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Conserved domains on  [gi|2048730172|ref|WP_215231951|]
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family 43 glycosylhydrolase [Dyadobacter sp. CECT 9623]

Protein Classification

glycoside hydrolase family protein( domain architecture ID 13039882)

glycoside hydrolase (GH) family protein may catalyze the hydrolysis of glycosidic bonds in complex sugars; may belong to glycosyl hydrolase families GH32, GH43, GH62, GH68, GH117, or GH130

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
70-350 6.56e-125

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: 367.12  E-value: 6.56e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDCGFAWQnKSAPFCGFKVYASPDLVNWTDKGYLFDAknpvwqSRCNGNTYGCFRPHVV 149
Cdd:cd18824     1 IDAHDGKIYFFGGAYYWYGTPYGCGCGSC-GFTLFCGFVVYSSVDLVNWTYRGVLFDP------NTCAGSPGVCFRPHVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDNVVGFRVFTSKNPAGPFTEVENPKLAVnqnaeaAGLNNGDHDTFVDDDGKGYVAYTDWRTKGTI 229
Cdd:cd18824    74 YNARTGRYVLWYNAYDGSSGYAVATSSTPTGPFVTVPDPVLAP------AGLQAGDFSLFVDDDGTGYLAYTTIDFPQSI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 230 VIEELTDDYLSGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDPNCGYCSGTGTSYRTAKSPLGPWSEGI---------- 299
Cdd:cd18824   148 VVEQLTDDYLNTTGEYVRDLIDQEAEAPSIFKRNGIYYILASNTCCGCCQGTGARVYRATSPLGPWTRQIdinscagalf 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 300 --SISDKSCGGQPSFVSTIQF-DSETVYLYGSDLWNNAA-KNEALANYFWAPLKF 350
Cdd:cd18824   228 ppSDSAYTCGGQPTAVLPLPSpGGETLYLYMGDRWRTAPdGRKGHDGHYWQPLSF 282
 
Name Accession Description Interval E-value
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
70-350 6.56e-125

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: 367.12  E-value: 6.56e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDCGFAWQnKSAPFCGFKVYASPDLVNWTDKGYLFDAknpvwqSRCNGNTYGCFRPHVV 149
Cdd:cd18824     1 IDAHDGKIYFFGGAYYWYGTPYGCGCGSC-GFTLFCGFVVYSSVDLVNWTYRGVLFDP------NTCAGSPGVCFRPHVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDNVVGFRVFTSKNPAGPFTEVENPKLAVnqnaeaAGLNNGDHDTFVDDDGKGYVAYTDWRTKGTI 229
Cdd:cd18824    74 YNARTGRYVLWYNAYDGSSGYAVATSSTPTGPFVTVPDPVLAP------AGLQAGDFSLFVDDDGTGYLAYTTIDFPQSI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 230 VIEELTDDYLSGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDPNCGYCSGTGTSYRTAKSPLGPWSEGI---------- 299
Cdd:cd18824   148 VVEQLTDDYLNTTGEYVRDLIDQEAEAPSIFKRNGIYYILASNTCCGCCQGTGARVYRATSPLGPWTRQIdinscagalf 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 300 --SISDKSCGGQPSFVSTIQF-DSETVYLYGSDLWNNAA-KNEALANYFWAPLKF 350
Cdd:cd18824   228 ppSDSAYTCGGQPTAVLPLPSpGGETLYLYMGDRWRTAPdGRKGHDGHYWQPLSF 282
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
69-295 2.14e-43

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 157.42  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  69 AIDAHDGEIAYFDGTYYLYGTSydcgFAWqnksapFCGFKVYASPDLVNWTDKGYLFDaKNPVWQSRCNGntyGCFRPHV 148
Cdd:COG3507    28 PGDYPDPSIIRVGDTYYLYGTS----FEY------FPGLPIFHSKDLVNWELVGHALD-RLPQWADPYSG---GIWAPDI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 149 VFNKktGLYVLWVNVYDNVVGFR---VFTSKNPAGPFTEVeNPKLAVNQNAeaaglnnGDHDTFVDDDGKGYVAYTDWRt 225
Cdd:COG3507    94 RYHN--GKYYLYYTAVDGGKNRSgigVATADDPEGPWSDP-GPLVCPGGNG-------IDPSVFVDDDGKAYLVYGSGG- 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 226 kGTIVIEELTDDYLS--GTGKHVKAVTPGK-TEAPGLMKRNGIYYLLYSdpnCGYCSGTG--TSYRTAKSPLGPW 295
Cdd:COG3507   163 -GGIYVAELDPDTGKllGEPKTLAPGGEGGwIEGPHIYKRNGYYYLFYS---EGGTCNSGyaVRVARSKSPTGPY 233
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
71-328 2.74e-28

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: 113.95  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  71 DAHDGEIAYFDGTYYLYGTSydcgFAWqnksapFCGFKVYASPDLVNWTDKGYLFDAKNPVWqSRCNGNTY-GCFRPHvv 149
Cdd:pfam04616   9 FYPDPSILRVGDDYYLTTSS----FEW------FPGIPIFHSKDLVNWKLVGPVLVRRSQLS-GRGSNASWaPDISYH-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 fnkkTGLYVLWVNVYDNVVGfrVFTSKNPAGPFTEVENPKLAVNqnaeaaGLnngDHDTFVDDDGKGYVAYTDWRT---K 226
Cdd:pfam04616  76 ----DGKYYLYYTAVAHGIF--VATADSPDGPWSDPGKLKSGGG------GI---DPSLFHDDDGKKYLVWGGWDPrhgH 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 227 GTIVIEELTDDYLSGTGKHVKAVTPGK-------TEAPGLMKRNGIYYLLYSdpncgyCSGTGTSYR----TAKSPLGPW 295
Cdd:pfam04616 141 GGIYLQELDNDGLKLVGPVTKLIYPGTrwvggkvTEGPHLYKRNGYYYLTYA------AGGTGGPYAvgvaRSRSPLGPY 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2048730172 296 SE--GISISDK-------SCGGQPSFVSTIQFDSETVYLYGS 328
Cdd:pfam04616 215 EWhpGNPILTSrspenpiYGPGHASLVETPDGEWWIVYHAGR 256
 
Name Accession Description Interval E-value
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
70-350 6.56e-125

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: 367.12  E-value: 6.56e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDCGFAWQnKSAPFCGFKVYASPDLVNWTDKGYLFDAknpvwqSRCNGNTYGCFRPHVV 149
Cdd:cd18824     1 IDAHDGKIYFFGGAYYWYGTPYGCGCGSC-GFTLFCGFVVYSSVDLVNWTYRGVLFDP------NTCAGSPGVCFRPHVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDNVVGFRVFTSKNPAGPFTEVENPKLAVnqnaeaAGLNNGDHDTFVDDDGKGYVAYTDWRTKGTI 229
Cdd:cd18824    74 YNARTGRYVLWYNAYDGSSGYAVATSSTPTGPFVTVPDPVLAP------AGLQAGDFSLFVDDDGTGYLAYTTIDFPQSI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 230 VIEELTDDYLSGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDPNCGYCSGTGTSYRTAKSPLGPWSEGI---------- 299
Cdd:cd18824   148 VVEQLTDDYLNTTGEYVRDLIDQEAEAPSIFKRNGIYYILASNTCCGCCQGTGARVYRATSPLGPWTRQIdinscagalf 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 300 --SISDKSCGGQPSFVSTIQF-DSETVYLYGSDLWNNAA-KNEALANYFWAPLKF 350
Cdd:cd18824   228 ppSDSAYTCGGQPTAVLPLPSpGGETLYLYMGDRWRTAPdGRKGHDGHYWQPLSF 282
GH43_CtGH43-like cd08985
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
70-350 3.04e-81

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: 254.56  E-value: 3.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDCGFawqnKSAPFCGFKVYASPDLVNWTDKGYLFDAkNPVWQSRCNGNTYGCFRPHVV 149
Cdd:cd08985     1 IHAHGGGILQEGDTYYWYGESRKGLD----NDNLSHGINCYSSTDLYNWRFEGLVLPA-SGVEVVRDISPGYVIERPKVL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDNVVGFR---VFTSKNPAGPFTEVENPKLavnqnaeaAGLNNGDHDTFVDDDGKGYVAYTDWRTK 226
Cdd:cd08985    76 YNARTRKYVMWFHLDNPNYGFAavgVATSDTPTGPFTFVRSFRP--------DGYPSRDMTLFQDPDGTAYLVRSTDHNT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 227 GtIVIEELTDDYLSGTGKHVKAVTPgKTEAPGLMKRNGIYYLLYSDPnCGYCSgTGTSYRTAKSPLGPWS------EGIS 300
Cdd:cd08985   148 D-IGISRLSDDYLDTTGASSTFKGP-KREAPALFKRGGTYYLITSGL-TGWNP-NPSRLARADSPLGPWStwgnlpVGGP 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2048730172 301 ISDKSCGGQPSFVSTIQFDSETVYLYGSDLWNNAAKNEALANYFWAPLKF 350
Cdd:cd08985   224 GADTTYDSQPAFVFPVEGQGGELFIYMGDRWNPGGGGVGNATYVWLPLLF 273
GH43_CtGH43-like cd18825
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
70-350 6.08e-48

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: 167.78  E-value: 6.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDCGFAWQnksAPFCGFKVYASPDLVNWTDKGYLFDAKNPVWQSRcNGNTYGCFRPHVV 149
Cdd:cd18825     1 IQAHGGGILKHNGTYYWYGEDKTGGTYRR---VDVIGVSCYSSKDLYNWKDEGIVLDAVDDAPASD-LYPNNVVERPKVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDNVVGFR-----VFTSKNPAGPFTEVENPKLavNQNAEAAGLNNG----DHDTFVDDDGKGYVAY 220
Cdd:cd18825    77 YNKKTKKYVMWFHLDGPGADYSraragVAVSDSPTGPFKYLGSFRP--NAGEKNRDFSNGqmsrDMTLFVDDDGKAYLIY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 221 TDWRTKgTIVIEELTDDYLSGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDpncgyCSG---TGTSYRTAKSPLGPWSE 297
Cdd:cd18825   155 SSEENK-TLYIAKLTDDYTGVTGDYARILIGQSREAPAVFKHDGKYYMITSG-----CTGwapNAARYAVADSIFGPWKE 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048730172 298 -------GISISDKSCGGQPSFVSTIQFDSETVYLYGsDLWNnaakNEALAN--YFWAPLKF 350
Cdd:cd18825   229 ignpcrgPNDDADTTFGSQSTFVLPVDGENGKFIYMG-DRWN----PKDLADsrYVWLPITF 285
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
70-350 8.42e-44

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: 156.24  E-value: 8.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSydcgfaWQNKSAPFCGFKVYASPDLVNWTDKGYLFDaknPVWQSRCNGNTYGcFRPHVV 149
Cdd:cd18821     1 IQAHGGGILKVGDTYYWFGED------KTDGSNLFQGVSCYSSTDLVNWTFEGLALP---PQESGDLGPNRVV-ERPKVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDN-----VVGfrVFTSKNPAGPFTEVENPKlavnqnaeAAGLNNGDHDTFVDDDGKGYVAYTDwR 224
Cdd:cd18821    71 YNPSTGKYVMWMHIDSSnygdaRVG--VATSDTVTGPYTYVGSFR--------PLGYESRDIGVFQDDDGTAYLLFED-R 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 225 TKGTIvIEELTDDYLSGTGKhVKAVTPGKTEAPGLMKRNGIYYLLYS-----DPNCGYcsgtgtsYRTAKSPLGPWSEGI 299
Cdd:cd18821   140 DNGLR-IYRLSDDYLSVVEL-VYTFIAAGLEAPAMFKVDGTYYLLGShltgwRPNDNV-------YFTATSLSGPWSEPG 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2048730172 300 SI---SDKSCGGQPSFVSTIQFDSETVYLYGSDLWNnaAKNEALANYFWAPLKF 350
Cdd:cd18821   211 LIapeGTNTYNSQSTFVLPVGGSKKTTYIYMGDRWD--SPDLSASTYVWLPLTI 262
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
69-295 2.14e-43

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 157.42  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  69 AIDAHDGEIAYFDGTYYLYGTSydcgFAWqnksapFCGFKVYASPDLVNWTDKGYLFDaKNPVWQSRCNGntyGCFRPHV 148
Cdd:COG3507    28 PGDYPDPSIIRVGDTYYLYGTS----FEY------FPGLPIFHSKDLVNWELVGHALD-RLPQWADPYSG---GIWAPDI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 149 VFNKktGLYVLWVNVYDNVVGFR---VFTSKNPAGPFTEVeNPKLAVNQNAeaaglnnGDHDTFVDDDGKGYVAYTDWRt 225
Cdd:COG3507    94 RYHN--GKYYLYYTAVDGGKNRSgigVATADDPEGPWSDP-GPLVCPGGNG-------IDPSVFVDDDGKAYLVYGSGG- 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 226 kGTIVIEELTDDYLS--GTGKHVKAVTPGK-TEAPGLMKRNGIYYLLYSdpnCGYCSGTG--TSYRTAKSPLGPW 295
Cdd:COG3507   163 -GGIYVAELDPDTGKllGEPKTLAPGGEGGwIEGPHIYKRNGYYYLFYS---EGGTCNSGyaVRVARSKSPTGPY 233
GH43_CtGH43-like cd18826
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
70-350 2.19e-43

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: 155.10  E-value: 2.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYG-----TSYDCGFaWQNksapfcGFKVYASPDLVNWTDKGYLF-----DAKNPVWQSRCNGn 139
Cdd:cd18826     1 IQAHGGSVIYVDGVYYWYGenkehTDGESGI-WHW------GVRCYSSTDLYNWEDEGLIIppdpdDPSSPLHPTRIMD- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 140 tygcfRPHVVFNKKTGLYVLWVNVY--DNVVGFRVFTSKNPAGPFTEVeNPKLavnqnaEAAGLNNGDHDTFVDDDGKGY 217
Cdd:cd18826    73 -----RPHIIYNEKTGKYVCWLKLYpgGDVQYFGVLTADSPTGPYTYV-HKFL------GPLGMGAGDFDLVVDPDGKAY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 218 VaYTDwRTKGTIVIEELTDDYLSGTGKHVKAVT----PGKTEAPGLMKRNGIYYLLYS-----DPNcgycsgtGTSYRTA 288
Cdd:cd18826   141 L-YFE-RVHKEVVCADLTDDYTDVTGEYSTHFPglgpPFAREAPAVFKRGGKHYLLTSgttgyFPN-------PSEVAVA 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 289 KSPLGPWSegiSISD--------KSCGGQPSFVSTIQFDSETvYLYGSDLWNnaaknealANYFWAPLKF 350
Cdd:cd18826   212 DSYHGPWT---VLGNphvgdgseTSFNSQISSVFKVPGKKDL-YIAMADRWI--------SRYVWLPIRF 269
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
70-350 2.60e-40

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: 146.61  E-value: 2.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDcgfawqnKSAPFCGFKVYASPDLVNWTDKGYLFDAKnpvwqSRCNGNTYGCF--RPH 147
Cdd:cd18822     1 IQAHGGGILKVGGTYYWYGENRD-------NNNGFNGVSLYSSTDLVNWEFRNTVLTRD-----TCSASELASCKieRPK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 148 VVFNKKTGLYVLWVNvYDNVVGFR-----VFTSKNPAGPFT--EVENPklavnqnaeaagLNNGDHD--TFVDDDGKGYV 218
Cdd:cd18822    69 VIYNPKTGKFVMWAH-WENGKDYGlaraaVATSDTPDGDYTfhGSFRP------------LGYDSRDmtLFVDDDGTAYL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 219 AYTDwRTKGTIVIEELTDDYLSGTGKhVKAVTPGKT-EAPGLMKRNGIYYLLYSdpncgYCSG---TGTSYRTAKSPLGP 294
Cdd:cd18822   136 ISAA-NDNADLNIYRLTPDYLSVDSL-VATLFKGQHrEAPALVKRNGYYYLFTS-----GASGwypNQGQYASATSLAGP 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2048730172 295 WSEGISISDKSC-GGQPSFVSTIQFDSETVYLYGSDLWNNA-AKNEALANYFWAPLKF 350
Cdd:cd18822   209 WSSLRNIGNNTTfGSQSTFILPVGGSGGTSYLYMGDRWNSPwGGDLGDSRYVWLPLSF 266
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
74-359 2.49e-35

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: 133.12  E-value: 2.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  74 DGEIAYFDGTYYLYGTSyDcGFAWQNKSApfcgFKVYASPDLVNWTDKGYLFDAKNPVWQsrcnGNTYGcFRPHVVfnKK 153
Cdd:cd09004     2 DPDIVVFGGRYYIYPTT-D-GPPGWSSTS----FHVFSSTDLVNWTDHGIILDLANDVWW----ANKGA-WAPAVA--ER 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 154 TGLYVLWVNVyDNVVGfrVFTSKNPAGPFTEVENPKLAVNQnaeaAGLNNGDHDTFVDDDGKGYVAYTDwrtkGTIVIEE 233
Cdd:cd09004    69 NGKYYFYFSA-GSQIG--VAVSDSPTGPFTDLGRPLVTGGD----YGGQAIDPMVFVDDDGQAYLYWGN----GTAYVAR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 234 LTDDYLSGTGKHVKAVTPGK-TEAPGLMKRNGIYYLLYS-----DPNcgYCsgtgTSYRTAKSPLGPWSEGISISDKSCG 307
Cdd:cd09004   138 LNDDMVSFDGEVVVSITPPNfREGPFVHKRNGIYYLSWSendtrDPD--YR----VRYATSDSPLGPWTYRGVGLLLDSA 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2048730172 308 GQ---PSFVSTIQFDS--ETVYLYgsDLWNNAAKNEALANYFWAPLKFDEKGAIEPV 359
Cdd:cd09004   212 GGikgTGHHSIVQVPGtdEWYIAY--HRFAVPGGDGYHREVAIDRLEFDADGTIRPV 266
GH43_RcAra43A-like cd18823
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ...
70-350 7.67e-35

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: 132.47  E-value: 7.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  70 IDAHDGEIAYFDGTYYLYGTSYDCGFAWQ-----NKSAPFCGFKVYASPDLVNWTDKGYLFDAKNPVWQS-RCNGNTYGC 143
Cdd:cd18823     1 IYSQGGGVFKVGDTYYWYGVKYSGAVTYAantkkNSDTSFKSVTLYSSTDLVNWTFEGNVLTASGAVDTAgDFAGAGWVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 144 fRPHVVFNKKTGLYVL---WVNVYDNVVGFRVFTSKNPAGPFTEVENpklaVNQNAEAAGLNNGDHDTFVDDDGKGYVAY 220
Cdd:cd18823    81 -RPGVAYNSATGKYVLliqWGSTGNGRNGVLFATSDSPTGPFTYQRV----QPMIDNVGTNNTGDQTSFFDDDGKAYLVY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 221 TDWRTKGTIVIEELTDDYLSG--TGKHVKAVTPGKtEAPGLMKRNGIYYLLYSDPNcgYCSGTGTSYRTAKSPLGPWSEG 298
Cdd:cd18823   156 SNDRGRGSLYIAKLRSDYLGIepAVRIDNYVGPGR-EGNALFKYGGTYYLCASDLH--GWNASQTYYMVATSLTGPYSPS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2048730172 299 ISI------SDKSCGGQPSFVSTIQFDSETVYLYGSDLWNNAAKNEALANYfWAPLKF 350
Cdd:cd18823   233 NVLettgpeSDNSHVTQTGFFIPVHGSKGTTYVYCGDRWSDFAGNGIGYNQ-WYPLTF 289
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
73-297 2.27e-32

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: 124.47  E-value: 2.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  73 HDGEIAYFDGTYYLYGTSYDCGFAWqnksapfcGFKVYASPDLVNWTDKGYLF-DAKNPVWqsrcngNTYGCFRPHVVFN 151
Cdd:cd08978     1 ADPSILKDNGRYYIYATTDDTGTGT--------GIVVWKSKDLVNWKEEGTVLsRGKSKSW------GTGNLWAPEVYYF 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 152 KkTGLYVLWVNVYDNVVGFRVF--TSKNPAGPFTEVENPKLAVnqnaeaagLNNGDHDT--FVDDDGKGYVAYTDWRTKG 227
Cdd:cd08978    67 N-SGKWYLYYSAVPNGGGGRIYvaTSDSPEGPFTPIVSGKLGD--------RGSGSIDPtvFVDDDGKLYLYYGDEDDSG 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048730172 228 TIVIEELTDDYLSGTGKhVKAVTPGK---------TEAPGLMKRNGIYYLLYSdpNCGYCSGTGTSYRTAKSPLGPWSE 297
Cdd:cd08978   138 DIYVAELDPDLLTIKGD-VTLLIGEVvgsgfrgnyFEGPAVFKRNGYYYLIYS--AGGTDGGYAIGYATSDSPLGPWEK 213
GH43_F5-8_typeC-like cd18608
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ...
74-359 2.49e-31

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: 122.39  E-value: 2.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  74 DGEIAYFDGTYYLYGTSyDcGFAWQNKSAPFcgfkVYASPDLVNWTDKGYLFDAKNPvwqsrcnGNTYGCFRPHVVFnKK 153
Cdd:cd18608     3 DPSIVKFGGTYYLYATT-D-GWGGFNSGEPV----VWKSKDFVNWKFEGLNWPTKAA-------SGDSKVWAPSVVK-GK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 154 TGLYVLWV----NVYdnvvgfrVFTSKNPAGPFTEVENPKLAVNQNAEAAGLNNGDHDTFVDDDGKGYVAY-TDWRTKGT 228
Cdd:cd18608    69 DGKYYMYVsvgsEIY-------VGVADSPLGPWKNANGDGPPIIPGDGKPNYHMIDAEPFIDDDGKAYLYWgSGLHVNGH 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 229 IVIEELTDDYLSGTGKHVKAVTP-GKTEAPGLMKRNGIYYLLYSDPNCG---YCsgtgTSYRTAKSPLGPWSEG----IS 300
Cdd:cd18608   142 CFAAKLNPDMVTFDGSEPTIVTPrDYFEAPFMFKRNGIYYLMYSGGGCWdetYN----VRYAVSDNPLGPFEEGenspIL 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048730172 301 ISDKSCG--GqPSFVSTIQFDSETVYLY---GSDLWNNAAKNEALANyfwaPLKFDEKGAIEPV 359
Cdd:cd18608   218 QTDEAKGifG-PGHHSVFEEGGQYYILYhrqGYPFSPGGTLRQVCVD----ELNFNADGTIKPV 276
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
79-297 2.47e-30

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: 119.59  E-value: 2.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  79 YFDGTYYLYGTSYDCGFawqnksapfcGFKVYASPDLVNWTDKGYLFDaKNPVWqsrcngNTYGCFRPHVVFNKktGLYV 158
Cdd:cd08991     7 KHNGTYYLYGTGGDDGR----------GFKVYVSDDLVNWEYPGGALE-EPGLW------GTKGFWAPEVFYYN--GKFY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 159 LW--VNVYDNVVGFRVFTSKNPAGPFTEVENPKLAVNQNAEaaglnngDHDTFVDDDGKGYVAYTDWRTKGT----IVIE 232
Cdd:cd08991    68 MYysANGGDHGEHIAVAVSDSPLGPFRDKGKLLIPAGGFSI-------DAHVFIDDDGKWYLYYVRDDLGGEpgnrIYVA 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048730172 233 ELTDDYLS-GTGKHVKAVTPGK------------TEAPGLMKRNGIYYLLYSdPNCgYCSGT-GTSYRTAKSPLGPWSE 297
Cdd:cd08991   141 ELEDDLSLiGEPTLVLCPTADErweygegrdwhtTEGPTVLKHNGTYYLTYS-ANH-FRSPDyAVGYATADSPLGPWTK 217
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
79-358 5.42e-30

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: 118.47  E-value: 5.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  79 YFDGTYYLYgTSYDCgfAWQNKSAPFCGFKVYASPDLVNWTDKGYLFDAKNPVWqsrcnGNTYGCFRPHVVFnkKTGLYV 158
Cdd:cd08990     7 VFNGKVYVY-ASHDE--APANGYFIMDDWHVFSSTDLVNWTDHGEILPPDDVFW-----WASGNAWAPDAVY--KNGKYY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 159 LWVNVYDNVVGFR--VFTSKNPAGPFTEVENPKLAVNQNAEAAGLnngDHDTFVDDDGKGYVaYtdWRTKGTIVIEELTD 236
Cdd:cd08990    77 FYFPVGQASDGFGigVAVSDSPAGPFKDALGKPLIPEGLNGIEGI---DPAVFVDDDGRAYL-Y--FGGGGGYYVAKLKD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 237 DYLSGTGKHVKAVTPGKT---EAPGLMKRNGIYYLLYSDPNCGYCSgtgTSYRTAKSPLGPWS-EGISISDKSCGG-QPS 311
Cdd:cd08990   151 DMISLAGEPQKIKNGGLKgffEAPWVFKRNGTYYLSYAGGWAYPAE---IAYSTADSPLGPYTyRGVILDPVGSGTnHGS 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2048730172 312 FVstiQFDSETVYLYgsdlwNNAAKNEALANY---FWAPLKFDEKGAIEP 358
Cdd:cd08990   228 IV---EFKGQWYLFY-----HTADLSGGGDFRrsvCIDYLHYNADGTIVP 269
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
71-328 2.74e-28

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: 113.95  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  71 DAHDGEIAYFDGTYYLYGTSydcgFAWqnksapFCGFKVYASPDLVNWTDKGYLFDAKNPVWqSRCNGNTY-GCFRPHvv 149
Cdd:pfam04616   9 FYPDPSILRVGDDYYLTTSS----FEW------FPGIPIFHSKDLVNWKLVGPVLVRRSQLS-GRGSNASWaPDISYH-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 fnkkTGLYVLWVNVYDNVVGfrVFTSKNPAGPFTEVENPKLAVNqnaeaaGLnngDHDTFVDDDGKGYVAYTDWRT---K 226
Cdd:pfam04616  76 ----DGKYYLYYTAVAHGIF--VATADSPDGPWSDPGKLKSGGG------GI---DPSLFHDDDGKKYLVWGGWDPrhgH 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 227 GTIVIEELTDDYLSGTGKHVKAVTPGK-------TEAPGLMKRNGIYYLLYSdpncgyCSGTGTSYR----TAKSPLGPW 295
Cdd:pfam04616 141 GGIYLQELDNDGLKLVGPVTKLIYPGTrwvggkvTEGPHLYKRNGYYYLTYA------AGGTGGPYAvgvaRSRSPLGPY 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2048730172 296 SE--GISISDK-------SCGGQPSFVSTIQFDSETVYLYGS 328
Cdd:pfam04616 215 EWhpGNPILTSrspenpiYGPGHASLVETPDGEWWIVYHAGR 256
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
81-310 1.31e-24

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: 103.81  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DGTYYLYGTSYDCGFAWQNKSAPfcgfkVYASPDLVNWTDKGYLFDAKNPVWqsrcNGNTYGCFRPHVVFNKktGLYVL- 159
Cdd:cd18616    18 DGYFYAYATEDPWGDGGGFRLVP-----ILRSKDLVNWEYVGDAFTSKPRWK----WDPGGGLWAPDIRYID--GKYVLy 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 160 -----WVNVYDNVVGfrVFTSKNPAGPFTevenPKLAVNQNAEAAGLNNGDHDtFVDDDGKGYVAYTDWRtkGTIVIEeL 234
Cdd:cd18616    87 yslsdWGADPNPGIG--VATADSPAGPFT----DQGKLFDSNEIGVRNSIDPF-VFEDDGKKYLFWGSFY--GIYAVE-L 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 235 TDDYLSGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDPNCgyCSGTGTSYRT----AKSPLGPW--SEGISISDKSCGG 308
Cdd:cd18616   157 TADGLALKPGEKVQIAGDRYEGPYIVKRDGYYYLFGSAGSC--CEGPNSTYRVvvgrSESLLGPYvdRDGRSLLDSGGGG 234

                  ..
gi 2048730172 309 QP 310
Cdd:cd18616   235 TP 236
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
74-295 1.35e-23

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


Pssm-ID: 350149 [Multi-domain]  Cd Length: 283  Bit Score: 100.81  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  74 DGEIAYFDGTYYLYGTSyDcGFA-WQNKSapfcgFKVYASPDLVNWTDKGYLFDAKNPVWQSRCNGNTYGcfrPHVVfnK 152
Cdd:cd18828     2 DPDIAYFDGKYYIYPTT-D-GFPgWSGTQ-----FHVFSSDDLVTWKDEGVILDLKNDQVVPWATGNAWA---PTIE--E 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 153 KTGLYVLWV--NVYDNVVGFRVFTSKNPAGPFTeVENPKLAVNQNAEAAGLNNGDHDTFVDD-DGKGYVAYTDwrtkGTI 229
Cdd:cd18828    70 RDGKYYFYFcgKNPDGRSQIGVAVADSPTGPFT-AQGSPLITHEMARVTMGQAIDPSVFTDPvDGKYYLYWGN----GYA 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048730172 230 VIEELTDDYLS---GTGKHVKAVTpGKTEAPGLMKRNGIYYLLYSdpncgyCSGTGT-----SYRTAKSPLGPW 295
Cdd:cd18828   145 AIAELNDDMISikpGTLVNLDGLT-DFREAVTVLYRDGLYHFTWS------CDDTGSenyhvNYGTSDSPYGPI 211
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
77-295 2.32e-23

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: 99.91  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  77 IAYFDGTYYLYGTSydcgFAWQNksapfcgFKVYASPDLVNWTDKGYlfDA--KNPVWQSRcNGNTYGcfrPHVVFNKKt 154
Cdd:cd08999    13 VIRVGGTYYAFATN----SGGKN-------VQVATSTDLVTWTLLGG--DAlpDLPAWAAA-GGNTWA---PDVVRRPD- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 155 GLYVLWVNVYDNVVGFR---VFTSKNPAGPFTEVENPKLAVNQNAEAAglnngDHDTFVDDDGKGYVAY-TDWRTKG--- 227
Cdd:cd08999    75 GKYVMYYSARLKSSGKHcigVATSDSPLGPFTPVGEPPLCPLDQGGAI-----DPSGFVDPDGKRYLVYkVDGNSIGvpt 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 228 TIVIEELTDDYLSGTGKHVKAVTPGKT------EAPGLMKRNGIYYLLYSDpNCgYCSGT-GTSYRTAKSPLGPW 295
Cdd:cd08999   150 PIMLQELSADGLTLVGEPVELLLNDGPwdgplvEAPSLVKRDGTYYLFYSS-NC-YCSPSyAVGYATSKSITGPY 222
GH43_XylA-like cd18620
Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium ...
74-295 8.10e-22

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: 95.35  E-value: 8.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  74 DGEIAYFDGTYYLYGtSYDCGFAWQnksapFCG--FKVYASP--DLVNWTDKGYLFDAKNPVWQSRcnGNTYGCFRPHVV 149
Cdd:cd18620     2 DGEPRVFGGRVYLYG-SHDEFGGDE-----YCSndYVVWSAPddDLSNWRYHGVIFRSDQDPDEVP--PGKGLLYAPDVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 fnKKTGLYVL-WVNVYDNVVGfrVFTSKNPAGPFtevENPKLaVNQNAEAAGLNNgDHDTFVDDDGKGYVAYTDWRTKGT 228
Cdd:cd18620    74 --KGPGRYYLyYCLSKGSVEG--VAVSDSPAGPF---EYLGP-VKYPRKGDIFQI-DPAVLVDDDGRVYLYWGQGGSKGA 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048730172 229 ivieELTDDYLSGTGKHVKAVTPGKT-------EAPGLMKRNGIYYLLYSDPNCGycSGTGTSYRTAKSPLGPW 295
Cdd:cd18620   145 ----ELDPDMLTIKPETIVDVPAGITfeghgffEGSSIRKINGIYYLVYSSISRG--RPTELCYATSKSPLGPF 212
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
74-359 6.57e-20

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: 89.64  E-value: 6.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  74 DGEIAYFDGTYYLYGTSydcgfawqnkSAPF---CGFKVYASPDLVNWTDKGYLFDAKNPVWQSRcngntyGCFRPHVVF 150
Cdd:cd18827     2 DPEIRIFDGQYWIYPTY----------SAPYeeqTFFDAFSSPDLVHWTKHERILDMADVPWANR------AVWAPSVIE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 151 nkKTGLYVLW-----VNVYDNVVGFRVFTSKNPAGPFTEVENPKLAvnqNAEAAGLNNGDHDTFVDDDGKGYVAYTDWrt 225
Cdd:cd18827    66 --KNGKYYLYfaandIQSDDEGGGIGVAVADRPEGPFKDALGKPLI---GEFHNGAQPIDQHVFKDDDGQAYLYYGGW-- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 226 kGTIVIEELTDDYLS----GTGKHVKAVTP-GKTEAPGLMKRNGIYYLLYSDPncGYCSGT-GTSYRTAKSPLGPW-SEG 298
Cdd:cd18827   139 -GHCNVAKLNDDMTSlvpfDDGETFKEITPeGYVEGPFMFKRNGKYYFMWSEG--GWTGPDySVAYAVADSPLGPFkRIG 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048730172 299 -ISISDKSCGGQPSFVSTIQFDsetvylyGSDLW----NNAAKNEALANY---FWAPLKFDEKGAIEPV 359
Cdd:cd18827   216 kILQQDPAIATGAGHHSVVNVP-------GTDDWyivyHRRPLGETDGNHrvvCIDRMEFNEDGTIKPV 277
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
73-295 5.36e-19

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: 87.19  E-value: 5.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  73 HDGEIAYFDGTYYLYGTSYDCGfawqnksapfcGFKVYASPDLVNWTDKGYLFdAKNPVWQSRCNGNTYG-CFRPHVVFN 151
Cdd:cd08988     1 HDPSIIKEGGTYYAFGTGTDGF-----------GIPIAKSKDLGNWTIVGEAF-ATLPSWKGGSPPSADGnLWAPDISQH 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 152 KktGLYVLWVNVYDNVVGFR---VFTSKNPAGPFTEVENPKLAVNQNAEAaglNNGDHDTFVDDDGKGYVAYTDWrtKGT 228
Cdd:cd08988    69 K--GKYYLYYSVSDNGSNTSaigLATANNPQGPFKDEGPAKPVVTSDNAG---NAIDPDLFQDEDGQNWLLYGSF--WGG 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 229 IVIEELTDDYL----SGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDPNCgyCSGTGTSYRTA----KSPLGPW 295
Cdd:cd08988   142 IWLQKLDKNGLvvnpPGNGKSIAVLYYVSIEAPYITYAGGYYYLFVSAGSC--CDGGNSTYHTRvgrsKKVTGPY 214
GH43_Xsa43E-like cd18618
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ...
80-296 8.87e-19

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: 86.50  E-value: 8.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  80 FDGTYYLYgTSYDcgfawqNKSAPFCGFK-----VYASPDLVNWTDKGYLFDAKNPVWQSrcngntYGCFRPHVVFNKkt 154
Cdd:cd18618    10 HGDTVYLY-TGHD------EAPPGGTFFVmndwrVFSTTDMVNWTDHGAVLSLKDFSWAK------GDAWAGQVIERN-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 155 GLYVLWVNVYDNVVGFR---VFTSKNPAGPFTEVENPKLAVNQNAEAAGLNNGDHD--TFVDDDGKGYVAYTDWRTKGTi 229
Cdd:cd18618    75 GKFYWYVPVHHKTNGGFaigVAVSDSPTGPFKDALGKPLITNDMTGTTNHSWDDIDptVFIDDDGQAYLYWGNPELYYV- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 230 vieELTDDY--LSGTGKHVKAVTPGK-TEAPGLMKRNGIYYLLYSdpnCGYCSGTGtsYRTAKSPLGPWS 296
Cdd:cd18618   154 ---KLKEDMisLDGEIGTIDISGLPDfTEAPWVHKRNGLYYLSYA---AGFPEKIA--YATSDSPTGPWT 215
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
112-308 2.05e-18

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: 85.26  E-value: 2.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 112 SPDLVNWTDKGYLFD--AKNPVWQSRCNGNTYG------CFRPHvvfnkkTGLYVLWVNVYDNvvGFRVFTSKNPAGPFT 183
Cdd:cd09001    41 SKDLVNWEIVGYVVDrlDDGDAYYLEDGKNAYGkgiwapSLRYH------NGKFYVYFCTNTG--GTYVYTADDPAGPWS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 184 EVENPKlavnqnaeaaglnNGDHDT--FVDDDGKGYVAYtdwrTKGTIVIEELTDDYLSGTGKHVKAVTPGKT----EAP 257
Cdd:cd09001   113 RPALIG-------------KGYHDPslLFDDDGKAYLVY----GNGEIRLTELSPDGTGVGGEGRVIIDGTEEglgaEGS 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2048730172 258 GLMKRNGIYYLLYSDPNCGycSGTGTSYRtAKSPLGPWSEGISISDKSCGG 308
Cdd:cd09001   176 HLYKINGYYYIFNIEWGGG--GRTQVVLR-SKSLYGPYEGRVVLDDGSGTG 223
GH43_XynD-like cd09003
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ...
80-295 4.23e-18

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: 85.39  E-value: 4.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  80 FDGTYYLYGTS--YDCGFAWQNKSAPFCGFK---VYASPDLVNWTDKGYLFDAKNPVWqSRCNGNTYGcfrPHVVFNKKT 154
Cdd:cd09003    17 YNGRVYVYGTNddQQYNANGKKKDNSYYNINsltVISSDDMVNWTDHGEIPVAGPNGI-AKWAGNSWA---PSVAYKNIN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 155 GLYVLWVNVYDNVVGFRVFTSKNPAGPFTEvENPKLAVNQNAEAAGLNNG--DHDTFVDDDGKGYVAY------TDWRTK 226
Cdd:cd09003    93 GKDKFYLYFANGGGGIGVLTADSPTGPWTD-PLGKPLITRSTPGCAGVVWlfDPAVFIDDDGQGYLYFgggvpgGSEANP 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048730172 227 GTIVIEELTDDYLSGTGKHVKAVTPGKTEAPGLMKRNGIYYLLYS----DPNCGYCSGTGT-SYRTAKSPLGPW 295
Cdd:cd09003   172 KTARVIKLGDDMISVDGSAVTIDAPYFFEASGINKINGKYYYSYCtnfsGRDDPAYPGAGSiAYMTSDNPMGPF 245
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
81-297 2.82e-13

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: 69.95  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DGTYYLYGTSYDCGFAWQNKsapfcGFKVYASPDLVNWTDKGYLFD-------AKNPVWQSRCNGNTYGCFRPHVVFNKK 153
Cdd:cd08986    12 DGYYYLTGTTGGPDWWGVND-----GIRLWRSKDLKDWEYLGLVWDlekdgwwQWEPQWWTPDSKNKRALWAPEIHYING 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 154 TglyvlWVNVY---DNVVGFRVFTSKNPAGPFTEVENPKLavnqnaeaaglnNGDHDT--FVDDDGKGYVAYTDwrtkGT 228
Cdd:cd08986    87 T-----WYITHsmnGGGTGLLKSTTGKPEGPYVDPMGGPL------------GKGIDPslFEDDDGTVYLVWGN----GQ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048730172 229 IVieELTDDyLSGTGKHVKAVTPGKTEAPG-----LMKRNGIYYLLYSDPNcGYCSGTGT---SYRTAKSPLGPWSE 297
Cdd:cd08986   146 IA--RLKKD-MSGFAEEPRKIDPSGNREIGhegafIFKIGGKYVLFGAAWS-TDKMRKGTydlYYATSDSIYGPYSE 218
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
72-294 1.14e-12

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: 68.34  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  72 AHDGEIAYF-DGTYYLYGTSYdcgfawqnksapfcGFKVYASPDLVNWTDKGYLFDAKNPVWQSRCNGNTYGCFRPHVVF 150
Cdd:cd08998     1 VHDPSIIKDdGGTYYVFSTGA--------------GIQIRTSKDLVNWEFVGTVFPEGPAWAAAEVPGGAGGLWAPDVVY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 151 NKktGLYVLwvnvYDNVVGF-------RVFTSKNPA-GPFT---EVENPKLAVNQNAEAAGLnngdhdtFVDDDGKGYVA 219
Cdd:cd08998    67 VN--GRYYL----YYSASTFgsnrsaiGLATSTTLDdGPWTdqgLVVSSSPGDDYNAIDPNV-------FVDADGRLWLA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 220 YTDWRTkGTIVIE---ELTDDYLSGTGKHVkAVTPGKT---EAPGLMKRNGIYYLLYSDPNCgyCSGTGTSYRT----AK 289
Cdd:cd08998   134 YGSFWG-GIKLVEldpATGKLRPGSTGTSI-ASRPGGPgaiEAPYIIYRGGYYYLFVSYGSC--CRGANSTYNIrvgrST 209

                  ....*
gi 2048730172 290 SPLGP 294
Cdd:cd08998   210 SITGP 214
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
81-295 3.33e-12

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: 67.15  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DGTYYLYGTSydcgFAWqnksapFCGFKVYASPDLVNWTDKGYLFDaKNPVWQSRCNGNTYGCFRPHVVFNKKTgLYVLW 160
Cdd:cd18617    17 GDDYYLVTSS----FEY------FPGLPIYHSKDLVNWELIGHALD-RPSQLDLRGVPSSGGIFAPTIRYHDGR-FYIIT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 161 VNVYDNVVGFRVFTSKNPAGPFTE---VENPklavnqnaeaaglnnG-DHDTFVDDDGKGYVAYTD-----WRTKGTIVI 231
Cdd:cd18617    85 TNVSTDGRGNFIVTADDPAGPWSDpvwLDGP---------------GiDPSLFFDDDGKVYLTGTGpppdpYEGHGGIWQ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 232 EEL---TDDYLSGTGKHVKAVTPGK-TEAPGLMKRNGIYYLLysdpncgyCSGTGTSY-------RtAKSPLGPW 295
Cdd:cd18617   150 QEIdleTGKLLGEPKVLWNGGTGGRwPEGPHLYKIDGWYYLL--------IAEGGTEEghsetiaR-SRSPWGPY 215
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
84-295 2.12e-11

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: 64.69  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  84 YYLYGTSydcgFAWqnksapFCGFKVYASPDLVNWTDKGYLFDAKN-----PVWQSRcngntyGCFRPHVVF-NKKTGLY 157
Cdd:cd08989    20 YYMVNST----FQY------FPGIPISHSKDLVHWTPIGHALTRPEqldltGGPDGG------GIWAPDISYhDGKFYIY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 158 VLWVNVYDNVVGFR--VFTSKNPAGPFTEvenpklavnqnaeAAGLNNGDHDT--FVDDDGKGYVAYTdwrtKGTIVIEE 233
Cdd:cd08989    84 YTVVLNVGSWKGRRnyLVTSEDPEGPWSE-------------PVWLDEGGIDPslFVDDDGKHYMLLN----PGGIRLAE 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048730172 234 LTDD--YLSGTGKHVKAVTPGK-TEAPGLMKRNGIYYLLYSDPncgycsGTGTSYRT----AKSPLGPW 295
Cdd:cd08989   147 LNPDctKQIGEPKRIWEGTGGRaPEGPHLYKKDGYYYLLTAEG------GTGYGHAItiarSKTIYGPY 209
GH43-like cd08982
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
77-296 2.80e-11

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


Pssm-ID: 350096 [Multi-domain]  Cd Length: 308  Bit Score: 64.51  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  77 IAYFDGTYYLYGTSydCGFAWqnksapfcgfkvyASPDLVNWTDKgylfdaknpvwqsRCNGNTYGCFRPHVVfnkktgl 156
Cdd:cd08982    10 VVLFKGKYYLFASK--SGGYW-------------HSDDLVNWKFI-------------PTNGLPIEDYAPTVV------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 157 yvlwvnVYDNVVGF-------RVFTSKNPAGPFTEVenpklavnqnAEAAGLNN-GDHDTFVDDDGKGYVAYtDWRTKGT 228
Cdd:cd08982    55 ------EINGTLYFtasggpgPIYRTDDPLGGKWEL----------VAESGPFGfWDPALFVDDDGRLYLYW-GCSNKDP 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 229 IVIEELTDDYLSG-TGKHVKAVTPGKT--------------------EAPGLMKRNGIYYLLYSDPncgycsgtGTSYRT 287
Cdd:cd08982   118 IYGVELDPNTGFRpIGEPVPLISFDPDkhgwerfgednedpglapwiEGAWMTKHNGKYYLQYAAP--------GTEFKT 189
                         250
                  ....*....|....*.
gi 2048730172 288 -------AKSPLGPWS 296
Cdd:cd08982   190 yadgvyvSDSPLGPFT 205
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
77-295 6.07e-10

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: 60.34  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  77 IAYFDGTYYLYGTSYdcgfawqnksAPFCGFKVYASPDLVNWTDKGYLFDAKN--PVWQSRCNGNTYGCFRPHVVFNKKT 154
Cdd:cd18833    16 VPEWDGTFFCVTSSF----------LAFPGIPIYASKDLINWKLISNVLSRPSqlPELATTGTGQQGGIWAPTLRYHDGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 155 gLYVLWVNVYDNVVGFR-----VFTSKNPAGPF-----TEVENPKLavnqnaeaaglnngDHDTFVDDDGKGYVAY-TDW 223
Cdd:cd18833    86 -FYVITTLVFPDKTDASrwdnlLFTTTDPYSDSawsdpIRFDFPGY--------------DPDLFWDDDGTAYVQGaHYW 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048730172 224 RTKGTIVIEEL-TDDYLSGTGKHVKAVTPGKT-EAPGLMKRNGIYYLLYSDpncgycSGTGTSYRTA----KSPLGPW 295
Cdd:cd18833   151 RVRPEIQQQEIdLKTGESLSPSPIWNGTGGSApEGPHMYKKDGWYYLLIAE------GGTGLGHSVTiarsRSIWGPY 222
GH43_Bt1873-like cd08981
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This ...
81-295 8.72e-09

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: 56.76  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DGTYYLYGTSYDCGFAWQNKsapfcGFKVYASPDLVNWTDKGYLFDAKNPVWQSRCNgntygcFRPHVVFNKktGLYVLW 160
Cdd:cd08981    17 TGTYYLYGTTDKDCWWGKGT-----GFDVYVSKDLENWEGPYEVFRPPEDFWADRNF------WAPEVHEYN--GKYYLF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 161 VNVYDNVVGFR---VFTSKNPAGPFTEVEN----PKlavnqnaeaaglnngDHDT-----FVDDDGKGYVAY-------T 221
Cdd:cd08981    84 ATFKAEGNGRRgtqILVSDSPLGPFVPLSDgpvtPE---------------DWMCldgtlYVDEDGKPWMVFchewvqvG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 222 DwrtkGTIVIEELTDDYLSGTGK------------HVKAVTPGK------TEAPGLMK-RNGIYYLLYSD-PNCGYCSGt 281
Cdd:cd08981   149 D----GTICAVRLSDDLKEAIGEpvllfraseapwARPIPEFGIggpgyvTDGPFLYRtKDGKLLMLWSSfGEGGYAIG- 223
                         250
                  ....*....|....*...
gi 2048730172 282 gtsyrTAKSP----LGPW 295
Cdd:cd08981   224 -----VARSEsgkiTGPW 236
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
82-285 2.52e-08

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: 55.63  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  82 GTYYLyGTSydcGFAWqnksapFCGFKVYASPDLVNW-------TDKGYLFDAKNP----VWQsrcngntygcfrPHVVF 150
Cdd:cd09000    18 DDYYI-ATS---TFEW------FPGVQIHHSKDLVNWelvarplTRVSQLDMRGNPdsggIWA------------PCLSY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 151 NKktGLYvlWVnVYDNVVGFR---------VFTSKNPAGPFTEvenPKLavnqnaeaagLNNGDHDT--FVDDDGKGYVA 219
Cdd:cd09000    76 AD--GKF--WL-VYTDVKSVDgpfkdvhnyLVTAESIEGPWSE---PIY----------LNSSGFDPslFHDDDGRKYLV 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048730172 220 YTDWRTK------GTIVIEELTDD--YLSGTGKHV-KAVTPGKTEAPGLMKRNGIYYLLysdpncgyCSGTGTSY 285
Cdd:cd09000   138 NMLWDHRpghnrfAGIVLQEFDPEtkKLVGERKVIfKGTELGLTEGPHLYKRDGYYYLL--------TAEGGTGY 204
GH43_CoXyl43_like cd18619
Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase ...
170-294 1.15e-07

Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Included in this subfamily is the metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43, which shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350131 [Multi-domain]  Cd Length: 313  Bit Score: 53.46  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 170 FR--VFTSKNPAGPFTEVENPklavnqnaeAAGLNNGDHDTFVDDDGKGYVAY--------TDWRTKGTIV--------- 230
Cdd:cd18619   102 FRigVAVSDKPEGPFKPEPEP---------IKGSYSIDPAVFVDDDGSYYLYFggiwggqlQRWQTGSYVSgdgdepqdd 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 231 -------IEELTDDYLS------------GTGKHVKAvtpGKT-----EAPGLMKRNGIYYLLYSdpncgycsgTGTS-- 284
Cdd:cd18619   173 epalgprIAKLSPDMLSfaeppreivildEDGKPLLA---GDHdrrffEGPWMHKYNGKYYLSYS---------TGDThl 240
                         170
                  ....*....|..
gi 2048730172 285 --YRTAKSPLGP 294
Cdd:cd18619   241 lvYATSDNPYGP 252
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
81-295 1.15e-07

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: 53.39  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DG-TYYLYGTSYDcgfawqnkSAPfcGFKVYASPDLVNWTDKGY-LFDAKNPVWQsrcngntygcfrPHVVfnKKTGLYV 158
Cdd:cd09002    18 DGdDYYMTHSSFD--------YYP--GLLIWHSRDLVNWEPIGAaLTEYIGTVWA------------PDLI--KHDGRYY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 159 LWVNVYDNvvGFRVFTSKNPAGPFTEVENPKLAvnqnaeaaglNNGDHDTFVDDDGKGYVaYTDwrtKGTIVieELTDDY 238
Cdd:cd09002    74 IYFPAKGG--TNYVITADDIAGPWSEPIDLKVG----------SGIDPGHVVDEDGKRYL-FLS---GGRRV--RLTDDG 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048730172 239 LSGTGKHVKAVTPGK-----------TEAPGLMKRNGIYYLLYSDpncGYCSGTGTS-----YRtAKSPLGPW 295
Cdd:cd09002   136 LSVAGPPEKVYDGWRypdewdvecfcLEGPKLFRRGGYYYLTTAQ---GGTAGPPTShmvvsAR-SKSPHGPW 204
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
72-288 1.35e-06

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: 49.97  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  72 AHDGEIAYFDGTYYLYGTsydcGFawqnksapfcGFKVYASPDLVNWTDKGYLFDaKNPVWQSRC----NGNTYGcfrPH 147
Cdd:cd18830     1 VHDPVMAREGGTYYLFST----GP----------GISVMSSKDLKNWTQERPVFD-EPPQWAKEAvpgfNGHIWA---PD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 148 VVFNKktGLYVLWVNVY---DNVVGFRVFTSK--NPAGPFTEVENPKLAVNQNAEAAGLNNGDHDTFVDDDGKGYVAY-T 221
Cdd:cd18830    63 ISFHN--GRYYLYYSCSafgKNTSAIGVATNKtlDPDSPDYKWEDHGMVVQSVPGRDLWNAIDPNVIVDEKGTPWLSFgS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 222 DWrtkGTIVIEELTDDYLS---------------GTGKHVKAVTPGKTEAPGLMKRNGIYYLLYSDPNCgyCSGTGTSYR 286
Cdd:cd18830   141 FW---GGIKLVKLDPDLKSlaepqewhtiarrerTFKLTDSEAGPGAIEAPFIFKKGGYYYLFVSWDYC--CRGVNSTYK 215

                  ..
gi 2048730172 287 TA 288
Cdd:cd18830   216 VV 217
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
74-295 3.03e-06

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: 48.75  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  74 DGEIAYFDGTYYLYGTSydcgfaWQNKSAPFCGFkvYASPDLVNWTDKGylfdaknPVWQSRCNG--NTYGCFRPHVVFN 151
Cdd:cd08772     2 DPSVVPYNGEYHLFFTI------GPKNTRPFLGH--ARSKDLIHWEEEP-------PAIVARGGGsyDTSYAFDPEVVYI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 152 KKTglYVLWVNVYDNVVGFR------VFTSKNPAGPFTEVENPkLAVNQNAEAAglNNGDHDTFVDDDGKGYVAYTDWRT 225
Cdd:cd08772    67 EGT--YYLTYCSDDLGDILRhgqhigVAYSKDPKGPWTRKDAP-LIEPPNAYSP--KNRDPVLFPRKIGKYYLLNVPSDN 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048730172 226 KGT----IVIEELTDDYLSGTGKHVKAVTP--GKTEAPGLMKRNGIYYLLYS-DPNCGYcsGTGTSYRTAKSPLGPW 295
Cdd:cd08772   142 GHTrfgkIAIAESPD*LHWINHSFVYNYNEqgKVGEGPSLWKTKGGWYLIYHaNTLTGY--GYGFGYALGDLDDPSK 216
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
81-277 5.72e-06

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: 48.00  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DGTYYLYGTSYDCGFAWQNKSAPfcGFKVYASPDLVNWTDKGYLFDAKNPvwqsrcngNTYGCFRPHVVFNKKTGLYVL- 159
Cdd:cd08983    29 DGKFYLVATDLWIAGGAQWNGSR--GIGVWESTDLVNWSEQRLVKMVSPP--------NAGNAWAPEAIYDPETGQYVVy 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 160 W---VNVYDNVVGFRVFTSKnpAGPFTEVENPKLavnqnaeaaGLNNGDH--DTFVDDDGKGYVAYT-DWRTKGTIVIE- 232
Cdd:cd08983    99 WsssLYGDGGGGNHRIYYAT--TKDFKTFSEPKV---------LFDPGFNviDTTIVKDGGTYYRFYkDETTGKGIRLAt 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2048730172 233 --ELTDDYlSGTGKHVKAVTPGKTEAPGLMKRNGI--YYLLYSD-PNCGY 277
Cdd:cd08983   168 sdSLTGPW-TTVTTGGGAGTGGGVEGPTVFKLNDGgkWYLYYDQyGGGGY 216
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
72-308 6.26e-06

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: 48.13  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  72 AHDGEIAYFDGTYYLYGTSYdcgfawqnksapfcGFKVYASPDLVNWTDKGYLFDAKNPVWQSRC-NGNTYGCFRPHVV- 149
Cdd:cd18829     1 THDPSIIKEGSTWWTFSTGD--------------GIPVKYSSDGLNWTQGPPIFGSPLSWWKTYVpANTTNDVWAPDVHy 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 150 FNKKTGLYVLWVNVYDN--VVGFrVFTSKNPAGPFTEvenpKLAVNQNAEAAGLNNGDHDTFVDDDGKGYVAYTDWRTKg 227
Cdd:cd18829    67 YNGKYWLYYAISTFGSNtsAIGL-ASASSIAAGNWTD----EGLVLRSTSADNYNAIDPNLVIDASGNPWLVFGSFWSG- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 228 tIVIEELTDDYLSGTGKHVK--AVTPGKTEAPGLMKRNGIYYLLYSDPNCgyCSGTGTSYRTA----KSPLGPWSEGISI 301
Cdd:cd18829   141 -IKITRLDKATMKPTGSIYSiaSRPSGGIEGPFIVYRDGYYYLFVSIDKC--CRGVNSTYKIAygrsTSITGPYLDKNGK 217

                  ....*..
gi 2048730172 302 SDKSCGG 308
Cdd:cd18829   218 DMLNGGG 224
GH_J cd08979
Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase ...
79-297 6.70e-06

Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and 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. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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: 350093 [Multi-domain]  Cd Length: 292  Bit Score: 47.95  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  79 YFDGTYYLYGTSYDCGFAWQNKSApfcgFKVYaSPDLVNWTDKGYLFDAKNPVwqsrcNGNTYGCFRPHVVFNKKTGLYV 158
Cdd:cd08979     8 NANGYYHLFYLYGPPKNFADNVSI----GHAY-SKDLENWIDLPKALGANDTI-----SDDQTQEWSGSATFTSDGKWRA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 159 LWVNVYDNVVGFRVFT---SKNPAGPFTEVENPklaVNQNAEAAGLNNGDHDTFVD------DDGKGYVAYTDWRT--KG 227
Cdd:cd08979    78 FYTGFSGKHYGVQSQTiaySKDLASWSSLNING---VPQFPDELPPSSGDNQTFRDphvvwdKEKGHWYMVFTAREgaNG 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048730172 228 TIVIEELTDDYlsgtgkHVKAVTP--------GKTEAPGLMKRNGIYYLLYSDPNCGYCSGTGTSYRTAKSPLGPWSE 297
Cdd:cd08979   155 VLGMYESTDLK------HWKKVMKpiasntvtGEWECPNLVKMNGRWYLFFGSRGSKGITSNGIHYLYAVGPSGPWRY 226
GH43_62_32_68_117_130-like cd08994
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
68-228 3.33e-05

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


Pssm-ID: 350108 [Multi-domain]  Cd Length: 294  Bit Score: 45.72  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  68 DAIDAHDGEIAYFDGTYYLYGTSYDCGFAWQNKSAPFCGFK---VYASPDL-VNWT-DKGYLFDAKNPVWQSRCNGNTYG 142
Cdd:cd08994    76 DGDTTHNPTIKKFDGKYYLYYIGNTGPGPDPPLWWGHRNNQrigVAVADSPnGPWKrFDKPILDPRPRSWDDLITSNPAV 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 143 CFRPhvvfnkkTGLYVL----WVNVYDNVVGFRVFTSKNPAGPFTEVENP---KLAVNQNAEaaglnngdhDTFV-DDDG 214
Cdd:cd08994   156 LKRP-------DGSYLLyykgGKKNPGGNRKHGVAVSDSPEGPYTKLSDPpvyEPGVNGQTE---------DPFIwYDKG 219
                         170
                  ....*....|....
gi 2048730172 215 KGYVAYTDWRTKGT 228
Cdd:cd08994   220 QYHLIVKDMGGIFT 233
GH32_EcAec43-like cd08995
Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 ...
81-296 4.92e-05

Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2); This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). GH32 family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) 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. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize.


Pssm-ID: 350109 [Multi-domain]  Cd Length: 281  Bit Score: 45.26  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  81 DGTYYLYGTSYDCGFAwqnksAPFCGFKVYASPDLVNWTdkgylfdaKNPVWQSRCNGNTYGC--FR-PHVVFNKKTGLY 157
Cdd:cd08995    71 DGTYHAFYTGHNPDFG-----KPKQVIMHATSTDLKTWT--------KDPEFTFIADPEGYEKndFRdPFVFWNEEEGEY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 158 VLWVnvydnvvgfrvftsknpagpftevenpklavnqnaeAAGLNNGDHDtfvdddGKGYVAY------TDWRTKGTIVi 231
Cdd:cd08995   138 WMLV------------------------------------AARKNDGPGN------RRGCIALytskdlKNWTFEGPFY- 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048730172 232 eeltddylsgtgkhvkavTPGKT---EAPGLMKRNGIYYLLYSDpncgYCSGTGTSYRTAKSPLGPWS 296
Cdd:cd08995   175 ------------------APGSYnmpECPDLFKMGDWWYLVFSE----FSERRKTHYRISDSPEGPWR 220
GH43_GsAbnA-like cd18832
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ...
73-277 9.45e-05

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


Pssm-ID: 350153 [Multi-domain]  Cd Length: 332  Bit Score: 44.55  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172  73 HDGEIAYFDGTYYLYGTSYdcGFAWqnksapfcgfkvyaSPDLVNWTDKGYLFDAKNPV------------WQSRCNGNT 140
Cdd:cd18832     2 HDPSIVKDDGTYYVFGSHL--AAAK--------------STDLMNWTQFTNGVTTDNPLlfnlfdstawelAEDFNWAGG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 141 YGCFRPHVVFNKKTGLYVLWVNVydNVVGFR----VFTSKNPAGPFTEV---------------ENPKLAVNQNAEAAGL 201
Cdd:cd18832    66 GNLWAPDVIYNKAMGKYCMYYSV--SGDDSPsaigLATADNIEGPYTYKgtvlksgftgstsadADVYLTGGKYNNNYHP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 202 NNGDHDTFVDDDGKGYVAYTDWrtKGTIVIEEL------------TDDYLS--GTGKHVKAVTPGKTEAPGLM--KRNGI 265
Cdd:cd18832   144 NAIDPCVFYDKDGKLWMVYGSW--SGGIFLLELdpktglrdysveTDGNLPdqYYGKKIAGGYHASGEGPYILydKDTGY 221
                         250
                  ....*....|....*.
gi 2048730172 266 YYLLYS----DPNCGY 277
Cdd:cd18832   222 YYLFVSygglDANGGY 237
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
252-333 5.01e-03

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: 38.96  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048730172 252 GKTEAPGLM-KRNGIYYLLYSDPNCGycSGTGTSYRTAKSPLGPWSEGISISDKSCGGQPSFVSTIQFDSETVYLYGSDL 330
Cdd:cd08978    56 GNLWAPEVYyFNSGKWYLYYSAVPNG--GGGRIYVATSDSPEGPFTPIVSGKLGDRGSGSIDPTVFVDDDGKLYLYYGDE 133

                  ...
gi 2048730172 331 WNN 333
Cdd:cd08978   134 DDS 136
 
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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