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Conserved domains on  [gi|839533633|gb|KMG09349|]
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xylan 1,4-beta-xylosidase [Klebsiella pneumoniae]

Protein Classification

glycoside hydrolase family 43 protein( domain architecture ID 14406677)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
 6-307 0e+00

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


:

Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 515.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGIWAPALSWADGQF 85
Cdd:cd09000    1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTDVKVTEGAFKDMTNYLTTAKDIRGPWSDPIKLNGVGFDASLFHDDDGRKYIVQQTWDHREYHHPFDGITLTELDT 165
Cdd:cd09000   81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 166 KTLKLMPEtARTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEAdSFETEPGDVFLTNVDTPDSY 245
Cdd:cd09000  161 ETKKLVGE-RKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFG-PYEVDPDNPLLTSWDDPENP 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839533633 246 IQKQGHGALVSTPEGEWYYASLCARPWNrpgesiydPRGWSTLGRETAIQKVYWDDEGWPRI 307
Cdd:cd09000  239 LQKAGHGSLVETPDGEWYLAHLCGRPLP--------GRGRCPLGRETAIQKVEWTDDGWPRL 292
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
 336-537 3.44e-61

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


:

Pssm-ID: 436093  Cd Length: 203  Bit Score: 200.57  E-value: 3.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  336 DDFTSPALDPNWNTLRVPFTAKMG--TTGDGKLTLIGQGSLANTHDLSLIARRWQAFYFDAAVKVKFEPFSYQQMAGLTN 413
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDESWYslTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  414 YYNDRHWSFVFLTWNEINGKVIEVGENNRGKYTSYLKDNAIKVPDGVEYVWFRTKVRKQTYSYEYSFDGVTFTEIPVQLD 493
Cdd:pfam17851  82 YYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPELD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 839533633  494 AAVLSDDYVLqsyGGFFTGAFVGLAAVDY-AGYGTQAEFYQFEYQ 537
Cdd:pfam17851 162 ASILSDEYAA---GGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
 6-307 0e+00

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


Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 515.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGIWAPALSWADGQF 85
Cdd:cd09000    1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTDVKVTEGAFKDMTNYLTTAKDIRGPWSDPIKLNGVGFDASLFHDDDGRKYIVQQTWDHREYHHPFDGITLTELDT 165
Cdd:cd09000   81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 166 KTLKLMPEtARTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEAdSFETEPGDVFLTNVDTPDSY 245
Cdd:cd09000  161 ETKKLVGE-RKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFG-PYEVDPDNPLLTSWDDPENP 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839533633 246 IQKQGHGALVSTPEGEWYYASLCARPWNrpgesiydPRGWSTLGRETAIQKVYWDDEGWPRI 307
Cdd:cd09000  239 LQKAGHGSLVETPDGEWYLAHLCGRPLP--------GRGRCPLGRETAIQKVEWTDDGWPRL 292
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
 4-305 1.91e-100

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: 305.01  E-value: 1.91e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633    4 IQNPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSggiWAPALSWADG 83
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   84 QFWLVYTDVKvtegafkdMTNYLTTAKDIRGPWSDPIKL--NGVGFDASLFHDDDGRKYIVQQTWDHReyhHPFDGITLT 161
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLksGGGGIDPSLFHDDDGKKYLVWGGWDPR---HGHGGIYLQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  162 ELDTKTLKLMPETARTIYRGTA---VALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLeADSFETEPGDVFLTN 238
Cdd:pfam04616 147 ELDNDGLKLVGPVTKLIYPGTRwvgGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSP-LGPYEWHPGNPILTS 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839533633  239 VDtPDSYIQKQGHGALVSTPEGEWYYASLCARPwnrpgesiydPRGWSTLGRETAIQKVYWDDEGWP 305
Cdd:pfam04616 226 RS-PENPIYGPGHASLVETPDGEWWIVYHAGRP----------GDGGYGLGRETRIQPVEWRADGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
4-416 1.47e-94

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 292.62  E-value: 1.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   4 IQNPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLdmkGNPSSGGIWAPALSWADG 83
Cdd:COG3507   22 YTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  84 QFWLVYTDVKVTEGAFKdmtNYLTTAKDIRGPWSDPIKL---NGVGFDASLFHDDDGRKYIVqqtwdhreYHHPFDGITL 160
Cdd:COG3507   99 KYYLYYTAVDGGKNRSG---IGVATADDPEGPWSDPGPLvcpGGNGIDPSVFVDDDGKAYLV--------YGSGGGGIYV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 161 TELDTKTLKLMPETaRTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGT-VFTHQEVVARSKTLEADsFETEPGDVFLTNV 239
Cdd:COG3507  168 AELDPDTGKLLGEP-KTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTcNSGYAVRVARSKSPTGP-YEDAPGNPILTQR 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 240 DtpDSYIQKQGHGALVSTPEGEWYYASLCARPWNrpgesiydprgwsTLGRETAIQKVYWDDEGWPRIEGGhGGKTFVEG 319
Cdd:COG3507  246 S--DGGIQGPGHGSLVETPDGEWYLVYHAYRPPG-------------GLGRETFLDPVTWNEDGWPVVGPG-TGEPPQPL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 320 PKdaiftesasdnSQQDDFTSPaLDPNWNTlrvpftakmgttgdGKLTLIGQgslanthdlsliarrwqafyFDAAVKVk 399
Cdd:COG3507  310 PA-----------PESDDFDGP-LGLQWSL--------------GYLRLTRQ--------------------FTATTKL- 342

                        410
                 ....*....|....*..
gi 839533633 400 fepfsyqqMAGLTNYYN 416
Cdd:COG3507  343 --------RAGLVLYGN 351
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
 336-537 3.44e-61

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


Pssm-ID: 436093  Cd Length: 203  Bit Score: 200.57  E-value: 3.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  336 DDFTSPALDPNWNTLRVPFTAKMG--TTGDGKLTLIGQGSLANTHDLSLIARRWQAFYFDAAVKVKFEPFSYQQMAGLTN 413
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDESWYslTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  414 YYNDRHWSFVFLTWNEINGKVIEVGENNRGKYTSYLKDNAIKVPDGVEYVWFRTKVRKQTYSYEYSFDGVTFTEIPVQLD 493
Cdd:pfam17851  82 YYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPELD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 839533633  494 AAVLSDDYVLqsyGGFFTGAFVGLAAVDY-AGYGTQAEFYQFEYQ 537
Cdd:pfam17851 162 ASILSDEYAA---GGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
 6-307 0e+00

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


Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 515.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGIWAPALSWADGQF 85
Cdd:cd09000    1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTDVKVTEGAFKDMTNYLTTAKDIRGPWSDPIKLNGVGFDASLFHDDDGRKYIVQQTWDHREYHHPFDGITLTELDT 165
Cdd:cd09000   81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 166 KTLKLMPEtARTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEAdSFETEPGDVFLTNVDTPDSY 245
Cdd:cd09000  161 ETKKLVGE-RKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFG-PYEVDPDNPLLTSWDDPENP 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839533633 246 IQKQGHGALVSTPEGEWYYASLCARPWNrpgesiydPRGWSTLGRETAIQKVYWDDEGWPRI 307
Cdd:cd09000  239 LQKAGHGSLVETPDGEWYLAHLCGRPLP--------GRGRCPLGRETAIQKVEWTDDGWPRL 292
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
 6-300 1.33e-103

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: 313.14  E-value: 1.33e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGIWAPALSWADGQF 85
Cdd:cd08989    1 NPVLPGFHPDPSVVRVGDDYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQLDLTGGPDGGGIWAPDISYHDGKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTDVKVtEGAFKDMTNYLTTAKDIRGPWSDPIKLNGVGFDASLFHDDDGRKYIVqqtwdhreYHHPfdGITLTELDT 165
Cdd:cd08989   81 YIYYTVVLN-VGSWKGRRNYLVTSEDPEGPWSEPVWLDEGGIDPSLFVDDDGKHYML--------LNPG--GIRLAELNP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 166 KTLKLMpETARTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEAdSFETEPGDVFLTNVDtPDSY 245
Cdd:cd08989  150 DCTKQI-GEPKRIWEGTGGRAPEGPHLYKKDGYYYLLTAEGGTGYGHAITIARSKTIYG-PYEPCPYNPILRQQD-PQAP 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 839533633 246 IQKQGHGALVSTPEGEWYYASLCARPwnrpgesiyDPRGWSTLGRETAIQKVYWD 300
Cdd:cd08989  227 LQRCGHGKLVETPDGEWWMVYLCGRP---------LPGGYCPLGRETALAPVEWT 272
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
 6-305 7.88e-103

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: 311.36  E-value: 7.88e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGIWAPALSWADGQF 85
Cdd:cd18617    1 NPILPGFYPDPSICRVGDDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQLDLRGVPSSGGIFAPTIRYHDGRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTDVKVTEGAfkdmtNYLTTAKDIRGPWSDPIKLNGVGFDASLFHDDDGRKYIVQQTWDHREYHHPFdGITLTELDT 165
Cdd:cd18617   81 YIITTNVSTDGRG-----NFIVTADDPAGPWSDPVWLDGPGIDPSLFFDDDGKVYLTGTGPPPDPYEGHG-GIWQQEIDL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 166 KTLKLMPETARTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEADsFETEPGDVFLTNVDTPDSY 245
Cdd:cd18617  155 ETGKLLGEPKVLWNGGTGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGP-YEPCPNNPILTHRHLGSNP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 246 IQKQGHGALVSTPEGEWYYASLCARPwnrpgesiyDPRGWSTLGRETAIQKVYWDDEGWP 305
Cdd:cd18617  234 VQNTGHADLVEDPDGSWWAVFLGVRP---------YGGGFHNLGRETFLAPVEWEDGWPV 284
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
 4-305 1.91e-100

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: 305.01  E-value: 1.91e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633    4 IQNPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSggiWAPALSWADG 83
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   84 QFWLVYTDVKvtegafkdMTNYLTTAKDIRGPWSDPIKL--NGVGFDASLFHDDDGRKYIVQQTWDHReyhHPFDGITLT 161
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLksGGGGIDPSLFHDDDGKKYLVWGGWDPR---HGHGGIYLQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  162 ELDTKTLKLMPETARTIYRGTA---VALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLeADSFETEPGDVFLTN 238
Cdd:pfam04616 147 ELDNDGLKLVGPVTKLIYPGTRwvgGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSP-LGPYEWHPGNPILTS 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839533633  239 VDtPDSYIQKQGHGALVSTPEGEWYYASLCARPwnrpgesiydPRGWSTLGRETAIQKVYWDDEGWP 305
Cdd:pfam04616 226 RS-PENPIYGPGHASLVETPDGEWWIVYHAGRP----------GDGGYGLGRETRIQPVEWRADGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
4-416 1.47e-94

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 292.62  E-value: 1.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   4 IQNPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLdmkGNPSSGGIWAPALSWADG 83
Cdd:COG3507   22 YTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  84 QFWLVYTDVKVTEGAFKdmtNYLTTAKDIRGPWSDPIKL---NGVGFDASLFHDDDGRKYIVqqtwdhreYHHPFDGITL 160
Cdd:COG3507   99 KYYLYYTAVDGGKNRSG---IGVATADDPEGPWSDPGPLvcpGGNGIDPSVFVDDDGKAYLV--------YGSGGGGIYV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 161 TELDTKTLKLMPETaRTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGT-VFTHQEVVARSKTLEADsFETEPGDVFLTNV 239
Cdd:COG3507  168 AELDPDTGKLLGEP-KTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTcNSGYAVRVARSKSPTGP-YEDAPGNPILTQR 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 240 DtpDSYIQKQGHGALVSTPEGEWYYASLCARPWNrpgesiydprgwsTLGRETAIQKVYWDDEGWPRIEGGhGGKTFVEG 319
Cdd:COG3507  246 S--DGGIQGPGHGSLVETPDGEWYLVYHAYRPPG-------------GLGRETFLDPVTWNEDGWPVVGPG-TGEPPQPL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 320 PKdaiftesasdnSQQDDFTSPaLDPNWNTlrvpftakmgttgdGKLTLIGQgslanthdlsliarrwqafyFDAAVKVk 399
Cdd:COG3507  310 PA-----------PESDDFDGP-LGLQWSL--------------GYLRLTRQ--------------------FTATTKL- 342

                        410
                 ....*....|....*..
gi 839533633 400 fepfsyqqMAGLTNYYN 416
Cdd:COG3507  343 --------RAGLVLYGN 351
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
 6-306 8.10e-65

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: 213.26  E-value: 8.10e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVE---DTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMK---GNPSSGGIWAPALS 79
Cdd:cd18833    1 NPIIPGFHPDPSCIFVPewdGTFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSQLPELattGTGQQGGIWAPTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  80 WADGQFWLVYTDVKVTEGAFKDMTNYLTTAKDIRGP--WSDPIKLNGVGFDASLFHDDDGRKYiVQQTWdhreYHHPFDG 157
Cdd:cd18833   81 YHDGTFYVITTLVFPDKTDASRWDNLLFTTTDPYSDsaWSDPIRFDFPGYDPDLFWDDDGTAY-VQGAH----YWRVRPE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 158 ITLTELDTKTLKLMPEtaRTIYRGTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEADsFETEPGDVFLT 237
Cdd:cd18833  156 IQQQEIDLKTGESLSP--SPIWNGTGGSAPEGPHMYKKDGWYYLLIAEGGTGLGHSVTIARSRSIWGP-YESYPSNPVLT 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839533633 238 NVDTpDSYIQKQGHGALVSTPEGEWYYASLCARpwNRPGESIYdPrgwstLGRETAIQKVYWDDEGWPR 306
Cdd:cd18833  233 NANT-SEYFQTVGHADLFQDANGNWWGVALATR--SGPEYEIY-P-----MGRETVLYPVTWEEGEWPV 292
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
 336-537 3.44e-61

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


Pssm-ID: 436093  Cd Length: 203  Bit Score: 200.57  E-value: 3.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  336 DDFTSPALDPNWNTLRVPFTAKMG--TTGDGKLTLIGQGSLANTHDLSLIARRWQAFYFDAAVKVKFEPFSYQQMAGLTN 413
Cdd:pfam17851   2 DDFDSPKLGLQWQWLRNPRDESWYslTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  414 YYNDRHWSFVFLTWNEINGKVIEVGENNRGKYTSYLKDNAIKVPDGVEYVWFRTKVRKQTYSYEYSFDGVTFTEIPVQLD 493
Cdd:pfam17851  82 YYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPELD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 839533633  494 AAVLSDDYVLqsyGGFFTGAFVGLAAVDY-AGYGTQAEFYQFEYQ 537
Cdd:pfam17851 162 ASILSDEYAA---GGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
 5-305 5.58e-53

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: 181.17  E-value: 5.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   5 QNPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNL----LPSpLSTTTLLDMKGNPS--SGGIWAPAL 78
Cdd:cd09001    3 TNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIvgyvVDR-LDDGDAYYLEDGKNayGKGIWAPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  79 SWADGQFWLVYTDvkVTEGAfkdmtnYLTTAKDIRGPWSdPIKLNGVGF-DASLFHDDDGRKYIVqqtwdhreyhHPFDG 157
Cdd:cd09001   82 RYHNGKFYVYFCT--NTGGT------YVYTADDPAGPWS-RPALIGKGYhDPSLLFDDDGKAYLV----------YGNGE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 158 ITLTELdTKTLKLMPETARTIYRGTAVAL-VEGPHLYKLNGYYYLFAAQGGtVFTHQEVVARSKTLEADsFETepGDVFL 236
Cdd:cd09001  143 IRLTEL-SPDGTGVGGEGRVIIDGTEEGLgAEGSHLYKINGYYYIFNIEWG-GGGRTQVVLRSKSLYGP-YEG--RVVLD 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839533633 237 TNVDTPDSYIqkqGHGALVSTPEGEWYYASLCARPWnrpgesiydprgwstLGRETAIQKVYWDDeGWP 305
Cdd:cd09001  218 DGSGTGDNGP---HQGGLVDTPDGEWWFMLFQDRGA---------------VGRIPVLVPVTWKD-GWP 267
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
 5-307 4.76e-44

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: 157.39  E-value: 4.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   5 QNPILRGFNADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTlldmkgnpssGGIWAPALSWADGQ 84
Cdd:cd09002    2 LNPILAGDYPDPSILRDGDDYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAALTEYI----------GTVWAPDLIKHDGR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  85 FWLVYtdvkvtegAFKDMTNYLTTAKDIRGPWSDPIKLN-GVGFDASLFHDDDGRKYIVqqtwdhreyhhpFDGITLTEL 163
Cdd:cd09002   72 YYIYF--------PAKGGTNYVITADDIAGPWSEPIDLKvGSGIDPGHVVDEDGKRYLF------------LSGGRRVRL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 164 DTKTLKLMPETaRTIYRG---------TAVALvEGPHLYKLNGYYYLFAAQGGT---VFTHQEVVARSKTLEAdSFETEP 231
Cdd:cd09002  132 TDDGLSVAGPP-EKVYDGwrypdewdvECFCL-EGPKLFRRGGYYYLTTAQGGTagpPTSHMVVSARSKSPHG-PWENSP 208

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839533633 232 GDVFLTNVDTPDSYIQKqGHGALVSTPEGEWYyaslcarpwnrpgeSIYDPR--GWSTLGRETAIQKVYWDDEGWPRI 307
Cdd:cd09002  209 YNPLVRTQSREEKWWSK-GHGTLVEGPDGKWW--------------MVYHGYenGYRTLGRQTLLEPVEWTADGWFRI 271
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
 14-267 5.40e-38

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: 140.26  E-value: 5.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANSTFEW--FPGVRLHESKDLKNWNLLPSPLStttlLDMKGNPSSGGIWAPALSW-ADGQFWLVYT 90
Cdd:cd08978    1 ADPSILKDNGRYYIYATTDDTgtGTGIVVWKSKDLVNWKEEGTVLS----RGKSKSWGTGNLWAPEVYYfNSGKWYLYYS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  91 DVKVTEGAfkdmTNYLTTAKDIRGPWSDP-----IKLNGVGFDASLFHDDDGRKYIVQQTWDHreyhhpFDGITLTEL-- 163
Cdd:cd08978   77 AVPNGGGG----RIYVATSDSPEGPFTPIvsgklGDRGSGSIDPTVFVDDDGKLYLYYGDEDD------SGDIYVAELdp 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 164 DTKTLKLMPETARTIYRGTAVA--LVEGPHLYKLNGYYYLFAAQGGTVFTHQEVVARSKTLEAdsfETEPGDVFLTNVDT 241
Cdd:cd08978  147 DLLTIKGDVTLLIGEVVGSGFRgnYFEGPAVFKRNGYYYLIYSAGGTDGGYAIGYATSDSPLG---PWEKASHNPGLQTS 223

                        250       260
                 ....*....|....*....|....*.
gi 839533633 242 PDSYIQKQGHGALVSTPEGEWYYASL 267
Cdd:cd08978  224 GATGIYGPGHGSIFQDEGDRWYIVYH 249
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
 15-223 3.22e-24

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: 102.63  E-value: 3.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVED-TYYIANSTfewfPGVRLHESKDLKNWNLLPSPLSTTTL-LDMKGNPSSGGIWAPALSWADGQFWLVYtdv 92
Cdd:cd08998    3 DPSIIKDDGgTYYVFSTG----AGIQIRTSKDLVNWEFVGTVFPEGPAwAAAEVPGGAGGLWAPDVVYVNGRYYLYY--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  93 kvteGAFKDMTN----YLTTAKDI-RGPWSDpiklNGVGF-----------DASLFHDDDGRKYIVQQTWdhreyhhpFD 156
Cdd:cd08998   76 ----SASTFGSNrsaiGLATSTTLdDGPWTD----QGLVVssspgddynaiDPNVFVDADGRLWLAYGSF--------WG 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839533633 157 GITLTELDTKTLKLMPETARTI--YRGTAVALVEGPHLYKLNGYYYLFAAQG----GTVFTHQEVVARSKTLE 223
Cdd:cd08998  140 GIKLVELDPATGKLRPGSTGTSiaSRPGGPGAIEAPYIIYRGGYYYLFVSYGsccrGANSTYNIRVGRSTSIT 212
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
 14-222 6.00e-20

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


Pssm-ID: 350102 [Multi-domain]  Cd Length: 277  Bit Score: 89.88  E-value: 6.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANSTFEWFpGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGG-IWAPALSWADGQFWLVYTdv 92
Cdd:cd08988    1 HDPSIIKEGGTYYAFGTGTDGF-GIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGnLWAPDISQHKGKYYLYYS-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  93 kVTEGAFKDMTNYLTTAKDIRGPWSD--------PIKLNGVGFDASLFHDDDGRKYIVQQTWdhreyhhpFDGITLTELD 164
Cdd:cd08988   78 -VSDNGSNTSAIGLATANNPQGPFKDegpakpvvTSDNAGNAIDPDLFQDEDGQNWLLYGSF--------WGGIWLQKLD 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839533633 165 TKTLKLMPETARTIYRGTAVALVEGPHLYKLNGYYYLFAAQG----GTVFTHQEVVARSKTL 222
Cdd:cd08988  149 KNGLVVNPPGNGKSIAVLYYVSIEAPYITYAGGYYYLFVSAGsccdGGNSTYHTRVGRSKKV 210
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
 6-306 6.46e-19

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


Pssm-ID: 350113 [Multi-domain]  Cd Length: 284  Bit Score: 87.20  E-value: 6.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYiANSTFEWFPGVRLHESKDLKNWNL-----LPSPLSTTTlldmkgnpSSGGIWAPALSW 80
Cdd:cd08999    1 NPVIDGDFPDPSVIRVGGTYY-AFATNSGGKNVQVATSTDLVTWTLlggdaLPDLPAWAA--------AGGNTWAPDVVR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  81 -ADGQFWLVYTDVKVTEG------AfkdmtnyltTAKDIRGPWSD-------PIKLNGVgFDASLFHDDDGRKYIV---- 142
Cdd:cd08999   72 rPDGKYVMYYSARLKSSGkhcigvA---------TSDSPLGPFTPvgepplcPLDQGGA-IDPSGFVDPDGKRYLVykvd 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 143 -----QQTWdhreyhhpfdgITLTELDTKTLKLMPETARTIYRGTAV--ALVEGPHLYKLNGYYYLFAAQGGTVFTHQEV 215
Cdd:cd08999  142 gnsigVPTP-----------IMLQELSADGLTLVGEPVELLLNDGPWdgPLVEAPSLVKRDGTYYLFYSSNCYCSPSYAV 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 216 -VARSKTLEAdSFETEPGDVFLTNVDT---PdsyiqkqGHGALVSTPEGEW--YYAslcarpwnrpgesiYDPRGWSTLG 289
Cdd:cd08999  211 gYATSKSITG-PYTKAGEPLLLTGDGGltgP-------GGADVVEDDGGDWmvFHA--------------WDGGDDVGGG 268

                        330
                 ....*....|....*..
gi 839533633 290 RETAIQKVYWDDeGWPR 306
Cdd:cd08999  269 RAMYTAELTWEG-GWPV 284
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
 6-222 2.84e-17

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: 82.24  E-value: 2.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGFNADPSIIRVEDTYYIANSTFE-WFPGVRLH-----ESKDLKNWNLLPSPLSTTTlldMKGNPSSGGIWAPALS 79
Cdd:cd18616    1 NPVFEPTFADPTVIRGDDGYFYAYATEDpWGDGGGFRlvpilRSKDLVNWEYVGDAFTSKP---RWKWDPGGGLWAPDIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  80 WADGQFWLVYTdvKVTEGAFKDMTNYLTTAKDIRGPWSDPIKL-----NGVG--FDASLFhDDDGRKYIvqqtwdhreYH 152
Cdd:cd18616   78 YIDGKYVLYYS--LSDWGADPNPGIGVATADSPAGPFTDQGKLfdsneIGVRnsIDPFVF-EDDGKKYL---------FW 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839533633 153 HPFDGITLTELDTKTLKLMPETARTIyrgtAVALVEGPHLYKLNGYYYLFAAQG----GTVFTHQEVVARSKTL 222
Cdd:cd18616  146 GSFYGIYAVELTADGLALKPGEKVQI----AGDRYEGPYIVKRDGYYYLFGSAGscceGPNSTYRVVVGRSESL 215
GH43_F5-8_typeC-like cd18608
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ...
 14-303 5.21e-16

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: 78.48  E-value: 5.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANSTFEWF------PGVrlHESKDLKNWNLLPSPLSTttllDMKGNPSSggIWAPALSWA-DGQFW 86
Cdd:cd18608    2 ADPSIVKFGGTYYLYATTDGWGgfnsgePVV--WKSKDFVNWKFEGLNWPT----KAASGDSK--VWAPSVVKGkDGKYY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  87 LVYTdvkvtegafKDMTNYLTTAKDIRGPWSDP-------IKLNGV----GFDASLFHDDDGRKYIVQQTWDHREYHhpf 155
Cdd:cd18608   74 MYVS---------VGSEIYVGVADSPLGPWKNAngdgppiIPGDGKpnyhMIDAEPFIDDDGKAYLYWGSGLHVNGH--- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 156 dgITLTELDTKTLKLMpETARTIyrGTAVALVEGPHLYKLNGYYYLFAAQGGTVF-THQEVVARSKTLEAdSFETEPGDV 234
Cdd:cd18608  142 --CFAAKLNPDMVTFD-GSEPTI--VTPRDYFEAPFMFKRNGIYYLMYSGGGCWDeTYNVRYAVSDNPLG-PFEEGENSP 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839533633 235 FLTNvdTPDSYIQKQGHGAlVSTPEGEWYYASLcarpwnrpgeSIYDPRGWSTLGRETAIQKVYWDDEG 303
Cdd:cd18608  216 ILQT--DEAKGIFGPGHHS-VFEEGGQYYILYH----------RQGYPFSPGGTLRQVCVDELNFNADG 271
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
 15-204 5.50e-15

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: 74.96  E-value: 5.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVEDTYYIANST----FEWFP--GVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSG--------GIWAPALSW 80
Cdd:cd08986    4 DPYITLGPDGYYYLTGTtggpDWWGVndGIRLWRSKDLKDWEYLGLVWDLEKDGWWQWEPQWWtpdsknkrALWAPEIHY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  81 ADGQFWLVYTDVKVTEGAFKdmtnylTTAKDIRGPWSDPIKLN-GVGFDASLFHDDDGRKYIVqqtWDHREYHHPFDGIT 159
Cdd:cd08986   84 INGTWYITHSMNGGGTGLLK------STTGKPEGPYVDPMGGPlGKGIDPSLFEDDDGTVYLV---WGNGQIARLKKDMS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 839533633 160 LTELDTKTLKlmPETARTIYRgtavalvEGPHLYKLNGYYYLFAA 204
Cdd:cd08986  155 GFAEEPRKID--PSGNREIGH-------EGAFIFKIGGKYVLFGA 190
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
 15-220 1.11e-14

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: 74.32  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVEDTYYiansTFEWFPGVRLHESKDLKNWNLLP----SPLS--TTTLLDMKGNpssgGIWAPALSWADGQFWLV 88
Cdd:cd18829    3 DPSIIKEGSTWW----TFSTGDGIPVKYSSDGLNWTQGPpifgSPLSwwKTYVPANTTN----DVWAPDVHYYNGKYWLY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  89 YTdvkVTE-GAFKDMTNYLTTAKDIRGPWSDP----IKLNGVGF---DASLFHDDDGRKYIVQQTWdhreyhhpFDGITL 160
Cdd:cd18829   75 YA---ISTfGSNTSAIGLASASSIAAGNWTDEglvlRSTSADNYnaiDPNLVIDASGNPWLVFGSF--------WSGIKI 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839533633 161 TELDTKTLKLMPETARTIYRgtAVALVEGPHLYKLNGYYYLFAAQG----GTVFTHQEVVARSK 220
Cdd:cd18829  144 TRLDKATMKPTGSIYSIASR--PSGGIEGPFIVYRDGYYYLFVSIDkccrGVNSTYKIAYGRST 205
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
 14-202 2.78e-13

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: 70.28  E-value: 2.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANSTFEWFPGVRLHESKDLKNWNLLPsplsttTLLDMKGNPSSGGIWAPALSWADGQFWLVYTdvk 93
Cdd:cd08991    1 ADPFVLKHNGTYYLYGTGGDDGRGFKVYVSDDLVNWEYPG------GALEEPGLWGTKGFWAPEVFYYNGKFYMYYS--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  94 vTEGAFKDMTNYLTTAKDIRGPWSD----PIKLNGVGFDASLFHDDDGRKYI--VQQTWDHREYHH----PFDGITLTEL 163
Cdd:cd08991   72 -ANGGDHGEHIAVAVSDSPLGPFRDkgklLIPAGGFSIDAHVFIDDDGKWYLyyVRDDLGGEPGNRiyvaELEDDLSLIG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 839533633 164 DTKTLKLMPETARTIYRGTAVA-LVEGPHLYKLNGYYYLF 202
Cdd:cd08991  151 EPTLVLCPTADERWEYGEGRDWhTTEGPTVLKHNGTYYLT 190
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 14-306 3.88e-13

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: 69.56  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANST--FEWFPGVRLH--ESKDLKNWNllpsplSTTTLLDMkGNPSS---GGIWAPALSWADGQFW 86
Cdd:cd09004    1 ADPDIVVFGGRYYIYPTTdgPPGWSSTSFHvfSSTDLVNWT------DHGIILDL-ANDVWwanKGAWAPAVAERNGKYY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  87 LVYT-----DVKVT---EGAFKDMTNYLTTAKDIRGpwsDPIklngvgfDASLFHDDDGRKYIVQQTWDHREYHHPFDGI 158
Cdd:cd09004   74 FYFSagsqiGVAVSdspTGPFTDLGRPLVTGGDYGG---QAI-------DPMVFVDDDGQAYLYWGNGTAYVARLNDDMV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 159 TLTEldtktlklmpETARTIyrgTAVALVEGPHLYKLNGYYYLFAAQGGTVFTHQEVV-ARSKTLeaDSFETEPGDVFLT 237
Cdd:cd09004  144 SFDG----------EVVVSI---TPPNFREGPFVHKRNGIYYLSWSENDTRDPDYRVRyATSDSP--LGPWTYRGVGLLL 208

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 238 NvdtPDSYIQKQGHGALVSTP-EGEWYYASlcaRPWNRPGesiydPRGWStlgRETAIQKVYWDDEGWPR 306
Cdd:cd09004  209 D---SAGGIKGTGHHSIVQVPgTDEWYIAY---HRFAVPG-----GDGYH---REVAIDRLEFDADGTIR 264
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
 14-303 1.38e-12

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


Pssm-ID: 350104 [Multi-domain]  Cd Length: 269  Bit Score: 68.01  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYI------ANSTFEWF-PGVRLHESKDLKNWNLLPSPLSTTTLldmkGNPSSGGIWAPALSWADGQFW 86
Cdd:cd08990    1 ADPAAHVFNGKVYVyashdeAPANGYFImDDWHVFSSTDLVNWTDHGEILPPDDV----FWWASGNAWAPDAVYKNGKYY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  87 LVYTdVKVTEGAFKdmtnylT---TAKDIRGPWSDPI-------KLNGV-GFDASLFHDDDGRKYIvqqtwdhreYHHPF 155
Cdd:cd08990   77 FYFP-VGQASDGFG------IgvaVSDSPAGPFKDALgkplipeGLNGIeGIDPAVFVDDDGRAYL---------YFGGG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 156 DGITLTEL--DTKTLKlmpETARTIYRGTAVALVEGPHLYKLNGYYYLFAAqggTVFTHQEVVARSKtleADSFET--EP 231
Cdd:cd08990  141 GGYYVAKLkdDMISLA---GEPQKIKNGGLKGFFEAPWVFKRNGTYYLSYA---GGWAYPAEIAYST---ADSPLGpyTY 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839533633 232 GDVFLTNVDTPdsyiqkQGHGALVSTpEGEWYYAslCARPWNRPGESIYdprgwstlgRETAIQKVYWDDEG 303
Cdd:cd08990  212 RGVILDPVGSG------TNHGSIVEF-KGQWYLF--YHTADLSGGGDFR---------RSVCIDYLHYNADG 265
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
 15-223 2.13e-12

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: 67.69  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVEDTYYIanstFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPS-SGGIWAPALSWADGQFWLVY---T 90
Cdd:cd18830    3 DPVMAREGGTYYL----FSTGPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGfNGHIWAPDISFHNGRYYLYYscsA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  91 DVKVTEgAFKDMTNYLTTAKDIRGPWSD--------PIKLNGVGFDASLFHDDDGRKYIVQQT-WdhreyhhpfDGITLT 161
Cdd:cd18830   79 FGKNTS-AIGVATNKTLDPDSPDYKWEDhgmvvqsvPGRDLWNAIDPNVIVDEKGTPWLSFGSfW---------GGIKLV 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839533633 162 ELDTKTLKLM-PETARTI---YRGTAV-------ALVEGPHLYKLNGYYYLFAAQG----GTVFTHQEVVARSKTLE 223
Cdd:cd18830  149 KLDPDLKSLAePQEWHTIarrERTFKLtdseagpGAIEAPFIFKKGGYYYLFVSWDyccrGVNSTYKVVVGRSKNVT 225
GH43_GsAbnA-like cd18832
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ...
 15-223 2.13e-12

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: 68.43  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVEDTYYIANSTFEWfpgvrlHESKDLKNW-----------NLLPSPLSTTTLLDMKGNPS--SGGIWAPALSW- 80
Cdd:cd18832    3 DPSIVKDDGTYYVFGSHLAA------AKSTDLMNWtqftngvttdnPLLFNLFDSTAWELAEDFNWagGGNLWAPDVIYn 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  81 -ADGQFWLVYTdvkVTEGAFKDMTNYLtTAKDIRGPWSD-----------------PIKLNGVGF---------DASLFH 133
Cdd:cd18832   77 kAMGKYCMYYS---VSGDDSPSAIGLA-TADNIEGPYTYkgtvlksgftgstsadaDVYLTGGKYnnnyhpnaiDPCVFY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 134 DDDGRKYIVQQTWdhreyhhpFDGITLTELDTKTLK---LMPETARTIYRGTAVALV-------EGPH-LY-KLNGYYYL 201
Cdd:cd18832  153 DKDGKLWMVYGSW--------SGGIFLLELDPKTGLrdySVETDGNLPDQYYGKKIAggyhasgEGPYiLYdKDTGYYYL 224

                        250       260
                 ....*....|....*....|....*...
gi 839533633 202 F------AAQGGtvftHQEVVARSKTLE 223
Cdd:cd18832  225 FvsygglDANGG----YNIRVFRSKNPD 248
GH43_AnAbnA-like cd18831
Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); ...
 15-208 1.00e-09

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


Pssm-ID: 350152 [Multi-domain]  Cd Length: 286  Bit Score: 59.92  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVEDTYYIANSTfewFPGVRLHESKDLKN-WNLLPSPLSTTTLLDMKGNpssGGIWAPALSWADGQFWLVYTdvk 93
Cdd:cd18831    3 DPSIIRREDGTYFRFST---GGGIRIATAPSLTGpWTYVGSVLPGGSSIDLAGN---DDLWAPDVHYVNGTYYCYYS--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  94 VTEGAFKDMTNYLTTAKDI-RGPWSDpiklNGVGF-----------DASLFHDDDGRKYIVqqtwdhreYHHPFDGITLT 161
Cdd:cd18831   74 VSTFGSQDSAIGVATSPTMePGSWTD----HGAVIrsssgdpynaiDPNLIVDDDGTPYLT--------FGSYWQGIFQV 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 839533633 162 ELDTKTLKLMPETARTIYRGTAVA--LVEGPHLYKLNGYYYLFAAQGGT 208
Cdd:cd18831  142 PLTDPLLSPAAGPPPTHLAYNPSGnhPEEGSFMYKHGGYYYLFFSSGIC 190
GH43-like cd08982
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
 14-266 5.60e-08

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: 54.49  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYI--ANSTFEWFpgvrlheSKDLKNWNLLPsplsTTTLLDMKgnpssggiWAPALSWADGQFWLVytd 91
Cdd:cd08982    6 ADPTVVLFKGKYYLfaSKSGGYWH-------SDDLVNWKFIP----TNGLPIED--------YAPTVVEINGTLYFT--- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  92 vkvtegAFKDMTNYLTTAKDIRGPWS--DPIKLNGVgFDASLFHDDDGRKYIvqqtwdhreYH--HPFDGITLTELDTKT 167
Cdd:cd08982   64 ------ASGGPGPIYRTDDPLGGKWElvAESGPFGF-WDPALFVDDDGRLYL---------YWgcSNKDPIYGVELDPNT 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 168 -LKLMPETARTIY----------------RGTAVALVEGPHLYKLNGYYYLFAAQGGTVF-THQEVVarsktLEADS--- 226
Cdd:cd08982  128 gFRPIGEPVPLISfdpdkhgwerfgedneDPGLAPWIEGAWMTKHNGKYYLQYAAPGTEFkTYADGV-----YVSDSplg 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 839533633 227 -FETEPGDVFLTNvdtPDSYIQKQGHGALVSTPEGEWYYAS 266
Cdd:cd08982  203 pFTYAPNNPFSYK---PGGFITGAGHGSTFQDKYGNYWHFG 240
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 15-203 2.06e-07

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: 52.62  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  15 DPSIIRVE--DTYYI------ANSTFEWFPGVRLH--ESKDLKNWnllpsplSTTTLLDMKGNPSSGGIWAPALSW--AD 82
Cdd:cd08983   20 DPFIIRGPedGKFYLvatdlwIAGGAQWNGSRGIGvwESTDLVNW-------SEQRLVKMVSPPNAGNAWAPEAIYdpET 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  83 GQFwLVY--TDVKVTEGAFKDMTnYLTTAKDIRGpWSDPIKLNGVGFDA---------SLFH----DDDGRKYIVQQTWD 147
Cdd:cd08983   93 GQY-VVYwsSSLYGDGGGGNHRI-YYATTKDFKT-FSEPKVLFDPGFNVidttivkdgGTYYrfykDETTGKGIRLATSD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 839533633 148 HreyhhpfdgitLTELDTktlklmpETARTIYRGTAVAlVEGPHLYKLN--GYYYLFA 203
Cdd:cd08983  170 S-----------LTGPWT-------TVTTGGGAGTGGG-VEGPTVFKLNdgGKWYLYY 208
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 14-304 5.00e-07

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: 51.51  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANST--FEWFPGVRLH--ESKDLKNWNllpsplSTTTLLDMKGNP----SSGGIWAPALSWADGQF 85
Cdd:cd18828    1 ADPDIAYFDGKYYIYPTTdgFPGWSGTQFHvfSSDDLVTWK------DEGVILDLKNDQvvpwATGNAWAPTIEERDGKY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTdvkvteGAFKDMTNYL--TTAKDIRGPWSD---PIKLN-------GVGFDASLFHDD-DGRKYIvqqTWDHreyh 152
Cdd:cd18828   75 YFYFC------GKNPDGRSQIgvAVADSPTGPFTAqgsPLITHemarvtmGQAIDPSVFTDPvDGKYYL---YWGN---- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 153 hpfDGITLTELDTKTLKLMPETARTIyrGTAVALVEGPHLYKLNGYYYLFAAQG-----------GTVFT-HQEVVARSK 220
Cdd:cd18828  142 ---GYAAIAELNDDMISIKPGTLVNL--DGLTDFREAVTVLYRDGLYHFTWSCDdtgsenyhvnyGTSDSpYGPITYRGV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 221 TLEADsfetepgdvfltnvdtPDSYIQKQGHGALVSTP-EGEWYYASLC-ARPWNRPGESiydpRGWStlgRETAIQKVY 298
Cdd:cd18828  217 ILQKD----------------PSKGILGTGHHSILQVPgTDEWYIAYHRfATPLGIYGSG----LGYH---RETCIDRLT 273


                 ....*.
gi 839533633 299 WDDEGW 304
Cdd:cd18828  274 FDADGL 279
GH43_Xsa43E-like cd18618
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ...
 12-207 2.75e-06

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: 49.14  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  12 FNADPSIIRVEDTYYI------ANSTFEWF--PGVRLHESKDLKNWNLLPSPLSTTTLldmkgNPSSGGIWAPALSWADG 83
Cdd:cd18618    1 YTADPAALVHGDTVYLytghdeAPPGGTFFvmNDWRVFSTTDMVNWTDHGAVLSLKDF-----SWAKGDAWAGQVIERNG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  84 QFWLVYT-----------DVKVT---EGAFKD------MTNYLTTAKDIrgPWSDpiklngvgFDASLFHDDDGRKYIVQ 143
Cdd:cd18618   76 KFYWYVPvhhktnggfaiGVAVSdspTGPFKDalgkplITNDMTGTTNH--SWDD--------IDPTVFIDDDGQAYLYW 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839533633 144 QTWDHREYHHPFDGITLTElDTKTLKLMPETARTiyrgtavalvEGPHLYKLNGYYYLFAAQGG 207
Cdd:cd18618  146 GNPELYYVKLKEDMISLDG-EIGTIDISGLPDFT----------EAPWVHKRNGLYYLSYAAGF 198
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
 14-207 2.83e-06

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: 49.20  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYIANST---------FEWFpgvrlhESKDLKNWNLLPSPLstttllDMKGNPSSG-GIWAPALSWADG 83
Cdd:cd18827    1 ADPEIRIFDGQYWIYPTYsapyeeqtfFDAF------SSPDLVHWTKHERIL------DMADVPWANrAVWAPSVIEKNG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  84 QFWLVYT-------------DVKVT---EGAFKDMTNYLTTAKDIRGpwSDPIklngvgfDASLFHDDDGRKYIVQQTWD 147
Cdd:cd18827   69 KYYLYFAandiqsddegggiGVAVAdrpEGPFKDALGKPLIGEFHNG--AQPI-------DQHVFKDDDGQAYLYYGGWG 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839533633 148 HreyhhpfdgITLTELDTKTLKLMPETARTIYRGTAVA-LVEGPHLYKLNGYYYLFAAQGG 207
Cdd:cd18827  140 H---------CNVAKLNDDMTSLVPFDDGETFKEITPEgYVEGPFMFKRNGKYYFMWSEGG 191
GH43_LbAraf43-like cd18820
Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis ...
 14-147 1.19e-05

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


Pssm-ID: 350141 [Multi-domain]  Cd Length: 258  Bit Score: 47.13  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  14 ADPSIIRVEDTYYianSTFEWFPGVRLHESKDLKNWNLLPSplstTTLLDMKGNPSSGGIWAPALSWADGQFWLVYTdvk 93
Cdd:cd18820    1 ADPWVVYHDGYYY---LTFTTGDRITIWKSKTLTGLGTAEP----KVVWTPPDPSRSCNIWAPELHFIDGRWYIYYA--- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839533633  94 VTEGAFKDMTNYL---TTAKDIRGPWSDPIKL----NGVGFDASLFhDDDGRKYIVQQTWD 147
Cdd:cd18820   71 ADDGDNANHRMYVlesASDDPPLGPYTFKGRLadptDKWAIDGTVL-EHNGKLYFVWSGWE 130
GH43_CtGH43-like cd08985
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
 18-235 4.93e-05

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: 45.40  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  18 IIRVEDTYYIANSTFE------WFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGIWAPALSW--ADGQFWLVY 89
Cdd:cd08985    8 ILQEGDTYYWYGESRKgldndnLSHGINCYSSTDLYNWRFEGLVLPASGVEVVRDISPGYVIERPKVLYnaRTRKYVMWF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  90 tdvkVTEGAFKDMTNYLT-TAKDIRGPWS---DPIKLNGVGFDASLFHDDDGRKYIVQQTWdhreyhhpfdgitlTELDT 165
Cdd:cd08985   88 ----HLDNPNYGFAAVGVaTSDTPTGPFTfvrSFRPDGYPSRDMTLFQDPDGTAYLVRSTD--------------HNTDI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 166 KTLKLMPE-TARTIYRGTAVALV-EGPHLYKLNGYYYLFA---------------AQGGTV-FTHQEVVARSKTLEADSF 227
Cdd:cd08985  150 GISRLSDDyLDTTGASSTFKGPKrEAPALFKRGGTYYLITsgltgwnpnpsrlarADSPLGpWSTWGNLPVGGPGADTTY 229


                 ....*...
gi 839533633 228 ETEPGDVF 235
Cdd:cd08985  230 DSQPAFVF 237
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
 17-202 2.58e-04

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: 42.99  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  17 SIIRVEDTYYIA---NSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSsgGIWAPALSW--ADGQFWLV--- 88
Cdd:cd18822    7 GILKVGGTYYWYgenRDNNNGFNGVSLYSSTDLVNWEFRNTVLTRDTCSASELASC--KIERPKVIYnpKTGKFVMWahw 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  89 -----YTDVKVtegafkdmtnYLTTAKDIRGPWS-----DPiklNGVG-FDASLFHDDDGRKYIVQQTWDHREyhhpfdg 157
Cdd:cd18822   85 engkdYGLARA----------AVATSDTPDGDYTfhgsfRP---LGYDsRDMTLFVDDDGTAYLISAANDNAD------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 839533633 158 ITLTELDTKTLKLMPETArTIYRGTAvalVEGPHLYKLNGYYYLF 202
Cdd:cd18822  145 LNIYRLTPDYLSVDSLVA-TLFKGQH---REAPALVKRNGYYYLF 185
GH43_RcAra43A-like cd18823
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ...
 18-203 1.22e-03

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


Pssm-ID: 350144 [Multi-domain]  Cd Length: 289  Bit Score: 41.18  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  18 IIRVEDTYY---------------IANSTFEWFPGVRLHESKDLKNWNLLPSPLSTTTLLDMKGNPSSGGiwapalsWAd 82
Cdd:cd18823    8 VFKVGDTYYwygvkysgavtyaanTKKNSDTSFKSVTLYSSTDLVNWTFEGNVLTASGAVDTAGDFAGAG-------WV- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  83 GQFWLVY-----TDVKVTEGAFKDMTN---YLTTAKDIRGPWS----DPIKLNGVGF---DASLFHDDDGRKYIVQqTWD 147
Cdd:cd18823   80 GRPGVAYnsatgKYVLLIQWGSTGNGRngvLFATSDSPTGPFTyqrvQPMIDNVGTNntgDQTSFFDDDGKAYLVY-SND 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 839533633 148 HREYHhpfdgITLTELDTKTLKLMPETARTIYRGTAValvEGPHLYKLNGYYYLFA 203
Cdd:cd18823  159 RGRGS-----LYIAKLRSDYLGIEPAVRIDNYVGPGR---EGNALFKYGGTYYLCA 206
GH43_XynD-like cd09003
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ...
 6-201 1.36e-03

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: 41.09  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPIL-RGFNADPSIIRVEDTYYI--ANSTFEWFPGVRLHE-------------SKDLKNWnllpsplstT---TLLDMKG 66
Cdd:cd09003    1 NPIIsHRFGADPTALVYNGRVYVygTNDDQQYNANGKKKDnsyyninsltvisSDDMVNW---------TdhgEIPVAGP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  67 N---PSSGGIWAPALSW----ADGQFWLVYTDVKVTEGafkdmtnyLTTAKDIRGPWSDPIK----------LNGVG--F 127
Cdd:cd09003   72 NgiaKWAGNSWAPSVAYkninGKDKFYLYFANGGGGIG--------VLTADSPTGPWTDPLGkplitrstpgCAGVVwlF 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 128 DASLFHDDDGRKYIvqqtwdhreYhhpFDGItltelDTKTLKLMPETARtIYR---------GTAV-----ALVEGPHLY 193
Cdd:cd09003  144 DPAVFIDDDGQGYL---------Y---FGGG-----VPGGSEANPKTAR-VIKlgddmisvdGSAVtidapYFFEASGIN 205


                 ....*...
gi 839533633 194 KLNGYYYL 201
Cdd:cd09003  206 KINGKYYY 213
COG3940 COG3940
Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism];
6-305 1.87e-03

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


Pssm-ID: 443140 [Multi-domain]  Cd Length: 309  Bit Score: 40.57  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633   6 NPILRGfNADPSIIRVEDTYYIANSTfeWFPGVRLHESKDLKNwnlLPSPLSTTTLLDMKGNPSSGGIWAPALSWADGQF 85
Cdd:COG3940    1 NPLIEQ-GADPWVYKHDGYYYFTATV--EYDRIVLRRSKTLAG---LATAEPVVVWTPPASGPMSKNIWAPELHFIDGKW 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  86 WLVYTDVKVTEGAFKDMTNYLTTAKD--IRGPWSDPIKL----NGVGFDASLFhDDDGRKYIVQQTWDHREYHHPFDGI- 158
Cdd:COG3940   75 YIYFAAGDGEDNNFNHRMYVLENASAdpLTGPWTEKGQIktpwDSWAIDATVF-EHNGKLYLVWSGWEGDINGNQNLYIa 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 159 ---TLTELDTKTLKLmpetARTIY----RGTAVAlvEGPHLYKLNGYYYLFAAQGGTvFTHQ------EVVARSKTLEAD 225
Cdd:COG3940  154 emsNPWTLSGPRVLL----SKPEYdwekIGFKVN--EGPAVLKHNGKVFITYSASAT-WDPNyclgllTADAGADLLDPA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 226 SFETEPGDVFLTNVDT----PdsyiqkqGHGALVSTPEGE--W--YYAslcarpwnRPGESI-YDPrgwstlGRETAIQK 296
Cdd:COG3940  227 SWTKSPEPVFQTSPENgvygP-------GHNSFTKSPDGKedWivYHA--------RSYPEIgCDP------NRHTRAQK 285


                 ....*....
gi 839533633 297 VYWDDEGWP 305
Cdd:COG3940  286 FTWNADGTP 294
GH43_XylA-like cd18620
Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium ...
 45-201 1.93e-03

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: 40.27  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633  45 DLKNWNLLPSPLSTTTllDMKGNPSSGGI-WAPALSWADGQFWLVYTDVKVT----------EGAFKDmtnylttAKDIR 113
Cdd:cd18620   40 DLSNWRYHGVIFRSDQ--DPDEVPPGKGLlYAPDVVKGPGRYYLYYCLSKGSvegvavsdspAGPFEY-------LGPVK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839533633 114 gpwsDPIKLNGVGFDASLFHDDDGRKYIVqqtWdhreyhhPFDGITLTELDTKTLKLMPETARTIYRGTAV---ALVEGP 190
Cdd:cd18620  111 ----YPRKGDIFQIDPAVLVDDDGRVYLY---W-------GQGGSKGAELDPDMLTIKPETIVDVPAGITFeghGFFEGS 176

                        170
                 ....*....|.
gi 839533633 191 HLYKLNGYYYL 201
Cdd:cd18620  177 SIRKINGIYYL 187
 
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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