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Conserved domains on  [gi|1802158205|gb|QHQ53920|]
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family 43 glycosylhydrolase [Bifidobacterium longum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 491-813 8.30e-90

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: 289.13  E-value: 8.30e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  491 TLNNGTPLFTSEFGEKGLRDPFIMKSKDGDKFYMLATDLKIDGraplnglngfaGAQANGSKYIEIWKSDDLVNWSKQSH 570
Cdd:cd08983      1 ALNGGNPVLTSTVGTKGVRDPFIIRGPEDGKFYLVATDLWIAG-----------GAQWNGSRGIGVWESTDLVNWSEQRL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  571 VK-VSSDYAGNTWAPEAYYDEEIGKYVVYWASNLYDNTDENsrkqltYNRMVYVTTDDFVNFSDPTVWIDvdrrggAGSG 649
Cdd:cd08983     70 VKmVSPPNAGNAWAPEAIYDPETGQYVVYWSSSLYGDGGGG------NHRIYYATTKDFKTFSEPKVLFD------PGFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  650 SIDVTVQKVGDTYYRIYKDE-NTMSLRQEKSTDLTAaiggagvknyadalkgsAWSEVATNIGKGQANGYgktftsgEGP 728
Cdd:cd08983    138 VIDTTIVKDGGTYYRFYKDEtTGKGIRLATSDSLTG-----------------PWTTVTTGGGAGTGGGV-------EGP 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  729 SLFKANDGDangyQYYLFADQPSYHqgpnHYVPMATEDIASGQWTVIGNKmpeanfptNSDGGKPRHGTVLPVTRAQYQK 808
Cdd:cd08983    194 TVFKLNDGG----KWYLYYDQYGGG----GYGPFETTDLASGTWTPASED--------YSLPGGPRHGTVLPITAAEYDA 257


                   ....*
gi 1802158205  809 VLEAY 813
Cdd:cd08983    258 LLAAW 262
aBig_2 pfam20578
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
 355-448 4.17e-13

Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.


:

Pssm-ID: 466727 [Multi-domain]  Cd Length: 89  Bit Score: 65.98  E-value: 4.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  355 AEQAKADLDVV--TIEDSDDIRSNFSVPTKGNNGSTISWEVTGGKDIATLGegvndksrtvTVKRPAAGSDAVTVTLKAI 432
Cdd:pfam20578    1 VAADKAALAIGyaGGDSASSVTQNLTLPTTGANGTTITWSSSNPAVISADG----------TVTRPAYGSGDATVTLTAT 70

                           90
                   ....*....|....*.
gi 1802158205  433 AKYGTATETKTFTVTI 448
Cdd:pfam20578   71 ITKGGATDTKTFTLTV 86
aBig_2 pfam20578
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
 283-351 4.76e-10

Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.


:

Pssm-ID: 466727 [Multi-domain]  Cd Length: 89  Bit Score: 57.12  E-value: 4.76e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802158205  283 TEDFALPTSAA-GVSIAWKSDNAAiaVDNATGkaTVTRPAATAADAEVILTATFGNNAKTA--DYTVLVPKQ 351
Cdd:pfam20578   22 TQNLTLPTTGAnGTTITWSSSNPA--VISADG--TVTRPAYGSGDATVTLTATITKGGATDtkTFTLTVLAL 89
Big_4 pfam07532
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ...
 822-876 2.16e-09

Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.


:

Pssm-ID: 400079 [Multi-domain]  Cd Length: 59  Bit Score: 54.25  E-value: 2.16e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802158205  822 VDALSAETTVGVAPTLPETAHLTHADGSVSDVAVEWDAIDASFYAKTGTFTVKGI 876
Cdd:pfam07532    1 IENIEVTVAQGESYTLPTTVTATYSDGSVKEVPVTWDLTPNVDTSKPGTYTVEGT 55
Laminin_G_3 super family cl48183
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 81-258 4.87e-08

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


The actual alignment was detected with superfamily member pfam13385:

Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 53.16  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205   81 LTGSQTISVPTTAIAGKkDVTVSIWLKNNyGNGNTAAAYIGAAKtgnypANGYWLLNPANPSGYaksVMTNAtaadpnns 160
Cdd:pfam13385    1 DGGSDYVTLPDALLPTS-DFTVSAWVKPD-SLPGWARAIISSSG-----GGGYSLGLDGDGRLR---FAVNG-------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  161 pwgtevGPGSTNAATTGTKATSDlALYTTVISGTNSTMSFYLNGKQVGDATYTipaGGLTNYGGLVAYIGKSSYADPNSK 240
Cdd:pfam13385   63 ------GNGGWDTVTSGASVPLG-QWTHVAVTYDGGTLRLYVNGVLVGSSTLT---GGPPPGTGGPLYIGRSPGGDDYFN 132

                          170
                   ....*....|....*...
gi 1802158205  241 LDVDDYAVYDTAISAADV 258
Cdd:pfam13385  133 GLIDEVRIYDRALSAAEI 150
 
Name Accession Description Interval E-value
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 491-813 8.30e-90

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: 289.13  E-value: 8.30e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  491 TLNNGTPLFTSEFGEKGLRDPFIMKSKDGDKFYMLATDLKIDGraplnglngfaGAQANGSKYIEIWKSDDLVNWSKQSH 570
Cdd:cd08983      1 ALNGGNPVLTSTVGTKGVRDPFIIRGPEDGKFYLVATDLWIAG-----------GAQWNGSRGIGVWESTDLVNWSEQRL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  571 VK-VSSDYAGNTWAPEAYYDEEIGKYVVYWASNLYDNTDENsrkqltYNRMVYVTTDDFVNFSDPTVWIDvdrrggAGSG 649
Cdd:cd08983     70 VKmVSPPNAGNAWAPEAIYDPETGQYVVYWSSSLYGDGGGG------NHRIYYATTKDFKTFSEPKVLFD------PGFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  650 SIDVTVQKVGDTYYRIYKDE-NTMSLRQEKSTDLTAaiggagvknyadalkgsAWSEVATNIGKGQANGYgktftsgEGP 728
Cdd:cd08983    138 VIDTTIVKDGGTYYRFYKDEtTGKGIRLATSDSLTG-----------------PWTTVTTGGGAGTGGGV-------EGP 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  729 SLFKANDGDangyQYYLFADQPSYHqgpnHYVPMATEDIASGQWTVIGNKmpeanfptNSDGGKPRHGTVLPVTRAQYQK 808
Cdd:cd08983    194 TVFKLNDGG----KWYLYYDQYGGG----GYGPFETTDLASGTWTPASED--------YSLPGGPRHGTVLPITAAEYDA 257


                   ....*
gi 1802158205  809 VLEAY 813
Cdd:cd08983    258 LLAAW 262
aBig_2 pfam20578
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
 355-448 4.17e-13

Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.


Pssm-ID: 466727 [Multi-domain]  Cd Length: 89  Bit Score: 65.98  E-value: 4.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  355 AEQAKADLDVV--TIEDSDDIRSNFSVPTKGNNGSTISWEVTGGKDIATLGegvndksrtvTVKRPAAGSDAVTVTLKAI 432
Cdd:pfam20578    1 VAADKAALAIGyaGGDSASSVTQNLTLPTTGANGTTITWSSSNPAVISADG----------TVTRPAYGSGDATVTLTAT 70

                           90
                   ....*....|....*.
gi 1802158205  433 AKYGTATETKTFTVTI 448
Cdd:pfam20578   71 ITKGGATDTKTFTLTV 86
aBig_2 pfam20578
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
 283-351 4.76e-10

Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.


Pssm-ID: 466727 [Multi-domain]  Cd Length: 89  Bit Score: 57.12  E-value: 4.76e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802158205  283 TEDFALPTSAA-GVSIAWKSDNAAiaVDNATGkaTVTRPAATAADAEVILTATFGNNAKTA--DYTVLVPKQ 351
Cdd:pfam20578   22 TQNLTLPTTGAnGTTITWSSSNPA--VISADG--TVTRPAYGSGDATVTLTATITKGGATDtkTFTLTVLAL 89
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
510-747 1.66e-09

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 60.73  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKskDGDKFYMLATDlkidgraplnglngfagaqANGSKYIEIWKSDDLVNWSKQSHV-----KVSSDYAGNTWAP 584
Cdd:COG3507     33 DPSIIR--VGDTYYLYGTS-------------------FEYFPGLPIFHSKDLVNWELVGHAldrlpQWADPYSGGIWAP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  585 EAYYDEeiGKYVVYWasnlydnTDENSRKQLTYNRMvyVTTDDFVN-FSDPTVWIDvdrrggAGSGSIDVTVqkvgdtyy 663
Cdd:COG3507     92 DIRYHN--GKYYLYY-------TAVDGGKNRSGIGV--ATADDPEGpWSDPGPLVC------PGGNGIDPSV-------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  664 riYKDENtmslrqekstdltaaiggaG-----VKNYADALKGSAWSEVATNI-GKGQ--ANGYGKTFTsgEGPSLFKand 735
Cdd:COG3507    147 --FVDDD-------------------GkaylvYGSGGGGIYVAELDPDTGKLlGEPKtlAPGGEGGWI--EGPHIYK--- 200

                          250
                   ....*....|..
gi 1802158205  736 gdANGYqYYLFA 747
Cdd:COG3507    201 --RNGY-YYLFY 209
Big_4 pfam07532
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ...
 822-876 2.16e-09

Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.


Pssm-ID: 400079 [Multi-domain]  Cd Length: 59  Bit Score: 54.25  E-value: 2.16e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802158205  822 VDALSAETTVGVAPTLPETAHLTHADGSVSDVAVEWDAIDASFYAKTGTFTVKGI 876
Cdd:pfam07532    1 IENIEVTVAQGESYTLPTTVTATYSDGSVKEVPVTWDLTPNVDTSKPGTYTVEGT 55
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
 508-747 2.30e-08

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: 56.56  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  508 LRDPFIMKskDGDKFYMLATdlkidgraplnglnGFAGAqangsKYIEIWKSDDLVNWSKQSHV-----KVSSDYAGNTW 582
Cdd:pfam04616   10 YPDPSILR--VGDDYYLTTS--------------SFEWF-----PGIPIFHSKDLVNWKLVGPVlvrrsQLSGRGSNASW 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  583 APEAYYDEeiGKYVVYWasnlydnTDENSRkqltynrmVYVTTDDFVN--FSDPtVWIdvdrrgGAGSGSIDVTV--QKV 658
Cdd:pfam04616   69 APDISYHD--GKYYLYY-------TAVAHG--------IFVATADSPDgpWSDP-GKL------KSGGGGIDPSLfhDDD 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  659 GDTYY---RIYKDENTMSLR-QEKSTDLTAAIGGAGVKNYAdalkGSAWSEVATNigkgqangygktftsgEGPSLFKAN 734
Cdd:pfam04616  125 GKKYLvwgGWDPRHGHGGIYlQELDNDGLKLVGPVTKLIYP----GTRWVGGKVT----------------EGPHLYKRN 184

                          250
                   ....*....|...
gi 1802158205  735 DGdangyqYYLFA 747
Cdd:pfam04616  185 GY------YYLTY 191
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 81-258 4.87e-08

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 53.16  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205   81 LTGSQTISVPTTAIAGKkDVTVSIWLKNNyGNGNTAAAYIGAAKtgnypANGYWLLNPANPSGYaksVMTNAtaadpnns 160
Cdd:pfam13385    1 DGGSDYVTLPDALLPTS-DFTVSAWVKPD-SLPGWARAIISSSG-----GGGYSLGLDGDGRLR---FAVNG-------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  161 pwgtevGPGSTNAATTGTKATSDlALYTTVISGTNSTMSFYLNGKQVGDATYTipaGGLTNYGGLVAYIGKSSYADPNSK 240
Cdd:pfam13385   63 ------GNGGWDTVTSGASVPLG-QWTHVAVTYDGGTLRLYVNGVLVGSSTLT---GGPPPGTGGPLYIGRSPGGDDYFN 132

                          170
                   ....*....|....*...
gi 1802158205  241 LDVDDYAVYDTAISAADV 258
Cdd:pfam13385  133 GLIDEVRIYDRALSAAEI 150
 
Name Accession Description Interval E-value
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 491-813 8.30e-90

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: 289.13  E-value: 8.30e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  491 TLNNGTPLFTSEFGEKGLRDPFIMKSKDGDKFYMLATDLKIDGraplnglngfaGAQANGSKYIEIWKSDDLVNWSKQSH 570
Cdd:cd08983      1 ALNGGNPVLTSTVGTKGVRDPFIIRGPEDGKFYLVATDLWIAG-----------GAQWNGSRGIGVWESTDLVNWSEQRL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  571 VK-VSSDYAGNTWAPEAYYDEEIGKYVVYWASNLYDNTDENsrkqltYNRMVYVTTDDFVNFSDPTVWIDvdrrggAGSG 649
Cdd:cd08983     70 VKmVSPPNAGNAWAPEAIYDPETGQYVVYWSSSLYGDGGGG------NHRIYYATTKDFKTFSEPKVLFD------PGFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  650 SIDVTVQKVGDTYYRIYKDE-NTMSLRQEKSTDLTAaiggagvknyadalkgsAWSEVATNIGKGQANGYgktftsgEGP 728
Cdd:cd08983    138 VIDTTIVKDGGTYYRFYKDEtTGKGIRLATSDSLTG-----------------PWTTVTTGGGAGTGGGV-------EGP 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  729 SLFKANDGDangyQYYLFADQPSYHqgpnHYVPMATEDIASGQWTVIGNKmpeanfptNSDGGKPRHGTVLPVTRAQYQK 808
Cdd:cd08983    194 TVFKLNDGG----KWYLYYDQYGGG----GYGPFETTDLASGTWTPASED--------YSLPGGPRHGTVLPITAAEYDA 257


                   ....*
gi 1802158205  809 VLEAY 813
Cdd:cd08983    258 LLAAW 262
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
 509-807 1.95e-21

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: 94.81  E-value: 1.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  509 RDPFIMKskDGDKFYMLATDLKIDGraplnglngfagaqangSKYIEIWKSDDLVNWSKQSHV--KVSSDY--AGNTWAP 584
Cdd:cd08978      1 ADPSILK--DNGRYYIYATTDDTGT-----------------GTGIVVWKSKDLVNWKEEGTVlsRGKSKSwgTGNLWAP 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  585 EAYYDeEIGKYVVYW-ASNLYDNTdensrkqltynRMVYVTTDDfvnFSDPTVWIDVDRRGGAGSGSIDVTVQKVGD-TY 662
Cdd:cd08978     62 EVYYF-NSGKWYLYYsAVPNGGGG-----------RIYVATSDS---PEGPFTPIVSGKLGDRGSGSIDPTVFVDDDgKL 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  663 YRIYKDENTMS--LRQEKSTDLTAaigGAGVKNYADALKGSAwsevatnigkgqangyGKTFTSGEGPSLFKandgdANG 740
Cdd:cd08978    127 YLYYGDEDDSGdiYVAELDPDLLT---IKGDVTLLIGEVVGS----------------GFRGNYFEGPAVFK-----RNG 182

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802158205  741 YqYYLFADQPSYHqgPNHYVPMATEDIASGQWTVIGNKMPEANFPTNsDGGKPRHGTVLPVTRAQYQ 807
Cdd:cd08978    183 Y-YYLIYSAGGTD--GGYAIGYATSDSPLGPWEKASHNPGLQTSGAT-GIYGPGHGSIFQDEGDRWY 245
aBig_2 pfam20578
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
 355-448 4.17e-13

Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.


Pssm-ID: 466727 [Multi-domain]  Cd Length: 89  Bit Score: 65.98  E-value: 4.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  355 AEQAKADLDVV--TIEDSDDIRSNFSVPTKGNNGSTISWEVTGGKDIATLGegvndksrtvTVKRPAAGSDAVTVTLKAI 432
Cdd:pfam20578    1 VAADKAALAIGyaGGDSASSVTQNLTLPTTGANGTTITWSSSNPAVISADG----------TVTRPAYGSGDATVTLTAT 70

                           90
                   ....*....|....*.
gi 1802158205  433 AKYGTATETKTFTVTI 448
Cdd:pfam20578   71 ITKGGATDTKTFTLTV 86
aBig_2 pfam20578
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
 283-351 4.76e-10

Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.


Pssm-ID: 466727 [Multi-domain]  Cd Length: 89  Bit Score: 57.12  E-value: 4.76e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802158205  283 TEDFALPTSAA-GVSIAWKSDNAAiaVDNATGkaTVTRPAATAADAEVILTATFGNNAKTA--DYTVLVPKQ 351
Cdd:pfam20578   22 TQNLTLPTTGAnGTTITWSSSNPA--VISADG--TVTRPAYGSGDATVTLTATITKGGATDtkTFTLTVLAL 89
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
510-747 1.66e-09

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 60.73  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKskDGDKFYMLATDlkidgraplnglngfagaqANGSKYIEIWKSDDLVNWSKQSHV-----KVSSDYAGNTWAP 584
Cdd:COG3507     33 DPSIIR--VGDTYYLYGTS-------------------FEYFPGLPIFHSKDLVNWELVGHAldrlpQWADPYSGGIWAP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  585 EAYYDEeiGKYVVYWasnlydnTDENSRKQLTYNRMvyVTTDDFVN-FSDPTVWIDvdrrggAGSGSIDVTVqkvgdtyy 663
Cdd:COG3507     92 DIRYHN--GKYYLYY-------TAVDGGKNRSGIGV--ATADDPEGpWSDPGPLVC------PGGNGIDPSV-------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  664 riYKDENtmslrqekstdltaaiggaG-----VKNYADALKGSAWSEVATNI-GKGQ--ANGYGKTFTsgEGPSLFKand 735
Cdd:COG3507    147 --FVDDD-------------------GkaylvYGSGGGGIYVAELDPDTGKLlGEPKtlAPGGEGGWI--EGPHIYK--- 200

                          250
                   ....*....|..
gi 1802158205  736 gdANGYqYYLFA 747
Cdd:COG3507    201 --RNGY-YYLFY 209
Big_4 pfam07532
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ...
 822-876 2.16e-09

Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.


Pssm-ID: 400079 [Multi-domain]  Cd Length: 59  Bit Score: 54.25  E-value: 2.16e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802158205  822 VDALSAETTVGVAPTLPETAHLTHADGSVSDVAVEWDAIDASFYAKTGTFTVKGI 876
Cdd:pfam07532    1 IENIEVTVAQGESYTLPTTVTATYSDGSVKEVPVTWDLTPNVDTSKPGTYTVEGT 55
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
 508-747 2.30e-08

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: 56.56  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  508 LRDPFIMKskDGDKFYMLATdlkidgraplnglnGFAGAqangsKYIEIWKSDDLVNWSKQSHV-----KVSSDYAGNTW 582
Cdd:pfam04616   10 YPDPSILR--VGDDYYLTTS--------------SFEWF-----PGIPIFHSKDLVNWKLVGPVlvrrsQLSGRGSNASW 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  583 APEAYYDEeiGKYVVYWasnlydnTDENSRkqltynrmVYVTTDDFVN--FSDPtVWIdvdrrgGAGSGSIDVTV--QKV 658
Cdd:pfam04616   69 APDISYHD--GKYYLYY-------TAVAHG--------IFVATADSPDgpWSDP-GKL------KSGGGGIDPSLfhDDD 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  659 GDTYY---RIYKDENTMSLR-QEKSTDLTAAIGGAGVKNYAdalkGSAWSEVATNigkgqangygktftsgEGPSLFKAN 734
Cdd:pfam04616  125 GKKYLvwgGWDPRHGHGGIYlQELDNDGLKLVGPVTKLIYP----GTRWVGGKVT----------------EGPHLYKRN 184

                          250
                   ....*....|...
gi 1802158205  735 DGdangyqYYLFA 747
Cdd:pfam04616  185 GY------YYLTY 191
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 81-258 4.87e-08

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 53.16  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205   81 LTGSQTISVPTTAIAGKkDVTVSIWLKNNyGNGNTAAAYIGAAKtgnypANGYWLLNPANPSGYaksVMTNAtaadpnns 160
Cdd:pfam13385    1 DGGSDYVTLPDALLPTS-DFTVSAWVKPD-SLPGWARAIISSSG-----GGGYSLGLDGDGRLR---FAVNG-------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  161 pwgtevGPGSTNAATTGTKATSDlALYTTVISGTNSTMSFYLNGKQVGDATYTipaGGLTNYGGLVAYIGKSSYADPNSK 240
Cdd:pfam13385   63 ------GNGGWDTVTSGASVPLG-QWTHVAVTYDGGTLRLYVNGVLVGSSTLT---GGPPPGTGGPLYIGRSPGGDDYFN 132

                          170
                   ....*....|....*...
gi 1802158205  241 LDVDDYAVYDTAISAADV 258
Cdd:pfam13385  133 GLIDEVRIYDRALSAAEI 150
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
 510-606 2.67e-07

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: 53.33  E-value: 2.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKskDGDKFYMLATDlkidgraplnglngfagaqANGSKYIEIWKSDDLVNWSKQSHVKVSSDYAGNT--WAPEAY 587
Cdd:cd08991      2 DPFVLK--HNGTYYLYGTG-------------------GDDGRGFKVYVSDDLVNWEYPGGALEEPGLWGTKgfWAPEVF 60

                           90
                   ....*....|....*....
gi 1802158205  588 YDEeiGKYVVYWASNLYDN 606
Cdd:cd08991     61 YYN--GKFYMYYSANGGDH 77
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
 510-600 3.42e-06

Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A; This glycosyl hydrolase family 43 (GH43) subgroup 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: 49.85  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKsKDGDKFYMLATDlkidgraplnglngfagaqangsKYIEIWKSDDLVNWSKQSHV---------KVSSDYAGN 580
Cdd:cd08998      3 DPSIIK-DDGGTYYVFSTG-----------------------AGIQIRTSKDLVNWEFVGTVfpegpawaaAEVPGGAGG 58

                           90       100
                   ....*....|....*....|
gi 1802158205  581 TWAPEAYYDEeiGKYVVYWA 600
Cdd:cd08998     59 LWAPDVVYVN--GRYYLYYS 76
GH43_Bt1873-like cd08981
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This ...
 508-595 6.94e-06

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the GH43 enzymes in this family may display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350095 [Multi-domain]  Cd Length: 289  Bit Score: 49.06  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  508 LRDPFIMKSKDGDKFYMLATDlkiDGRAPLNGLNGFagaqangskyiEIWKSDDLVNWSKQS---HVKVSSDYAGNTWAP 584
Cdd:cd08981      6 IRDPFILADKKTGTYYLYGTT---DKDCWWGKGTGF-----------DVYVSKDLENWEGPYevfRPPEDFWADRNFWAP 71

                           90
                   ....*....|..
gi 1802158205  585 EAY-YDeeiGKY 595
Cdd:cd08981     72 EVHeYN---GKY 80
GH43_LbAraf43-like cd18820
Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis ...
 510-666 1.73e-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: 47.52  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKskDGDKFYMLATDlkidgraplnglngfagaqanGSKyIEIWKSDDLVNWSKQSHVKVSSD----YAGNTWAPE 585
Cdd:cd18820      2 DPWVVY--HDGYYYLTFTT---------------------GDR-ITIWKSKTLTGLGTAEPKVVWTPpdpsRSCNIWAPE 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  586 AYYDEeiGKYVVYWASNlyDNTDEnsrkqltyNRMVYV---TTDDfvnfsDPT-VWIDVDR-RGGAGSGSIDVTVQKVGD 660
Cdd:cd18820     58 LHFID--GRWYIYYAAD--DGDNA--------NHRMYVlesASDD-----PPLgPYTFKGRlADPTDKWAIDGTVLEHNG 120


                   ....*.
gi 1802158205  661 TYYRIY 666
Cdd:cd18820    121 KLYFVW 126
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
 510-600 3.01e-05

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: 47.18  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKSKDGDkFYMLAT-DLKIDGRaplnglngfagaqanGSKYIEIWKSDDLVNWSK-----QSHVKVSSDYAGNTWA 583
Cdd:cd18616     10 DPTVIRGDDGY-FYAYATeDPWGDGG---------------GFRLVPILRSKDLVNWEYvgdafTSKPRWKWDPGGGLWA 73

                           90
                   ....*....|....*...
gi 1802158205  584 PE-AYYDeeiGKYVVYWA 600
Cdd:cd18616     74 PDiRYID---GKYVLYYS 88
Glyco_hydro_32N pfam00251
Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal ...
 462-582 2.71e-04

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


Pssm-ID: 425557  Cd Length: 308  Bit Score: 44.16  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  462 VWAFFTG----EGVGGEKISLAASKgNDALDWNTLNNGTPLFT-SEFGEKGLRDPFIMKSKDGdKFYMLAtdlkidgrap 536
Cdd:pfam00251   81 LVLIYTGnvrdEGRDTQVQNLAYSK-DDGRTFTKYPNNPVIINlPAGYTKHFRDPKVAWYEDG-KWYMVL---------- 148

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1802158205  537 lnglngfaGAQANGSKY-IEIWKSDDLVNWSKQSHVKVSSDYAGNTW 582
Cdd:pfam00251  149 --------GAQDNDKKGkILLYKSDDLKNWTFVGELLHSNDGGGYMW 187
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
 519-755 8.30e-04

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: 42.50  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  519 GDKFYMLATDLkidgraplnglngfagaqaNGSKYIEIWKSDDLVNWSKQSHV-------------KVSSDYAGNTWAPE 585
Cdd:cd09001     20 GDTYYMVSSTM-------------------HFSPGAPILHSKDLVNWEIVGYVvdrlddgdayyleDGKNAYGKGIWAPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  586 -AYYDeeiGKYVVYWASNlydntDENsrkqlTYnrmVYVTTD----------DFVNFSDPTVWIDVDRRG--GAGSGSID 652
Cdd:cd09001     81 lRYHN---GKFYVYFCTN-----TGG-----TY---VYTADDpagpwsrpalIGKGYHDPSLLFDDDGKAylVYGNGEIR 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  653 VTvqkvgdtyyriykdentmslrqEKSTDLTAAIGgagvknyadalkgsawseVATNIGKGQANGYGktftsGEGPSLFK 732
Cdd:cd09001    145 LT----------------------ELSPDGTGVGG------------------EGRVIIDGTEEGLG-----AEGSHLYK 179

                          250       260
                   ....*....|....*....|...
gi 1802158205  733 ANDgdangyQYYLFADQPSYHQG 755
Cdd:cd09001    180 ING------YYYIFNIEWGGGGR 196
SacC COG1621
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];
458-582 9.53e-04

Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];


Pssm-ID: 441228 [Multi-domain]  Cd Length: 459  Bit Score: 42.99  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  458 DEAYVWAFFTG-----EGVGGEKISLAASkgNDALDWN------TLNNGTPLFTSEFgekglRDPFIMKskDGDKFYMLA 526
Cdd:COG1621     86 DDGNLVLFYTGnvrdgDGGRRQYQCLAYS--TDGRTFTkyegnpVIPNPPGGYTKDF-----RDPKVWW--DDGKWYMVL 156

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802158205  527 tdlkidgraplnglngfaGAQ-ANGSKYIEIWKSDDLVNWSKQSHVKVSSDYAGNTW 582
Cdd:COG1621    157 ------------------GAQtGDGKGTVLLYTSPDLKNWTYLGEFGEGDGAFGYMW 195
GH32_FFase cd08996
Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves ...
 453-566 1.29e-03

Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350110  Cd Length: 281  Bit Score: 41.85  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  453 AAEEKDEAYvwAFFTG---EGVGGEKISLAASKgNDALDW-NTLNNGTPLFTSEFGEKGLRDPFIMKskDGDKFYMLATd 528
Cdd:cd08996     68 AVVDDGKPT--LFYTGvrdLGDGRQTQCLATSD-DDLITWeKYPGNPVIPPPPGGGVTDFRDPFVWK--EGGTWYMVVG- 141

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1802158205  529 lkidgraplNGLNGFAGAqangskyIEIWKSDDLVNWS 566
Cdd:cd08996    142 ---------GGLEDGGGA-------VLLYRSDDLRDWE 163
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 8-431 2.55e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 42.07  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205    8 ATGLTVGVATLLAGLVLPMTASAESASPIDASPIIHYSFDNALTSKTIANEGSAANSDATLSGDATVANGQINLTGSQTI 87
Cdd:COG4625     99 GGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGG 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205   88 SVPTTAIAGKKDVTVSIWLKNNYGNGNTAAAYIGAAKTGNYPANGYWLLNPANPSGYAKSVMTNATAADPNNSPWGTEVG 167
Cdd:COG4625    179 GGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGN 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  168 PGSTNAATTGTKATSDLALYTTVISGTNSTMSFYLNGKQVGDATYTIPAGGLTNYGGLVAYIGKSSYADPNSKLDVDDYA 247
Cdd:COG4625    259 GGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGG 338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  248 VYDTAISAADVTKLYDAQVLDKAEAAVKAAVPASATEDFALPTSAAGVSIAWKSDNAAIAVDNATGKATVTRPAATAADA 327
Cdd:COG4625    339 GSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGG 418

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  328 EVILTATFGNNAKTADYTVLVPKQLSDAEQAKADLDVVTIEDSDDIRSNFSVPTKGNNGSTISWEVTGGKDIATLGEGVN 407
Cdd:COG4625    419 AAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTVNGGGNYTQ 498

                          410       420
                   ....*....|....*....|....
gi 1802158205  408 DKSRTVTVKRPAAGSDAVTVTLKA 431
Cdd:COG4625    499 SAGSTLAVEVDAANSDRLVVTGTA 522
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
 556-606 6.94e-03

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: 39.52  E-value: 6.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1802158205  556 IWKSDDLVNWSKQSHvkVSSDYAGNTWAPE-AYYDeeiGKYVVYWASNLYDN 606
Cdd:cd09002     37 IWHSRDLVNWEPIGA--ALTEYIGTVWAPDlIKHD---GRYYIYFPAKGGTN 83
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
 554-600 7.79e-03

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: 39.57  E-value: 7.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802158205  554 IEIWKSDDLVNWSKQSHV---------KVSSDYAGNTWAPEAYYDEeiGKYVVYWA 600
Cdd:cd18830     22 ISVMSSKDLKNWTQERPVfdeppqwakEAVPGFNGHIWAPDISFHN--GRYYLYYS 75
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 510-607 8.39e-03

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: 39.57  E-value: 8.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  510 DPFIMKSkdGDKFYMLATDlkidgraplnglNGFAGAqanGSKYIEIWKSDDLVNW--------SKQSHvkVSSDYAGNT 581
Cdd:cd18828      2 DPDIAYF--DGKYYIYPTT------------DGFPGW---SGTQFHVFSSDDLVTWkdegvildLKNDQ--VVPWATGNA 62

                           90       100
                   ....*....|....*....|....*.
gi 1802158205  582 WAPEAyyDEEIGKYVVYWASNLYDNT 607
Cdd:cd18828     63 WAPTI--EERDGKYYFYFCGKNPDGR 86
GH_J cd08979
Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase ...
 457-588 8.57e-03

Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350093 [Multi-domain]  Cd Length: 292  Bit Score: 39.48  E-value: 8.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  457 KDEAYVW-AFFTG---EGVGGEKISLAASKgNDALDWNTLNNGTPLFT-----SEFGEKGLRDPFIMKSKDGDKFYMLAT 527
Cdd:cd08979     69 FTSDGKWrAFYTGfsgKHYGVQSQTIAYSK-DLASWSSLNINGVPQFPdelppSSGDNQTFRDPHVVWDKEKGHWYMVFT 147

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802158205  528 dlkidGRAPLNGLngfagaqangskyIEIWKSDDLVNWSKQSHVKVSSDYAGNTWAPEAYY 588
Cdd:cd08979    148 -----AREGANGV-------------LGMYESTDLKHWKKVMKPIASNTVTGEWECPNLVK 190
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
 508-588 9.20e-03

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: 39.13  E-value: 9.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802158205  508 LRDPFIMKSKDGdKFYMLATdlkidgrAPLNGLNGFAGaqangskYIEIWKSDDLVNWS-------------KQSHVKVS 574
Cdd:cd08986      2 LRDPYITLGPDG-YYYLTGT-------TGGPDWWGVND-------GIRLWRSKDLKDWEylglvwdlekdgwWQWEPQWW 66

                           90
                   ....*....|....*..
gi 1802158205  575 SDYAGNT---WAPEAYY 588
Cdd:cd08986     67 TPDSKNKralWAPEIHY 83
 
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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