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Conserved domains on  [gi|302749813|gb|ADL66908|]
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SacB [Cloning vector pNit::ET]

Protein Classification

glycoside hydrolase family protein( domain architecture ID 52385)

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

Gene Ontology:  GO:0016798
PubMed:  8535779

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH43_62_32_68_117_130 super family cl14647
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 44-470 1.09e-150

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


The actual alignment was detected with superfamily member pfam02435:

Pssm-ID: 449341  Cd Length: 419  Bit Score: 435.80  E-value: 1.09e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813   44 SHITRHDMLQIPE-QQKNEKYQVPEFDSSTIKNISSAKG-----LDVWDSWPLQNADGTVANYHGYHIVFALAGDPK--- 114
Cdd:pfam02435   4 TQWTRADALKINKnDATTERYAIPYFNAKTMPNIPADFPvmsddLWVWDTWPLRDADGTVVSYNGWSVIFALTADPNagy 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  115 --NADDTSIYMFYQKVGETSIDSWKNAGRVFKDSDKfdandsilkDQTQEWSGSATFTS-DGKIRLFYT--DFSGKHYGK 189
Cdd:pfam02435  84 ndRHGDARIGYFYSKAGDNNFDGWKNGGRVFKDGAS---------PRTAEWSGSAILAPgDGSVELFYTsvDFNDKPGNN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  190 QTLTTAQVNVS-ASDSSLNINGVEDYKSIFDGDGKTYQNVQQfidegnyssGDNHTLRDPHYVEDK--GHKYLVFEANTG 266
Cdd:pfam02435 155 QALITATKGRIyADDKGVWFDGFEDVKSLFQADGVYYQNYAQ---------NNFWNFRDPHVFEDPhdGKTYMVFEANTA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  267 TEDGYqgeeslfnkAYYGKSTSFFRQESQKLLQSDKKRTAELANGALGMIELNDDY-TLKKVMKPLIASNTVTDEIERAN 345
Cdd:pfam02435 226 TERGS---------ANYGEAELGPVPSLPNTLDPQMYKGARYANAAIGIAVAKDDSrTEWEFLPPLVTANGVNDQTERPH 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  346 VFKMNGKWYLFTDSRGSKMTiDGITSNDIYMLGYVSNSLTGPYKPLNKTGLVLKMDLDPNDVTF-TYSHFAVPQakGNNV 424
Cdd:pfam02435 297 VVFQNGKYYLFTISHKSTYA-DGVTGPDGVYGFVVSNGLTGPYKPLNGSGLVLGNPPSQAPWRTqTYSHYVMPN--GLVT 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 302749813  425 VITSYMTNRGFYADKQSTFAPSFLLNIKGKKTSVVKDSILEQGQLT 470
Cdd:pfam02435 374 SFIDYMTNRGENYRIGGTLAPTVLIELKGDRTFVVEVYDTQYGYIP 419
 
Name Accession Description Interval E-value
Glyco_hydro_68 pfam02435
Levansucrase/Invertase; This Pfam family consists of the glycosyl hydrolase 68 family, ...
 44-470 1.09e-150

Levansucrase/Invertase; This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas.


Pssm-ID: 426772  Cd Length: 419  Bit Score: 435.80  E-value: 1.09e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813   44 SHITRHDMLQIPE-QQKNEKYQVPEFDSSTIKNISSAKG-----LDVWDSWPLQNADGTVANYHGYHIVFALAGDPK--- 114
Cdd:pfam02435   4 TQWTRADALKINKnDATTERYAIPYFNAKTMPNIPADFPvmsddLWVWDTWPLRDADGTVVSYNGWSVIFALTADPNagy 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  115 --NADDTSIYMFYQKVGETSIDSWKNAGRVFKDSDKfdandsilkDQTQEWSGSATFTS-DGKIRLFYT--DFSGKHYGK 189
Cdd:pfam02435  84 ndRHGDARIGYFYSKAGDNNFDGWKNGGRVFKDGAS---------PRTAEWSGSAILAPgDGSVELFYTsvDFNDKPGNN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  190 QTLTTAQVNVS-ASDSSLNINGVEDYKSIFDGDGKTYQNVQQfidegnyssGDNHTLRDPHYVEDK--GHKYLVFEANTG 266
Cdd:pfam02435 155 QALITATKGRIyADDKGVWFDGFEDVKSLFQADGVYYQNYAQ---------NNFWNFRDPHVFEDPhdGKTYMVFEANTA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  267 TEDGYqgeeslfnkAYYGKSTSFFRQESQKLLQSDKKRTAELANGALGMIELNDDY-TLKKVMKPLIASNTVTDEIERAN 345
Cdd:pfam02435 226 TERGS---------ANYGEAELGPVPSLPNTLDPQMYKGARYANAAIGIAVAKDDSrTEWEFLPPLVTANGVNDQTERPH 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  346 VFKMNGKWYLFTDSRGSKMTiDGITSNDIYMLGYVSNSLTGPYKPLNKTGLVLKMDLDPNDVTF-TYSHFAVPQakGNNV 424
Cdd:pfam02435 297 VVFQNGKYYLFTISHKSTYA-DGVTGPDGVYGFVVSNGLTGPYKPLNGSGLVLGNPPSQAPWRTqTYSHYVMPN--GLVT 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 302749813  425 VITSYMTNRGFYADKQSTFAPSFLLNIKGKKTSVVKDSILEQGQLT 470
Cdd:pfam02435 374 SFIDYMTNRGENYRIGGTLAPTVLIELKGDRTFVVEVYDTQYGYIP 419
GH68 cd08997
Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase; ...
 84-459 2.06e-145

Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase; Glycosyl hydrolase family 68 (GH68) consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Levansucrase, also known as beta-D-fructofuranosyl transferase, catalyzes the transfer of the sucrose fructosyl moiety to a growing levan chain. Similarly, inulosucrase catalyzes long inulin-type of fructans, and beta-fructofuranosidases create fructooligosaccharides (FOS). However, in the absence of high fructan/sucrose ratio, some GH68 enzymes can also use fructan as donor substrate. GH68 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. 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. Biotechnological applications of these enzymes include use of inulin in inexpensive production of rich fructose syrups as well as use of FOS as health-promoting pre-biotics.


Pssm-ID: 350111  Cd Length: 354  Bit Score: 419.74  E-value: 2.06e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  84 VWDSWPLQNADGTVANYHGYHIVFALAGDP-----KNADDTSIYMFYQKVGETSIDSWKnagrvfkdsdkfdANDSILKD 158
Cdd:cd08997    1 VWDSWPLQDADGTVANYNGYRLVFALTAPRnpdpdDRHDDARIRLFYSRDGGWWDLGGK-------------AFPDGLTP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 159 QTQEWSGSATFTSDGKIRLFYTDFSGKHYGKQTLTTAQVNVSASDSS----LNINGVEDYKSIFDGDGKTYQNVQQFide 234
Cdd:cd08997   68 GSREWSGSAVLDPDGTVTLFYTAAGRRGEAGQTFEQRLFEVTATLSGdgggVSISGWTDHKEIFEADGEIYQTVDQG--- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 235 gNYSSGDNHTLRDPHYVEDK--GHKYLVFEANTGTEDGYQGEESLFNKayygkstsffrqesQKLLQSDKKRTAELANGA 312
Cdd:cd08997  145 -GGAGGDIKAFRDPHYFRDPadGKRYLVFEANTAGSRGQQGCNNLDNG--------------QVLKNSVKKDGASYFNGA 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 313 LGMIELNDDYTLK-KVMKPLIASNTVTDEIERANVFKMNGKWYLFTDSRGSKMTIDGITSNDiYMLGYVSNSLTGPYKPL 391
Cdd:cd08997  210 IGLAEANNDDLTKwELLPPLLSANGVNDELERPHIVVHNGKYYLFTSTHGSTFAPDGLSGPT-GLYGFVSDSLRGPYKPL 288

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302749813 392 NKTGLVLKMdlDPNDVTFTYSHFAVPqakgnNVVITSYMTNRGFYADKQ-----STFAPSFLLNIKGKKTSVV 459
Cdd:cd08997  289 NGSGLVLAN--PPEAPFQTYSWYVLP-----DLLVTSFVDTRGLAGGEArarfgGTFAPSFKLRIDGDTTRVV 354
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
315-394 2.57e-04

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 43.01  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 315 MIELNDDyTLKKVMKP-LIASNTVTDEIERANVFKMNGKWYLFTdSRGSkmtidgiTSNDIYMLGY-VSNSLTGPYKPLN 392
Cdd:COG3507  167 VAELDPD-TGKLLGEPkTLAPGGEGGWIEGPHIYKRNGYYYLFY-SEGG-------TCNSGYAVRVaRSKSPTGPYEDAP 237


                 ..
gi 302749813 393 KT 394
Cdd:COG3507  238 GN 239
 
Name Accession Description Interval E-value
Glyco_hydro_68 pfam02435
Levansucrase/Invertase; This Pfam family consists of the glycosyl hydrolase 68 family, ...
 44-470 1.09e-150

Levansucrase/Invertase; This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas.


Pssm-ID: 426772  Cd Length: 419  Bit Score: 435.80  E-value: 1.09e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813   44 SHITRHDMLQIPE-QQKNEKYQVPEFDSSTIKNISSAKG-----LDVWDSWPLQNADGTVANYHGYHIVFALAGDPK--- 114
Cdd:pfam02435   4 TQWTRADALKINKnDATTERYAIPYFNAKTMPNIPADFPvmsddLWVWDTWPLRDADGTVVSYNGWSVIFALTADPNagy 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  115 --NADDTSIYMFYQKVGETSIDSWKNAGRVFKDSDKfdandsilkDQTQEWSGSATFTS-DGKIRLFYT--DFSGKHYGK 189
Cdd:pfam02435  84 ndRHGDARIGYFYSKAGDNNFDGWKNGGRVFKDGAS---------PRTAEWSGSAILAPgDGSVELFYTsvDFNDKPGNN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  190 QTLTTAQVNVS-ASDSSLNINGVEDYKSIFDGDGKTYQNVQQfidegnyssGDNHTLRDPHYVEDK--GHKYLVFEANTG 266
Cdd:pfam02435 155 QALITATKGRIyADDKGVWFDGFEDVKSLFQADGVYYQNYAQ---------NNFWNFRDPHVFEDPhdGKTYMVFEANTA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  267 TEDGYqgeeslfnkAYYGKSTSFFRQESQKLLQSDKKRTAELANGALGMIELNDDY-TLKKVMKPLIASNTVTDEIERAN 345
Cdd:pfam02435 226 TERGS---------ANYGEAELGPVPSLPNTLDPQMYKGARYANAAIGIAVAKDDSrTEWEFLPPLVTANGVNDQTERPH 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  346 VFKMNGKWYLFTDSRGSKMTiDGITSNDIYMLGYVSNSLTGPYKPLNKTGLVLKMDLDPNDVTF-TYSHFAVPQakGNNV 424
Cdd:pfam02435 297 VVFQNGKYYLFTISHKSTYA-DGVTGPDGVYGFVVSNGLTGPYKPLNGSGLVLGNPPSQAPWRTqTYSHYVMPN--GLVT 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 302749813  425 VITSYMTNRGFYADKQSTFAPSFLLNIKGKKTSVVKDSILEQGQLT 470
Cdd:pfam02435 374 SFIDYMTNRGENYRIGGTLAPTVLIELKGDRTFVVEVYDTQYGYIP 419
GH68 cd08997
Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase; ...
 84-459 2.06e-145

Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase; Glycosyl hydrolase family 68 (GH68) consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Levansucrase, also known as beta-D-fructofuranosyl transferase, catalyzes the transfer of the sucrose fructosyl moiety to a growing levan chain. Similarly, inulosucrase catalyzes long inulin-type of fructans, and beta-fructofuranosidases create fructooligosaccharides (FOS). However, in the absence of high fructan/sucrose ratio, some GH68 enzymes can also use fructan as donor substrate. GH68 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. 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. Biotechnological applications of these enzymes include use of inulin in inexpensive production of rich fructose syrups as well as use of FOS as health-promoting pre-biotics.


Pssm-ID: 350111  Cd Length: 354  Bit Score: 419.74  E-value: 2.06e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  84 VWDSWPLQNADGTVANYHGYHIVFALAGDP-----KNADDTSIYMFYQKVGETSIDSWKnagrvfkdsdkfdANDSILKD 158
Cdd:cd08997    1 VWDSWPLQDADGTVANYNGYRLVFALTAPRnpdpdDRHDDARIRLFYSRDGGWWDLGGK-------------AFPDGLTP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 159 QTQEWSGSATFTSDGKIRLFYTDFSGKHYGKQTLTTAQVNVSASDSS----LNINGVEDYKSIFDGDGKTYQNVQQFide 234
Cdd:cd08997   68 GSREWSGSAVLDPDGTVTLFYTAAGRRGEAGQTFEQRLFEVTATLSGdgggVSISGWTDHKEIFEADGEIYQTVDQG--- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 235 gNYSSGDNHTLRDPHYVEDK--GHKYLVFEANTGTEDGYQGEESLFNKayygkstsffrqesQKLLQSDKKRTAELANGA 312
Cdd:cd08997  145 -GGAGGDIKAFRDPHYFRDPadGKRYLVFEANTAGSRGQQGCNNLDNG--------------QVLKNSVKKDGASYFNGA 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 313 LGMIELNDDYTLK-KVMKPLIASNTVTDEIERANVFKMNGKWYLFTDSRGSKMTIDGITSNDiYMLGYVSNSLTGPYKPL 391
Cdd:cd08997  210 IGLAEANNDDLTKwELLPPLLSANGVNDELERPHIVVHNGKYYLFTSTHGSTFAPDGLSGPT-GLYGFVSDSLRGPYKPL 288

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302749813 392 NKTGLVLKMdlDPNDVTFTYSHFAVPqakgnNVVITSYMTNRGFYADKQ-----STFAPSFLLNIKGKKTSVV 459
Cdd:cd08997  289 NGSGLVLAN--PPEAPFQTYSWYVLP-----DLLVTSFVDTRGLAGGEArarfgGTFAPSFKLRIDGDTTRVV 354
GH_J cd08979
Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase ...
 85-450 1.70e-106

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: 318.36  E-value: 1.70e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  85 WDSWPLQNADGtvanyhgYHIVFALAGDPKN-ADDTSIYMFYQKVGETSIDSWKNAGrvfkdsdkfdANDSILKDQTQEW 163
Cdd:cd08979    1 WDPWPLQNANG-------YYHLFYLYGPPKNfADNVSIGHAYSKDLENWIDLPKALG----------ANDTISDDQTQEW 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 164 SGSATFTSDGKIRLFYTDFSGKHYGKQTLTTAQVNVSASDSSLNINGVEdyksifdgdgktyqnvqQFIDEGNYSSGDNH 243
Cdd:cd08979   64 SGSATFTSDGKWRAFYTGFSGKHYGVQSQTIAYSKDLASWSSLNINGVP-----------------QFPDELPPSSGDNQ 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 244 TLRDPHYVEDK--GHKYLVFEANTGtedgyqgeeslfnkayygkstsffrqesqkllqsdkkrtaelANGALGMIELNDD 321
Cdd:cd08979  127 TFRDPHVVWDKekGHWYMVFTAREG------------------------------------------ANGVLGMYESTDL 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 322 YTLKKVMKPlIASNTVTDEIERANVFKMNGKWYLFTDSRGSKmtidGITSNDIYMLGYVSNSLTGPYKPLNKTGLVLKMD 401
Cdd:cd08979  165 KHWKKVMKP-IASNTVTGEWECPNLVKMNGRWYLFFGSRGSK----GITSNGIHYLYAVGPSGPWRYKPLNKTGLVLSTD 239

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302749813 402 LDPNDVTFTYSHFAVPQAKGNNVVITSYMTNRGFYAD----KQSTFAPSFLLN 450
Cdd:cd08979  240 LDPDDGTFFYAGKLVPDAKGNNLVLTGWMPNRGFYADsgadWQSGFAIPRLLN 292
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
 247-395 6.78e-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: 44.49  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 247 DPHYVEDKGHKYLvfeantgtedgyqgeeslfnkaYYGkstSFFrqesqkllqsdkkrtaelangALGMIELNDDYT-LK 325
Cdd:cd18616  131 DPFVFEDDGKKYL----------------------FWG---SFY---------------------GIYAVELTADGLaLK 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302749813 326 KVMKPLIASNTvtdeIERANVFKMNGKWYLFTdSRGSKMtiDGITSndiymlGY-----VSNSLTGPYkpLNKTG 395
Cdd:cd18616  165 PGEKVQIAGDR----YEGPYIVKRDGYYYLFG-SAGSCC--EGPNS------TYrvvvgRSESLLGPY--VDRDG 224
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
315-394 2.57e-04

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 43.01  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 315 MIELNDDyTLKKVMKP-LIASNTVTDEIERANVFKMNGKWYLFTdSRGSkmtidgiTSNDIYMLGY-VSNSLTGPYKPLN 392
Cdd:COG3507  167 VAELDPD-TGKLLGEPkTLAPGGEGGWIEGPHIYKRNGYYYLFY-SEGG-------TCNSGYAVRVaRSKSPTGPYEDAP 237


                 ..
gi 302749813 393 KT 394
Cdd:COG3507  238 GN 239
GH32_EcAec43-like cd08995
Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 ...
 94-389 3.46e-04

Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2); This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). GH32 family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize.


Pssm-ID: 350109 [Multi-domain]  Cd Length: 281  Bit Score: 42.56  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813  94 DGTvanYHGYHIvFALAGDPKNADDTSIYMFyqkvgeTSID--SWKNAGRVFKDSDKFDANDSIlkdqtqeWSGSAtFTS 171
Cdd:cd08995    9 DGK---FHLFYL-HDPRDPAPHRGGHPWALV------TTKDlvHWTEHGEAIPYGGDDDQDLAI-------GTGSV-IKD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 172 DGKIRLFYTDFSGKH-YGKQTLTTAQvnvsasdSSLNINGVEDYKSIFDGDGKTYqnvqqfidegnyssgDNHTLRDPH- 249
Cdd:cd08995   71 DGTYHAFYTGHNPDFgKPKQVIMHAT-------STDLKTWTKDPEFTFIADPEGY---------------EKNDFRDPFv 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302749813 250 -YVEDKGhKYLVfeantgtedgyqgeeslfnkayygkstsffrqesqkLLQSDKKRTAELANGALGMIELNDdytLK--K 326
Cdd:cd08995  129 fWNEEEG-EYWM------------------------------------LVAARKNDGPGNRRGCIALYTSKD---LKnwT 168

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302749813 327 VMKPLIASNTvTDEIERANVFKMNGKWYL-FTDSRGSKMTidgitsndIYMlgyVSNSLTGPYK 389
Cdd:cd08995  169 FEGPFYAPGS-YNMPECPDLFKMGDWWYLvFSEFSERRKT--------HYR---ISDSPEGPWR 220
 
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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