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Conserved domains on  [gi|2588820556|ref|WP_314602092|]
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glycosyltransferase [Enterobacter sichuanensis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
7-208 6.20e-49

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd04195:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 201  Bit Score: 160.56  E-value: 6.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   7 VIMSIYKSDDPEALRVALDSLINQTYPCD-IFVYQDGEIPLALTSVIQDYVDNRQIKLTSCLVNKGLAHGLNTLINEVlq 85
Cdd:cd04195     2 VLMSVYIKEKPEFLREALESILKQTLPPDeVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHC-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  86 gDYIYIARMDSDDISRPERMFEQVSYLEKNPQIDICGTFCQEFGSTYA-LTEKRLPKAHEDLVKFSIARCPFIHPTVMFR 164
Cdd:cd04195    80 -TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNdIGKRRLPTSHDDILKFARRRSPFNHPTVMFR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2588820556 165 RRVFENGHRYPTHtTYTEDMALWFALIDAGFKLGNVDKVLLDYR 208
Cdd:cd04195   159 KSKVLAVGGYQDL-PLVEDYALWARMLANGARFANLPEILVKAR 201
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
7-208 6.20e-49

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 160.56  E-value: 6.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   7 VIMSIYKSDDPEALRVALDSLINQTYPCD-IFVYQDGEIPLALTSVIQDYVDNRQIKLTSCLVNKGLAHGLNTLINEVlq 85
Cdd:cd04195     2 VLMSVYIKEKPEFLREALESILKQTLPPDeVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHC-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  86 gDYIYIARMDSDDISRPERMFEQVSYLEKNPQIDICGTFCQEFGSTYA-LTEKRLPKAHEDLVKFSIARCPFIHPTVMFR 164
Cdd:cd04195    80 -TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNdIGKRRLPTSHDDILKFARRRSPFNHPTVMFR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2588820556 165 RRVFENGHRYPTHtTYTEDMALWFALIDAGFKLGNVDKVLLDYR 208
Cdd:cd04195   159 KSKVLAVGGYQDL-PLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
4-221 1.28e-15

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 73.58  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   4 KLAVIMSIYksDDPEALRVALDSLINQTYP-CDIFVYQDGeiplaltS------VIQDYV-DNRQIKLTSCLVNKGLAHG 75
Cdd:COG0463     3 LVSVVIPTY--NEEEYLEEALESLLAQTYPdFEIIVVDDG-------StdgtaeILRELAaKDPRIRVIRLERNRGKGAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  76 LNTLINEVlQGDYIyiARMDSDDISRPERMFEQVSYLEKNPQIDICGTFCQEFGSTYAlteKRLPKAHEDLVKFSIARCP 155
Cdd:COG0463    74 RNAGLAAA-RGDYI--AFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDL---RRLGSRLFNLVRLLTNLPD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2588820556 156 FIHPTVMFRRRVFengHRYPTHTTYTEDMALwFALIDAGFKLGNVDKvllDYRLTEDTILRRRGFK 221
Cdd:COG0463   148 STSGFRLFRREVL---EELGFDEGFLEDTEL-LRALRHGFRIAEVPV---RYRAGESKLNLRDLLR 206
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-169 5.82e-09

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 53.94  E-value: 5.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   7 VIMSIYKSddPEALRVALDSLINQTYP-CDIFVYQDGEiPLALTSVIQDYVDNR-QIKLTSCLVNKGLAHGLNTLINEVl 84
Cdd:pfam00535   2 VIIPTYNE--EKYLLETLESLLNQTYPnFEIIVVDDGS-TDGTVEIAEEYAKKDpRVRVIRLPENRGKAGARNAGLRAA- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  85 QGDYIyiARMDSDDISRPERMFEQVSYLEKNP------QIDICGTFCQEFGSTYALTEKRLPKAHEDLVKFSIARCpFIH 158
Cdd:pfam00535  78 TGDYI--AFLDADDEVPPDWLEKLVEALEEDGadvvvgSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPF-LIG 154
                         170
                  ....*....|.
gi 2588820556 159 PTVMFRRRVFE 169
Cdd:pfam00535 155 GFALYRREALE 165
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
7-208 6.20e-49

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 160.56  E-value: 6.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   7 VIMSIYKSDDPEALRVALDSLINQTYPCD-IFVYQDGEIPLALTSVIQDYVDNRQIKLTSCLVNKGLAHGLNTLINEVlq 85
Cdd:cd04195     2 VLMSVYIKEKPEFLREALESILKQTLPPDeVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHC-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  86 gDYIYIARMDSDDISRPERMFEQVSYLEKNPQIDICGTFCQEFGSTYA-LTEKRLPKAHEDLVKFSIARCPFIHPTVMFR 164
Cdd:cd04195    80 -TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNdIGKRRLPTSHDDILKFARRRSPFNHPTVMFR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2588820556 165 RRVFENGHRYPTHtTYTEDMALWFALIDAGFKLGNVDKVLLDYR 208
Cdd:cd04195   159 KSKVLAVGGYQDL-PLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
4-221 1.28e-15

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 73.58  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   4 KLAVIMSIYksDDPEALRVALDSLINQTYP-CDIFVYQDGeiplaltS------VIQDYV-DNRQIKLTSCLVNKGLAHG 75
Cdd:COG0463     3 LVSVVIPTY--NEEEYLEEALESLLAQTYPdFEIIVVDDG-------StdgtaeILRELAaKDPRIRVIRLERNRGKGAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  76 LNTLINEVlQGDYIyiARMDSDDISRPERMFEQVSYLEKNPQIDICGTFCQEFGSTYAlteKRLPKAHEDLVKFSIARCP 155
Cdd:COG0463    74 RNAGLAAA-RGDYI--AFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDL---RRLGSRLFNLVRLLTNLPD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2588820556 156 FIHPTVMFRRRVFengHRYPTHTTYTEDMALwFALIDAGFKLGNVDKvllDYRLTEDTILRRRGFK 221
Cdd:COG0463   148 STSGFRLFRREVL---EELGFDEGFLEDTEL-LRALRHGFRIAEVPV---RYRAGESKLNLRDLLR 206
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-266 2.05e-15

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 74.39  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   4 KLAVIMSIYksDDPEALRVALDSLINQTYPCD---IFVYQDGEIPlALTSVIQDYVD-NRQIKLTSCLVNKGLAHGLNTL 79
Cdd:COG1215    30 RVSVIIPAY--NEEAVIEETLRSLLAQDYPKEkleVIVVDDGSTD-ETAEIARELAAeYPRVRVIERPENGGKAAALNAG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  80 INEVlQGDYIyiARMDSDDISRPERMFEQVSYLEkNPQIDICGTFCqefgstyaltekrlpkahedlvkfsiarcpfihp 159
Cdd:COG1215   107 LKAA-RGDIV--VFLDADTVLDPDWLRRLVAAFA-DPGVGASGANL---------------------------------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556 160 tvMFRRRVFENGHRYPTHtTYTEDMALWFALIDAGFKLGNVDKVLLDYRLTEDT---ILRRRGFKKSISEVKLRVKYMMR 236
Cdd:COG1215   149 --AFRREALEEVGGFDED-TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLralFRQRRRWARGGLQLLLKHRPLLR 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 2588820556 237 LKMLTLKNVMLITSRVIFHLLPVSFMRFMY 266
Cdd:COG1215   226 PRRLLLFLLLLLLPLLLLLLLLALLALLLL 255
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-208 2.75e-11

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 61.49  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   6 AVIMSIYksdDPEA-LRVALDSLINQTYPCD-IFVYQDG------EIplaltsvIQDYVDN--RQIKLTSCLVNKGLAHG 75
Cdd:cd04196     1 AVLMATY---NGEKyLREQLDSILAQTYKNDeLIISDDGstdgtvEI-------IKEYIDKdpFIIILIRNGKNLGVARN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  76 LNTLINEVlQGDYIYIArmDSDDISRPERMFEQVSYLEKNPQID-ICG--TFCQEFG-----STYALTEKRLPKAHEDLV 147
Cdd:cd04196    71 FESLLQAA-DGDYVFFC--DQDDIWLPDKLERLLKAFLKDDKPLlVYSdlELVDENGnpigeSFFEYQKIKPGTSFNNLL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2588820556 148 KFSIAR-CpfihpTVMFRRRVFENGHRYPTHTTYTEDMALWfALIDAGFKLGNVDKVLLDYR 208
Cdd:cd04196   148 FQNVVTgC-----TMAFNRELLELALPFPDADVIMHDWWLA-LLASAFGKVVFLDEPLILYR 203
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
7-196 1.60e-09

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 55.59  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   7 VIMSIYksDDPEALRVALDSLINQTYP-CDIFVYQDGEIPLALTSVIQDYVDNRQIKLTSCLVNKGLAHGLNTLInEVLQ 85
Cdd:cd00761     1 VIIPAY--NEEPYLERCLESLLAQTYPnFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGL-KAAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  86 GDYIyiARMDSDDISRPERMFEQVSYLEKNPQIDICGTFCqefgstyaltekrlpkahedlvkfsiarcpfihpTVMFRR 165
Cdd:cd00761    78 GEYI--LFLDADDLLLPDWLERLVAELLADPEADAVGGPG----------------------------------NLLFRR 121
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2588820556 166 RVF-ENGHRYPTHTTYTEDMALWFALIDAGFK 196
Cdd:cd00761   122 ELLeEIGGFDEALLSGEEDDDFLLRLLRGGKV 153
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-169 5.82e-09

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 53.94  E-value: 5.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   7 VIMSIYKSddPEALRVALDSLINQTYP-CDIFVYQDGEiPLALTSVIQDYVDNR-QIKLTSCLVNKGLAHGLNTLINEVl 84
Cdd:pfam00535   2 VIIPTYNE--EKYLLETLESLLNQTYPnFEIIVVDDGS-TDGTVEIAEEYAKKDpRVRVIRLPENRGKAGARNAGLRAA- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  85 QGDYIyiARMDSDDISRPERMFEQVSYLEKNP------QIDICGTFCQEFGSTYALTEKRLPKAHEDLVKFSIARCpFIH 158
Cdd:pfam00535  78 TGDYI--AFLDADDEVPPDWLEKLVEALEEDGadvvvgSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPF-LIG 154
                         170
                  ....*....|.
gi 2588820556 159 PTVMFRRRVFE 169
Cdd:pfam00535 155 GFALYRREALE 165
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
4-120 6.35e-09

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 54.52  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   4 KLAVIMSIYKSDdPEALRVALDSLINQTYPC-DIFVYQDGEIPLALTSVIQDY-VDNRQIKLTSCLVNKGLAHGLNTLIn 81
Cdd:cd04184     2 LISIVMPVYNTP-EKYLREAIESVRAQTYPNwELCIADDASTDPEVKRVLKKYaAQDPRIKVVFREENGGISAATNSAL- 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2588820556  82 EVLQGDYIyiARMDSDDISRPERMFEQVSYLEKNPQIDI 120
Cdd:cd04184    80 ELATGEFV--ALLDHDDELAPHALYEVVKALNEHPDADL 116
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
24-213 1.36e-08

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 53.70  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  24 LDSLINQTYPcDI-FVYQDG-------EIplaltsvIQDYVDNRqikltSCLV-----------NKGLAHGlntlinevl 84
Cdd:cd06433    17 IDSVLSQTYP-NIeYIVIDGgstdgtvDI-------IKKYEDKI-----TYWIsepdkgiydamNKGIALA--------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556  85 QGDYIYIarMDSDDISRPERMFEQVSYLEKNPQIDICGTFCQEFGSTYALTEKRLPKAHEDLVKFsiARCPFIHPTVMFR 164
Cdd:cd06433    75 TGDIIGF--LNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLL--YGMPICHQATFFR 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2588820556 165 RRVFENGHRYPTHTTYTEDMALWFALIDAGFKLGNVDKVLLDYRLTEDT 213
Cdd:cd06433   151 RSLFEKYGGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVS 199
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-99 1.74e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 41.52  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   1 MTGKLAVIMSIYksDDPEALRVALDSLINQTY-PCDIFVYQDGEIPLALTSVIQdyVDNRQIKLTSCLVNKGLAHGLNTL 79
Cdd:COG1216     1 MRPKVSVVIPTY--NRPELLRRCLESLLAQTYpPFEVIVVDNGSTDGTAELLAA--LAFPRVRVIRNPENLGFAAARNLG 76
                          90       100
                  ....*....|....*....|
gi 2588820556  80 INEVlQGDYIYIarMDSDDI 99
Cdd:COG1216    77 LRAA-GGDYLLF--LDDDTV 93
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
6-118 7.01e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 36.88  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588820556   6 AVIMSiYKsDDPEALRVALDSLINQTYPcdIFVYQDGEIPlalTSVIQDYVDNRQIKLTSCLVNKGLAHGLNTLINEVLQ 85
Cdd:cd02526     1 AVVVT-YN-PDLSKLKELLAALAEQVDK--VVVVDNSSGN---DIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALE 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2588820556  86 GDYIYIARMDSDdiSRP-----ERMFEQVSYLEKNPQI 118
Cdd:cd02526    74 NGADYVLLFDQD--SVPppdmvEKLLAYKILSDKNSNI 109
 
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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