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Conserved domains on  [gi|1082321616|gb|AOW86342|]
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glycoside hydrolase [Streptomyces olivaceus]

Protein Classification

glycoside hydrolase 43 family protein( domain architecture ID 14406689)

glycoside hydrolase 43 family protein similar to Bifidobacterium adolescentis arabinofuranohydrolase D3 that releases only C3-linked arabinose residues from double-substituted xylose residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
8-286 2.93e-119

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: 351.05  E-value: 2.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   8 TYTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHQ----DRGVWAPA 83
Cdd:cd09001     1 TYTNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAYYLEDGknayGKGIWAPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  84 LRHHAGRFWIFWGDPDQGVFQVNAPEIRGPWTAPHLVksGRGLIDPCPLWDgESGEAYLVHAWarsrsgvkNRLTGHRMR 163
Cdd:cd09001    81 LRYHNGKFYVYFCTNTGGTYVYTADDPAGPWSRPALI--GKGYHDPSLLFD-DDGKAYLVYGN--------GEIRLTELS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 164 PDGTGLLDDGEVIVDGDrlPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQGAFRSRAFFGPYEEKVVLEQ-RDTDVNGP 242
Cdd:cd09001   150 PDGTGVGGEGRVIIDGT--EEGLGAEGSHLYKINGYYYIFNIEWGGGGRTQVVLRSKSLYGPYEGRVVLDDgSGTGDNGP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1082321616 243 HQGGWVRTRTGEDWFLHFQSRGAYGRVVHLQPMRWDgDGWPVLG 286
Cdd:cd09001   228 HQGGLVDTPDGEWWFMLFQDRGAVGRIPVLVPVTWK-DGWPVIG 270
GH43_C2 super family cl38978
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
312-506 3.30e-18

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.


The actual alignment was detected with superfamily member pfam17851:

Pssm-ID: 436093  Cd Length: 203  Bit Score: 83.09  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 312 DDFPGGRFGRQWSWAANPRDG-WA--TQHAGdGLRLacvRAAGVDDLRLQPNSLTQRLPGAPSVIEVDLTLDSEEPGARA 388
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDEsWYslTERPG-YLRL---YGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 389 GLAVLGDAYRWIGL--QRDTDGTVHLvhRFADAAAESVTGAERDADRPRPAPGGRVRLRVE-TAPGARCRFFYDlGDGPR 465
Cdd:pfam17851  78 GLVVYYNEYNHYYLgvTKDEDGGRVL--RLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEvDGDTYQFSYSYD-GKDWK 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1082321616 466 PTGREFAAR--------PWRWVGALLGLFALApTGPGHAGAATFTRFRV 506
Cdd:pfam17851 155 TIGPELDASilsdeyaaGGGFTGAFVGLYATD-NGKGSSGYADFDWFEY 202
 
Name Accession Description Interval E-value
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
8-286 2.93e-119

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: 351.05  E-value: 2.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   8 TYTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHQ----DRGVWAPA 83
Cdd:cd09001     1 TYTNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAYYLEDGknayGKGIWAPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  84 LRHHAGRFWIFWGDPDQGVFQVNAPEIRGPWTAPHLVksGRGLIDPCPLWDgESGEAYLVHAWarsrsgvkNRLTGHRMR 163
Cdd:cd09001    81 LRYHNGKFYVYFCTNTGGTYVYTADDPAGPWSRPALI--GKGYHDPSLLFD-DDGKAYLVYGN--------GEIRLTELS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 164 PDGTGLLDDGEVIVDGDrlPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQGAFRSRAFFGPYEEKVVLEQ-RDTDVNGP 242
Cdd:cd09001   150 PDGTGVGGEGRVIIDGT--EEGLGAEGSHLYKINGYYYIFNIEWGGGGRTQVVLRSKSLYGPYEGRVVLDDgSGTGDNGP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1082321616 243 HQGGWVRTRTGEDWFLHFQSRGAYGRVVHLQPMRWDgDGWPVLG 286
Cdd:cd09001   228 HQGGLVDTPDGEWWFMLFQDRGAVGRIPVLVPVTWK-DGWPVIG 270
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
9-283 5.38e-89

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: 274.20  E-value: 5.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   9 YTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHqdrgVWAPALRHHA 88
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNA----SWAPDISYHD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  89 GRFWIFWGDPDQGVFQVNAPEIRGPWTAPHLVKSGRGLIDPCPLWDGEsGEAYLVHAWARSRSGvKNRLTGHRMRPDGTG 168
Cdd:pfam04616  77 GKYYLYYTAVAHGIFVATADSPDGPWSDPGKLKSGGGGIDPSLFHDDD-GKKYLVWGGWDPRHG-HGGIYLQELDNDGLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 169 LLDDG-EVIVDGDRLPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQ-GAFRSRAFFGPYEEKVVLE-----QRDTDVNG 241
Cdd:pfam04616 155 LVGPVtKLIYPGTRWVGGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAvGVARSRSPLGPYEWHPGNPiltsrSPENPIYG 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1082321616 242 PHQGGWVRTRTGEDWFLHFQSRGA-----YGRVVHLQPMRWDGDGWP 283
Cdd:pfam04616 235 PGHASLVETPDGEWWIVYHAGRPGdggygLGRETRIQPVEWRADGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
6-332 1.41e-88

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 275.67  E-value: 1.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   6 AKTYTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPereFAAPHqDRGVWAPALR 85
Cdd:COG3507    19 GNTYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQ---WADPY-SGGIWAPDIR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  86 HHAGRFWIFWGDPD-----QGVFQVNAPEIRGPWTAPH-LVKSGRGLIDPCPLWDgESGEAYLVHAWARsrsgvkNRLTG 159
Cdd:COG3507    95 YHNGKYYLYYTAVDggknrSGIGVATADDPEGPWSDPGpLVCPGGNGIDPSVFVD-DDGKAYLVYGSGG------GGIYV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 160 HRMRPDGTGLLDDGEVIVDGDrlpGWFTLEGPKLYRHDGWFWILAPAGSVE--TGWQGAFRSRAFFGPYE---EKVVLEQ 234
Cdd:COG3507   168 AELDPDTGKLLGEPKTLAPGG---EGGWIEGPHIYKRNGYYYLFYSEGGTCnsGYAVRVARSKSPTGPYEdapGNPILTQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 235 R-DTDVNGPHQGGWVRTRTGEDWFLHFQSR--GAYGRVVHLQPMRWDGDGWPVLGEGGAPVAEYTRPALPPQPPAAPATD 311
Cdd:COG3507   245 RsDGGIQGPGHGSLVETPDGEWYLVYHAYRppGGLGRETFLDPVTWNEDGWPVVGPGTGEPPQPLPAPESDDFDGPLGLQ 324
                         330       340
                  ....*....|....*....|.
gi 1082321616 312 DDFPGGRFGRQWSWAANPRDG 332
Cdd:COG3507   325 WSLGYLRLTRQFTATTKLRAG 345
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
312-506 3.30e-18

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: 83.09  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 312 DDFPGGRFGRQWSWAANPRDG-WA--TQHAGdGLRLacvRAAGVDDLRLQPNSLTQRLPGAPSVIEVDLTLDSEEPGARA 388
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDEsWYslTERPG-YLRL---YGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 389 GLAVLGDAYRWIGL--QRDTDGTVHLvhRFADAAAESVTGAERDADRPRPAPGGRVRLRVE-TAPGARCRFFYDlGDGPR 465
Cdd:pfam17851  78 GLVVYYNEYNHYYLgvTKDEDGGRVL--RLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEvDGDTYQFSYSYD-GKDWK 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1082321616 466 PTGREFAAR--------PWRWVGALLGLFALApTGPGHAGAATFTRFRV 506
Cdd:pfam17851 155 TIGPELDASilsdeyaaGGGFTGAFVGLYATD-NGKGSSGYADFDWFEY 202
 
Name Accession Description Interval E-value
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
8-286 2.93e-119

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: 351.05  E-value: 2.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   8 TYTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHQ----DRGVWAPA 83
Cdd:cd09001     1 TYTNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAYYLEDGknayGKGIWAPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  84 LRHHAGRFWIFWGDPDQGVFQVNAPEIRGPWTAPHLVksGRGLIDPCPLWDgESGEAYLVHAWarsrsgvkNRLTGHRMR 163
Cdd:cd09001    81 LRYHNGKFYVYFCTNTGGTYVYTADDPAGPWSRPALI--GKGYHDPSLLFD-DDGKAYLVYGN--------GEIRLTELS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 164 PDGTGLLDDGEVIVDGDrlPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQGAFRSRAFFGPYEEKVVLEQ-RDTDVNGP 242
Cdd:cd09001   150 PDGTGVGGEGRVIIDGT--EEGLGAEGSHLYKINGYYYIFNIEWGGGGRTQVVLRSKSLYGPYEGRVVLDDgSGTGDNGP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1082321616 243 HQGGWVRTRTGEDWFLHFQSRGAYGRVVHLQPMRWDgDGWPVLG 286
Cdd:cd09001   228 HQGGLVDTPDGEWWFMLFQDRGAVGRIPVLVPVTWK-DGWPVIG 270
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
9-283 5.38e-89

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: 274.20  E-value: 5.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   9 YTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHqdrgVWAPALRHHA 88
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNA----SWAPDISYHD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  89 GRFWIFWGDPDQGVFQVNAPEIRGPWTAPHLVKSGRGLIDPCPLWDGEsGEAYLVHAWARSRSGvKNRLTGHRMRPDGTG 168
Cdd:pfam04616  77 GKYYLYYTAVAHGIFVATADSPDGPWSDPGKLKSGGGGIDPSLFHDDD-GKKYLVWGGWDPRHG-HGGIYLQELDNDGLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 169 LLDDG-EVIVDGDRLPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQ-GAFRSRAFFGPYEEKVVLE-----QRDTDVNG 241
Cdd:pfam04616 155 LVGPVtKLIYPGTRWVGGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAvGVARSRSPLGPYEWHPGNPiltsrSPENPIYG 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1082321616 242 PHQGGWVRTRTGEDWFLHFQSRGA-----YGRVVHLQPMRWDGDGWP 283
Cdd:pfam04616 235 PGHASLVETPDGEWWIVYHAGRPGdggygLGRETRIQPVEWRADGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
6-332 1.41e-88

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 275.67  E-value: 1.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   6 AKTYTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPereFAAPHqDRGVWAPALR 85
Cdd:COG3507    19 GNTYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQ---WADPY-SGGIWAPDIR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  86 HHAGRFWIFWGDPD-----QGVFQVNAPEIRGPWTAPH-LVKSGRGLIDPCPLWDgESGEAYLVHAWARsrsgvkNRLTG 159
Cdd:COG3507    95 YHNGKYYLYYTAVDggknrSGIGVATADDPEGPWSDPGpLVCPGGNGIDPSVFVD-DDGKAYLVYGSGG------GGIYV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 160 HRMRPDGTGLLDDGEVIVDGDrlpGWFTLEGPKLYRHDGWFWILAPAGSVE--TGWQGAFRSRAFFGPYE---EKVVLEQ 234
Cdd:COG3507   168 AELDPDTGKLLGEPKTLAPGG---EGGWIEGPHIYKRNGYYYLFYSEGGTCnsGYAVRVARSKSPTGPYEdapGNPILTQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 235 R-DTDVNGPHQGGWVRTRTGEDWFLHFQSR--GAYGRVVHLQPMRWDGDGWPVLGEGGAPVAEYTRPALPPQPPAAPATD 311
Cdd:COG3507   245 RsDGGIQGPGHGSLVETPDGEWYLVYHAYRppGGLGRETFLDPVTWNEDGWPVVGPGTGEPPQPLPAPESDDFDGPLGLQ 324
                         330       340
                  ....*....|....*....|.
gi 1082321616 312 DDFPGGRFGRQWSWAANPRDG 332
Cdd:COG3507   325 WSLGYLRLTRQFTATTKLRAG 345
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
11-278 8.16e-49

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: 169.08  E-value: 8.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  11 NPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPhQDRGVWAPALRHHAGR 90
Cdd:cd08989     1 NPVLPGFHPDPSVVRVGDDYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQLDLTGGP-DGGGIWAPDISYHDGK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  91 FWIF-------WGDPDQGVFQVNAPEIRGPWTAPHLVKSgrGLIDPCPLWDgESGEAYLVhawarsrsgvkNRLTGHRMR 163
Cdd:cd08989    80 FYIYytvvlnvGSWKGRRNYLVTSEDPEGPWSEPVWLDE--GGIDPSLFVD-DDGKHYML-----------LNPGGIRLA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 164 ---PDGTGLLDDGEVIVDGdrlPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQ-GAFRSRAFFGPYE---EKVVLEQRD 236
Cdd:cd08989   146 elnPDCTKQIGEPKRIWEG---TGGRAPEGPHLYKKDGYYYLLTAEGGTGYGHAiTIARSKTIYGPYEpcpYNPILRQQD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1082321616 237 TDVN--GPHQGGWVRTRTGEDWFLHFQSR---GAY---GRVVHLQPMRWD 278
Cdd:cd08989   223 PQAPlqRCGHGKLVETPDGEWWMVYLCGRplpGGYcplGRETALAPVEWT 272
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
11-284 3.68e-48

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: 168.07  E-value: 3.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  11 NPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHqDRGVWAPALRHHAGR 90
Cdd:cd18617     1 NPILPGFYPDPSICRVGDDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQLDLRGVPS-SGGIFAPTIRYHDGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  91 FWI----FWGDPdQGVFQVNAPEIRGPWTAPHLVKsGRGlIDPCPLWDgESGEAYLVhaWARSRSGVKNRLTGHRMR--- 163
Cdd:cd18617    80 FYIittnVSTDG-RGNFIVTADDPAGPWSDPVWLD-GPG-IDPSLFFD-DDGKVYLT--GTGPPPDPYEGHGGIWQQeid 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 164 PDgTG-LLDDGEVIVDGDRLPGWftLEGPKLYRHDGWFWILAPAGSVETG-WQGAFRSRAFFGPYEE---KVVLEQRDTD 238
Cdd:cd18617   154 LE-TGkLLGEPKVLWNGGTGGRW--PEGPHLYKIDGWYYLLIAEGGTEEGhSETIARSRSPWGPYEPcpnNPILTHRHLG 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1082321616 239 VNGPHQGG---WVRTRTGEDW--FLHFQSRGAY----GRVVHLQPMRWDGDGWPV 284
Cdd:cd18617   231 SNPVQNTGhadLVEDPDGSWWavFLGVRPYGGGfhnlGRETFLAPVEWEDGWPVV 285
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
9-285 7.23e-42

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: 150.84  E-value: 7.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   9 YTNPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALdrleperefaaPHQDRGVWAPALRHHA 88
Cdd:cd09002     1 YLNPILAGDYPDPSILRDGDDYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAAL-----------TEYIGTVWAPDLIKHD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  89 GRFWIFWGDPDQGVFQVNAPEIRGPWTAPHLVKSGRGlIDPCPLWDgESGEAYLVHAwarsrSGVKNRLTghrmrPDGTG 168
Cdd:cd09002    70 GRYYIYFPAKGGTNYVITADDIAGPWSEPIDLKVGSG-IDPGHVVD-EDGKRYLFLS-----GGRRVRLT-----DDGLS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 169 LLDDGEVIVDGDRLPG-W----FTLEGPKLYRHDGWFWILAPAGsvetGWQG--------AFRSRAFFGPYEekvvleqr 235
Cdd:cd09002   138 VAGPPEKVYDGWRYPDeWdvecFCLEGPKLFRRGGYYYLTTAQG----GTAGpptshmvvSARSKSPHGPWE-------- 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082321616 236 dtdvNGPHQgGWVRTRTGE-----------------DWFLHFQSR--GAY--GRVVHLQPMRWDGDGWPVL 285
Cdd:cd09002   206 ----NSPYN-PLVRTQSREekwwskghgtlvegpdgKWWMVYHGYenGYRtlGRQTLLEPVEWTADGWFRI 271
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
11-285 9.87e-42

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: 150.78  E-value: 9.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  11 NPVLNADWSDPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHqDRGVWAPALRHHAGR 90
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPD-SGGIWAPCLSYADGK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  91 FWIFWGDPDQ--GVFQ------VNAPEIRGPWTAPHLVKSGrGLiDPCPLWDgESGEAYLVHAWARSRSGvKNRLTGHRM 162
Cdd:cd09000    80 FWLVYTDVKSvdGPFKdvhnylVTAESIEGPWSEPIYLNSS-GF-DPSLFHD-DDGRKYLVNMLWDHRPG-HNRFAGIVL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 163 R---PDGTGLLDDGEVIVDGDRLPGwftLEGPKLYRHDGWFWILAPAGSveTGWQGAF---RSRAFFGPYE---EKVVLE 233
Cdd:cd09000   156 QefdPETKKLVGERKVIFKGTELGL---TEGPHLYKRDGYYYLLTAEGG--TGYEHAVtvaRSRNIFGPYEvdpDNPLLT 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082321616 234 QRDTDVNgPHQ----GGWVRTRTGEdWF--------LHFQSRGAYGRVVHLQPMRWDGDGWPVL 285
Cdd:cd09000   231 SWDDPEN-PLQkaghGSLVETPDGE-WYlahlcgrpLPGRGRCPLGRETAIQKVEWTDDGWPRL 292
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
11-284 2.34e-32

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: 125.44  E-value: 2.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  11 NPVLNADWSDPDVIRVG---DDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLE--PEREFAAPHQDRGVWAPALR 85
Cdd:cd18833     1 NPIIPGFHPDPSCIFVPewdGTFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSqlPELATTGTGQQGGIWAPTLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  86 HHAGRFWI-----FWGDPDQG-----VFQVNAPEIRGPWTAPhLVKSGRGlIDPCPLWDGEsGEAYLVHAWA-RSRSGVk 154
Cdd:cd18833    81 YHDGTFYVittlvFPDKTDASrwdnlLFTTTDPYSDSAWSDP-IRFDFPG-YDPDLFWDDD-GTAYVQGAHYwRVRPEI- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 155 nrltgHRMRPD-GTGLLDDGEVIVDGDrlpGWFTLEGPKLYRHDGWFWILAPAGSVETGWQGAF-RSRAFFGPYEEKV-- 230
Cdd:cd18833   157 -----QQQEIDlKTGESLSPSPIWNGT---GGSAPEGPHMYKKDGWYYLLIAEGGTGLGHSVTIaRSRSIWGPYESYPsn 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082321616 231 -VLEQRDT--------------DVNGPHQGGWVRTRTGEDWflhfqsrGAY--GRVVHLQPMRWDGDGWPV 284
Cdd:cd18833   229 pVLTNANTseyfqtvghadlfqDANGNWWGVALATRSGPEY-------EIYpmGRETVLYPVTWEEGEWPV 292
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
20-286 6.37e-21

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: 92.62  E-value: 6.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYLTASSFGRAPGLPLLHSRDLVNWTLVGHALDRLeperefaAPHQDRGVWAPALRHHAGRFWIF----W 95
Cdd:cd08991     2 DPFVLKHNGTYYLYGTGGDDGRGFKVYVSDDLVNWEYPGGALEEP-------GLWGTKGFWAPEVFYYNGKFYMYysanG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  96 GDPDQ--GVFQVNAPEirGP--WTAPHLVKSGRGLIDPCPLWDgESGEAYLVHAWARSRSGVKNRLTGHRMRPDGTglLD 171
Cdd:cd08991    75 GDHGEhiAVAVSDSPL--GPfrDKGKLLIPAGGFSIDAHVFID-DDGKWYLYYVRDDLGGEPGNRIYVAELEDDLS--LI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 172 DGEVIV------DGDRLPG---WFTLEGPKLYRHDGWFWILAPAgsvetgwqGAFRSRAFF----------GP---YEEK 229
Cdd:cd08991   150 GEPTLVlcptadERWEYGEgrdWHTTEGPTVLKHNGTYYLTYSA--------NHFRSPDYAvgyatadsplGPwtkYEGN 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 230 VVLEQRDTDVNGPHQGGWVRTRTGEDWFL---HFQSRGAYGRVVHLQPMRWDGDGWPVLG 286
Cdd:cd08991   222 PILSRNDGGVNGPGHNSVFKDPDGDLYIVyhtHDSDETVEPRKMRIDRLRFDGDKLSVLG 281
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
11-284 1.33e-19

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: 88.74  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  11 NPVLNADWSDPDVIRVGDDFYLTASSfGRAPGLPLLHSRDLVNWTLVGH-ALDRLEPEREfaaphQDRGVWAPALRHHA- 88
Cdd:cd08999     1 NPVIDGDFPDPSVIRVGGTYYAFATN-SGGKNVQVATSTDLVTWTLLGGdALPDLPAWAA-----AGGNTWAPDVVRRPd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  89 GRFWIFW--GDPDQGVFQVN---APEIRGPWT----APHLVKSGRGLIDPCPLWDgESGEAYLVhaW--ARSRSGVKNRL 157
Cdd:cd08999    75 GKYVMYYsaRLKSSGKHCIGvatSDSPLGPFTpvgePPLCPLDQGGAIDPSGFVD-PDGKRYLV--YkvDGNSIGVPTPI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 158 TGHRMRPDGTGLLDDGEVIVDGDRLPGWFTLEGPKLYRHDGWFWILAPAG-----SVETGWqgAfRSRAFFGPYE--EKV 230
Cdd:cd08999   152 MLQELSADGLTLVGEPVELLLNDGPWDGPLVEAPSLVKRDGTYYLFYSSNcycspSYAVGY--A-TSKSITGPYTkaGEP 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1082321616 231 VLEQRDTDVNGPhqGGWVRTRTGEDWFLHF-----QSRGAYGRVVHLQPMRWDGdGWPV 284
Cdd:cd08999   229 LLLTGDGGLTGP--GGADVVEDDGGDWMVFhawdgGDDVGGGRAMYTAELTWEG-GWPV 284
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
11-277 4.27e-19

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: 87.63  E-value: 4.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  11 NPVLNADWSDPDVIRVGDD-FYL--TASSFGRAPG---LPLLHSRDLVNWTLVGHALdrlePEREFAAPHQDRGVWAPAL 84
Cdd:cd18616     1 NPVFEPTFADPTVIRGDDGyFYAyaTEDPWGDGGGfrlVPILRSKDLVNWEYVGDAF----TSKPRWKWDPGGGLWAPDI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  85 RHHAGRFWIF-----WG-DPDQGVFQVNAPEIRGPWTaPH--LVKSG----RGLIDPCPLWDGesGEAYLVhaWArSRSG 152
Cdd:cd18616    77 RYIDGKYVLYyslsdWGaDPNPGIGVATADSPAGPFT-DQgkLFDSNeigvRNSIDPFVFEDD--GKKYLF--WG-SFYG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 153 VKNRltghRMRPDGTGLLDDGEVIVDGDRlpgwftLEGPKLYRHDGWFWILAPAGS----------VETGwqgafRSRAF 222
Cdd:cd18616   151 IYAV----ELTADGLALKPGEKVQIAGDR------YEGPYIVKRDGYYYLFGSAGSccegpnstyrVVVG-----RSESL 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082321616 223 FGPYEEK---VVLEQR--DTDVNGPHQGGWVRT--------RTGEDWFL-H-------FQSRGAYGRVVHLQPMRW 277
Cdd:cd18616   216 LGPYVDRdgrSLLDSGggGTPVVLQNGNRFVGPghnavitdDAGQDWMLyHaydrndpYLPGGYNRRPLLLDRLDW 291
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
312-506 3.30e-18

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: 83.09  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 312 DDFPGGRFGRQWSWAANPRDG-WA--TQHAGdGLRLacvRAAGVDDLRLQPNSLTQRLPGAPSVIEVDLTLDSEEPGARA 388
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDEsWYslTERPG-YLRL---YGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 389 GLAVLGDAYRWIGL--QRDTDGTVHLvhRFADAAAESVTGAERDADRPRPAPGGRVRLRVE-TAPGARCRFFYDlGDGPR 465
Cdd:pfam17851  78 GLVVYYNEYNHYYLgvTKDEDGGRVL--RLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEvDGDTYQFSYSYD-GKDWK 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1082321616 466 PTGREFAAR--------PWRWVGALLGLFALApTGPGHAGAATFTRFRV 506
Cdd:pfam17851 155 TIGPELDASilsdeyaaGGGFTGAFVGLYATD-NGKGSSGYADFDWFEY 202
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
20-260 5.20e-17

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: 80.56  E-value: 5.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYLTASSFGRAPGLPLL--HSRDLVNWTLVGHALDRlepereFAAPHQDRG-VWAPALRHHA-GRFWIFW 95
Cdd:cd08978     2 DPSILKDNGRYYIYATTDDTGTGTGIVvwKSKDLVNWKEEGTVLSR------GKSKSWGTGnLWAPEVYYFNsGKWYLYY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  96 ----GDPDQGVFQVNAPEIRGPWTAPHLVK---SGRGLIDPCPLWDGEsGEAYLVhaWARSRSGvkNRLTGHRMRPD--- 165
Cdd:cd08978    76 savpNGGGGRIYVATSDSPEGPFTPIVSGKlgdRGSGSIDPTVFVDDD-GKLYLY--YGDEDDS--GDIYVAELDPDllt 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 166 GTGLLDDGEVIVdGDRLPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQ-GAFRSRAFFGPYEEK----VVLEQRDTDVN 240
Cdd:cd08978   151 IKGDVTLLIGEV-VGSGFRGNYFEGPAVFKRNGYYYLIYSAGGTDGGYAiGYATSDSPLGPWEKAshnpGLQTSGATGIY 229
                         250       260
                  ....*....|....*....|
gi 1082321616 241 GPHQGGWVRTRTGEDWFLHF 260
Cdd:cd08978   230 GPGHGSIFQDEGDRWYIVYH 249
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
20-278 1.47e-15

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: 76.82  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYLTassFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHQDRGVWAPALRHHAGRFWIF----- 94
Cdd:cd08998     3 DPSIIKDDGGTYYV---FSTGAGIQIRTSKDLVNWEFVGTVFPEGPAWAAAEVPGGAGGLWAPDVVYVNGRYYLYysast 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  95 WGDPDQGVFQVNAPEI-RGPWT-APHLVKSGRGL----IDPCPLWDGEsGEAYLvhAWARSRSGVKnrLTghRMRPDgTG 168
Cdd:cd08998    80 FGSNRSAIGLATSTTLdDGPWTdQGLVVSSSPGDdynaIDPNVFVDAD-GRLWL--AYGSFWGGIK--LV--ELDPA-TG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 169 LLDDGEVIVD-GDRLPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQGAF-----RSRAFFGPYEEKV----------VL 232
Cdd:cd08998   152 KLRPGSTGTSiASRPGGPGAIEAPYIIYRGGYYYLFVSYGSCCRGANSTYnirvgRSTSITGPYVDRNgvdmlegggtLL 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1082321616 233 EQRDTDVNGP-HQGgwVRTRTGEDWFLHFQSRGAYGRVVHLQ--PMRWD 278
Cdd:cd08998   232 LGGHGRWIGPgHNS--VFRDGDGDYLVYHYYDGDDGGAPKLQirPLLWT 278
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
20-229 2.93e-14

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


Pssm-ID: 350102 [Multi-domain]  Cd Length: 277  Bit Score: 72.93  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYLTASSFGrAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHQDRGVWAPALRHHAGRFWIF----- 94
Cdd:cd08988     2 DPSIIKEGGTYYAFGTGTD-GFGIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGNLWAPDISQHKGKYYLYysvsd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  95 WGDPDQGVFQVNAPEIRGPWTAPHLVKSGR------GLIDPCPLWDgESGEAYLvhAWARSRSGVK-NRLTGHRMRPDGT 167
Cdd:cd08988    81 NGSNTSAIGLATANNPQGPFKDEGPAKPVVtsdnagNAIDPDLFQD-EDGQNWL--LYGSFWGGIWlQKLDKNGLVVNPP 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082321616 168 GlldDGEVIVDGDrlpgWFTLEGPKLYRHDGWFWILAPAGSVETGWQGA-----FRSRAFFGPYEEK 229
Cdd:cd08988   158 G---NGKSIAVLY----YVSIEAPYITYAGGYYYLFVSAGSCCDGGNSTyhtrvGRSKKVTGPYLDK 217
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
20-284 4.72e-09

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: 57.24  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYL--TASSFG--RAPGLPLLHSRDLVNWTLVGHALDRLEPERefaapHQDRGVWAPALRHHAGRFWIFW 95
Cdd:cd09004     2 DPDIVVFGGRYYIypTTDGPPgwSSTSFHVFSSTDLVNWTDHGIILDLANDVW-----WANKGAWAPAVAERNGKYYFYF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  96 GDPDQ-GVFQVNAPEirGPWT---APhLVKSGRG---LIDPCPLWDgESGEAYLVhaWARSRsgvknrLTGHRMRPDGTG 168
Cdd:cd09004    77 SAGSQiGVAVSDSPT--GPFTdlgRP-LVTGGDYggqAIDPMVFVD-DDGQAYLY--WGNGT------AYVARLNDDMVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 169 LldDGEVIVDGDrlPGWFTlEGPKLYRHDGWFWIL-------APAGSVETGwqgafRSRAFFGPYEEKVVLEQRDTD--V 239
Cdd:cd09004   145 F--DGEVVVSIT--PPNFR-EGPFVHKRNGIYYLSwsendtrDPDYRVRYA-----TSDSPLGPWTYRGVGLLLDSAggI 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1082321616 240 NGPHQGGWVRTRTGEDWFL--H-FQSRGAYG--RVVHLQPMRWDGDGWPV 284
Cdd:cd09004   215 KGTGHHSIVQVPGTDEWYIayHrFAVPGGDGyhREVAIDRLEFDADGTIR 264
GH43_F5-8_typeC-like cd18608
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ...
20-281 5.18e-07

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: 51.13  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYLTASS---FGRAPGLPLL-HSRDLVNWTLVGhaldrlePEREFAAPHQDRGVWAPA-LRHHAGRFWIF 94
Cdd:cd18608     3 DPSIVKFGGTYYLYATTdgwGGFNSGEPVVwKSKDFVNWKFEG-------LNWPTKAASGDSKVWAPSvVKGKDGKYYMY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  95 WGDpDQGVFQVNAPEIRGPWTA---------PHLVKSGRGLIDPCPLWDgESGEAYLVhaWARSRSGVKNRLTGhRMRPD 165
Cdd:cd18608    76 VSV-GSEIYVGVADSPLGPWKNangdgppiiPGDGKPNYHMIDAEPFID-DDGKAYLY--WGSGLHVNGHCFAA-KLNPD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 166 GTGLldDGEVIVDGDrLPGWFtlEGPKLYRHDG-WFWILAPAGSVETGWQGAFR-SRAFFGPYEE---KVVLE-QRDTDV 239
Cdd:cd18608   151 MVTF--DGSEPTIVT-PRDYF--EAPFMFKRNGiYYLMYSGGGCWDETYNVRYAvSDNPLGPFEEgenSPILQtDEAKGI 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1082321616 240 NGP-HqgGWVRTRTGEDWFL-HFQSRGAYG----RVVHLQPMRWDGDG 281
Cdd:cd18608   226 FGPgH--HSVFEEGGQYYILyHRQGYPFSPggtlRQVCVDELNFNADG 271
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
20-226 7.57e-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: 50.74  E-value: 7.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYLtassFGRAPGLPLLHSRDLVNWTLVGHALDRLEPEREFAAPHQDRGVWAPALRHHAGRFWIFWG--- 96
Cdd:cd18830     3 DPVMAREGGTYYL----FSTGPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGFNGHIWAPDISFHNGRYYLYYScsa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  97 ----------------DP--------DQGVFQVNAPEiRGPWTAphlvksgrglIDPCPLWDgESGEAYLvhAWARSRSG 152
Cdd:cd18830    79 fgkntsaigvatnktlDPdspdykweDHGMVVQSVPG-RDLWNA----------IDPNVIVD-EKGTPWL--SFGSFWGG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 153 VKnrLTghRMRPDGTGLLDDGE---------VIVDGDRLPGWFTLEGPKLYRHDGWFWILAPAGSVETGWQGAF-----R 218
Cdd:cd18830   145 IK--LV--KLDPDLKSLAEPQEwhtiarrerTFKLTDSEAGPGAIEAPFIFKKGGYYYLFVSWDYCCRGVNSTYkvvvgR 220

                  ....*...
gi 1082321616 219 SRAFFGPY 226
Cdd:cd18830   221 SKNVTGPY 228
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
48-281 2.21e-06

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: 49.13  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  48 SRDLVNWTLVGHALDrlePEREFAAPhqDRGVWAPALRHHAGRF-WIFWGDPDQGVFQVN---APEIRGPWTAPH---LV 120
Cdd:cd08990    37 STDLVNWTDHGEILP---PDDVFWWA--SGNAWAPDAVYKNGKYyFYFPVGQASDGFGIGvavSDSPAGPFKDALgkpLI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 121 KSGRG---LIDPCPLWDGEsGEAYLVHawarsrsGVKNRLTGHRMRPDGTGlLDDGEVIVDGDRLPGWFtlEGPKLYRHD 197
Cdd:cd08990   112 PEGLNgieGIDPAVFVDDD-GRAYLYF-------GGGGGYYVAKLKDDMIS-LAGEPQKIKNGGLKGFF--EAPWVFKRN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 198 GWFWILAPAGSVETGwQGAF-RSRAFFGPYEEK-VVLEQRDTDVNgpHQGgwvRTRTGEDWFL--HFQ---SRGAYGRVV 270
Cdd:cd08990   181 GTYYLSYAGGWAYPA-EIAYsTADSPLGPYTYRgVILDPVGSGTN--HGS---IVEFKGQWYLfyHTAdlsGGGDFRRSV 254
                         250
                  ....*....|.
gi 1082321616 271 HLQPMRWDGDG 281
Cdd:cd08990   255 CIDYLHYNADG 265
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
20-228 5.17e-06

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: 47.99  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDD-FYLTASS-----FGRAPGLPLLHSRDLVNWTLVGHALD-------RLEPEREFAAPHQDRGVWAPALRH 86
Cdd:cd08986     4 DPYITLGPDGyYYLTGTTggpdwWGVNDGIRLWRSKDLKDWEYLGLVWDlekdgwwQWEPQWWTPDSKNKRALWAPEIHY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  87 HAGRFWIFWGDPDQGVF----QVNAPEirGPWTAPHLVKSGRGlIDPCPLWDGEsGEAYLVhaWARSRSGvknrltghRM 162
Cdd:cd08986    84 INGTWYITHSMNGGGTGllksTTGKPE--GPYVDPMGGPLGKG-IDPSLFEDDD-GTVYLV--WGNGQIA--------RL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082321616 163 RPDGTGLLDD-GEVIVDGDRLPGwftLEGPKLYRHDGWFWILApagsveTGWQGAFR-----------SRAFFGPYEE 228
Cdd:cd08986   150 KKDMSGFAEEpRKIDPSGNREIG---HEGAFIFKIGGKYVLFG------AAWSTDKMrkgtydlyyatSDSIYGPYSE 218
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
23-214 1.13e-05

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


Pssm-ID: 350142 [Multi-domain]  Cd Length: 262  Bit Score: 46.84  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  23 VIRVGDDFYLtassFG--RAPGLPLLH------SRDLVNWTLVGHALDRLEPERefAAPhqDRGVWAPAL--RHHAGRFW 92
Cdd:cd18821     8 ILKVGDTYYW----FGedKTDGSNLFQgvscysSTDLVNWTFEGLALPPQESGD--LGP--NRVVERPKViyNPSTGKYV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  93 IFW-------GDPDQGVfqVNAPEIRGPWTaphLVKSGRGLidPCPLWD-----GESGEAYLVHAwARSRSGVKNRLTgh 160
Cdd:cd18821    80 MWMhidssnyGDARVGV--ATSDTVTGPYT---YVGSFRPL--GYESRDigvfqDDDGTAYLLFE-DRDNGLRIYRLS-- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1082321616 161 rmrPDGTGLLDDGEVIVDGDrlpgwftLEGPKLYRHDGWFWILapaGSVETGWQ 214
Cdd:cd18821   150 ---DDYLSVVELVYTFIAAG-------LEAPAMFKVDGTYYLL---GSHLTGWR 190
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
20-229 2.20e-05

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: 46.20  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDFYltasSFGRAPGLPLLHSRDLVNWTLVGHALDR-LEPEREFAAPHQDRGVWAPALRHHAGRFWIFW--- 95
Cdd:cd18829     3 DPSIIKEGSTWW----TFSTGDGIPVKYSSDGLNWTQGPPIFGSpLSWWKTYVPANTTNDVWAPDVHYYNGKYWLYYais 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  96 --GDPDQGVFQVNAPEI-RGPWTAPHLV-----KSGRGLIDPCPLWDgESGEAYLVHA--WarsrSGVK-NRLTGHRMRP 164
Cdd:cd18829    79 tfGSNTSAIGLASASSIaAGNWTDEGLVlrstsADNYNAIDPNLVID-ASGNPWLVFGsfW----SGIKiTRLDKATMKP 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082321616 165 DGTgllddgevIVD-GDRLPGwfTLEGPKLYRHDGWFWILAPAG----SVETGWQGAF-RSRAFFGPYEEK 229
Cdd:cd18829   154 TGS--------IYSiASRPSG--GIEGPFIVYRDGYYYLFVSIDkccrGVNSTYKIAYgRSTSITGPYLDK 214
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
20-281 5.64e-05

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: 44.96  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  20 DPDVIRVGDDF--YLTASS-FGRAPGLPLLHSRDLVNWTLVGHALDrlepereFAAPHQD-RGVWAPALRHHAGRFWIFW 95
Cdd:cd18827     2 DPEIRIFDGQYwiYPTYSApYEEQTFFDAFSSPDLVHWTKHERILD-------MADVPWAnRAVWAPSVIEKNGKYYLYF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  96 GDPDQ---------GVFQVNAPEirGPWtAPHLVKS-------GRGLIDPCPLWDgESGEAYLVhaWARSrsgvknrltG 159
Cdd:cd18827    75 AANDIqsddegggiGVAVADRPE--GPF-KDALGKPligefhnGAQPIDQHVFKD-DDGQAYLY--YGGW---------G 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 160 H----RMRPDGTGL--LDDGEvIVDGDRLPGWFtlEGPKLYRHDGWFWILAPAGsvetGWQGAFRSRAF------FGPYE 227
Cdd:cd18827   140 HcnvaKLNDDMTSLvpFDDGE-TFKEITPEGYV--EGPFMFKRNGKYYFMWSEG----GWTGPDYSVAYavadspLGPFK 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616 228 -EKVVLEQRDTDVNGPHQGGWVRTRTGEDWFLHFQSR-----GAYGRVVHLQPMRWDGDG 281
Cdd:cd18827   213 rIGKILQQDPAIATGAGHHSVVNVPGTDDWYIVYHRRplgetDGNHRVVCIDRMEFNEDG 272
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
5-99 5.18e-04

Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This subfamily contains glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), and includes Bacteroides enzymes, BT3780 and BACOVA_03624. Members of this family possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. GH130 enzymes have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages where these phosphorylases mediate bond cleavage by a single displacement reaction in which phosphate functions as the catalytic nucleophile. However, some lack the conserved basic residues that bind the phosphate nucleophile, as observed for the Bacteroides enzymes, BT3780 and BACOVA_03624, which are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism.


Pssm-ID: 350122 [Multi-domain]  Cd Length: 301  Bit Score: 42.19  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616   5 HAKTYTNPVLNAD----WS----DPDVIRVGDD-FYLTASSFGRA-PGLPLLHSRDLVNWTLVGHALDRlEPEREFAAPH 74
Cdd:cd18610    56 HFTRLPEPVLYPEedyeWPggceDPRIVEIEDGtYYMTYTAYDGKtARLCLATSTDLVHWTKHGPAFPD-ADGGKYRDLW 134
                          90       100
                  ....*....|....*....|....*...
gi 1082321616  75 QDRGVWAPALRHHA---GRFWIFWGDPD 99
Cdd:cd18610   135 SKSGAIVPELKGAAkinGKYWMYWGESN 162
GH43_CtGH43-like cd08985
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
23-238 9.47e-04

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: 41.16  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  23 VIRVGDDFYLTASSFGRAPGLPLLH------SRDLVNWTLVGHALDRLEPErEFAAPHQDRGVWAP-ALRHHAGRFWIFW 95
Cdd:cd08985     8 ILQEGDTYYWYGESRKGLDNDNLSHgincysSTDLYNWRFEGLVLPASGVE-VVRDISPGYVIERPkVLYNARTRKYVMW 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082321616  96 GDPDQGVFQVN------APEIRGPWT-APHLVKSGRGLIDpCPLWDGESGEAYLVhawarSRSGVKNRLTGHRMRPDGTG 168
Cdd:cd08985    87 FHLDNPNYGFAavgvatSDTPTGPFTfVRSFRPDGYPSRD-MTLFQDPDGTAYLV-----RSTDHNTDIGISRLSDDYLD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082321616 169 LLdDGEVIVDGDRlpgwftLEGPKLYRHDGWFWILApagSVETGWQGA----FRSRAFFGPYEEKVVLEQRDTD 238
Cdd:cd08985   161 TT-GASSTFKGPK------REAPALFKRGGTYYLIT---SGLTGWNPNpsrlARADSPLGPWSTWGNLPVGGPG 224
 
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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