNWKQVGHILNRPSqlvNMEGQHvsgGIFAPAISYnpHNKTYYMVTTNVG 162
Cdd:cd08981    17 TGTYYLYGTTDKDCwwgkgTGFDVYVSKDLENWEGPYEVFRPPE---DFWADR---NFWAPEVHE--YNGKYYLFATFKA 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1467206167 163 AGNFFVKTQ----D----PFGEWSD-PIMLPEVTGIDPSFFFDEDGKAYLV 204
Cdd:cd08981    89 EGNGRRGTQilvsDsplgPFVPLSDgPVTPEDWMCLDGTLYVDEDGKPWMV 139
 
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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