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Conserved domains on  [gi|2236564873|ref|WP_248616868|]
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glycosyltransferase [Porphyromonas catoniae]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

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
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 78-390 1.52e-49

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03820:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 351  Bit Score: 170.88  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873  78 ILRESKargIQVVIIPIALPNDQLAYLRsAGLRLIYWCHSSPLWELIDRRERAGykphhpwhkniysllirrtrrllvpd 157
Cdd:cd03820    82 YLKNNK---PDVVISFRTSLLTFLALIG-LKSKLIVWEHNNYEAYNKGLRRLLL-------------------------- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 158 RARLIKWYqhlvsevDCFITLAPGYIKIFadslglSEEEQKKFVSLPNMVrPPKGEVTLLDRP-KKIIFMGRLSYaDKRA 236
Cdd:cd03820   132 RRLLYKRA-------DKIVVLTEADKLKK------YKQPNSNVVVIPNPL-SFPSEEPSTNLKsKRILAVGRLTY-QKGF 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 237 DRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQ 315
Cdd:cd03820   197 DLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEdRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAM 276

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2236564873 316 SYGVVPIAFGCSDGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYFPERNIPRWQ 390
Cdd:cd03820   277 AYGLPIISFDCPTGPSEIIEDGE-NGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWE 350
 
Name Accession Description Interval E-value
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 78-390 1.52e-49

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 170.88  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873  78 ILRESKargIQVVIIPIALPNDQLAYLRsAGLRLIYWCHSSPLWELIDRRERAGykphhpwhkniysllirrtrrllvpd 157
Cdd:cd03820    82 YLKNNK---PDVVISFRTSLLTFLALIG-LKSKLIVWEHNNYEAYNKGLRRLLL-------------------------- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 158 RARLIKWYqhlvsevDCFITLAPGYIKIFadslglSEEEQKKFVSLPNMVrPPKGEVTLLDRP-KKIIFMGRLSYaDKRA 236
Cdd:cd03820   132 RRLLYKRA-------DKIVVLTEADKLKK------YKQPNSNVVVIPNPL-SFPSEEPSTNLKsKRILAVGRLTY-QKGF 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 237 DRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQ 315
Cdd:cd03820   197 DLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEdRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAM 276

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2236564873 316 SYGVVPIAFGCSDGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYFPERNIPRWQ 390
Cdd:cd03820   277 AYGLPIISFDCPTGPSEIIEDGE-NGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWE 350
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 220-373 1.14e-23

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 96.19  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 220 PKKIIFMGRLSYaDKRADRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLI--YPQSS 296
Cdd:pfam00534   2 KKIILFVGRLEP-EKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPelLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2236564873 297 VLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSdGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEAS 373
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVG-GPPEVVKDGET-GFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 291-396 5.43e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.57  E-value: 5.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 291 IYPQSSVLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSdGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLA 370
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGE-TGLLVPPGDPEALAEAILRLLEDPELRRRLG 94

                          90       100
                  ....*....|....*....|....*..
gi 2236564873 371 EASMRRVEEYF-PERNIPRWQGIFDQL 396
Cdd:COG0438    95 EAARERAEERFsWEAIAERLLALYEEL 121
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
218-356 1.91e-12

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 67.81  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 218 DRPKKIIFMGRL-SYADKRADRLIYIWEQIHrelPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLIYPQS 295
Cdd:PRK09922  178 DKPAVFLYVGRLkFEGQKNVKELFDGLSQTT---GEWQLHIIGDGSDFEKCKAYSRELGIEqRIIWHGWQSQPWEVVQQK 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2236564873 296 ----SVLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSDGVKEIIGTGEQyGRLVTPFDLDEYATKL 356
Cdd:PRK09922  255 iknvSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGLN-GELYTPGNIDEFVGKL 318
 
Name Accession Description Interval E-value
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 78-390 1.52e-49

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 170.88  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873  78 ILRESKargIQVVIIPIALPNDQLAYLRsAGLRLIYWCHSSPLWELIDRRERAGykphhpwhkniysllirrtrrllvpd 157
Cdd:cd03820    82 YLKNNK---PDVVISFRTSLLTFLALIG-LKSKLIVWEHNNYEAYNKGLRRLLL-------------------------- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 158 RARLIKWYqhlvsevDCFITLAPGYIKIFadslglSEEEQKKFVSLPNMVrPPKGEVTLLDRP-KKIIFMGRLSYaDKRA 236
Cdd:cd03820   132 RRLLYKRA-------DKIVVLTEADKLKK------YKQPNSNVVVIPNPL-SFPSEEPSTNLKsKRILAVGRLTY-QKGF 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 237 DRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQ 315
Cdd:cd03820   197 DLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEdRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAM 276

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2236564873 316 SYGVVPIAFGCSDGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYFPERNIPRWQ 390
Cdd:cd03820   277 AYGLPIISFDCPTGPSEIIEDGE-NGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWE 350
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 180-389 9.33e-30

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 117.02  E-value: 9.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 180 PGYIKIFADSLGLSEEEQKKFVSLPNmvrppkgevtlldRPKKIIFMGRLSyADKRADRLIYIWEQIHRELPEWSVEIYG 259
Cdd:cd04949   133 NKYPPIFTIPVGYVDQLDTAESNHER-------------KSNKIITISRLA-PEKQLDHLIEAVAKAVKKVPEITLDIYG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 260 QGKEEKYLRALIEDKQLPR-ISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSDGVKEIIGTGE 338
Cdd:cd04949   199 YGEEREKLKKLIEELHLEDnVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSELIEDGE 278

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2236564873 339 QyGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYFPERNIPRW 389
Cdd:cd04949   279 N-GYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYSTENVMEKW 328
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 8-381 1.97e-28

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 113.99  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873   8 VAIVHRRLALGGAEEVSRETSLIFRQMGICTHFF---AEEHRAEEWVLPTCPEISLTLFPEGVRLWTRESADVILRESKA 84
Cdd:cd03811     2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVllrDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873  85 RGIQVVIIPIALPNDQLAYLRSAGLRLIYWCHSSPLWELIDRRERAgykphhpWHKNIYSLlirrtrrllvpdrarlikw 164
Cdd:cd03811    82 AKPDVVISFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLL-------LKLKLYKK------------------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 165 yqhlvseVDCFITLAPGYIKIFADSLGLSEEeqkKFVSLPNMVRPP-------KGEVTLLDRPKKIIFMGRLSYaDKRAD 237
Cdd:cd03811   136 -------ADKIVCVSKGIKEDLIRLGPSPPE---KIEVIYNPIDIDriralakEPILNEPEDGPVILAVGRLDP-QKGHD 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 238 RLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQL-PRISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQS 316
Cdd:cd03811   205 LLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLaERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMA 284

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2236564873 317 YGVVPIAFGCsDGVKEIIGTGEqYGRLVTPFDLDEYATKLREL---CLREELRQSLAEASMRRVEEYF 381
Cdd:cd03811   285 LGTPVVSTDC-PGPREILDDGE-NGLLVPDGDAAALAGILAALlqkKLDAALRERLAKAQEAVFREYT 350
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 7-393 2.41e-24

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 103.00  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873   7 HVAIVHRRL--ALGGAEEVSRETSLIFRQMGICTHFFAEEHRAEEWVLPTCPEISLTLFPEGVRLWTRESADVILRESKA 84
Cdd:cd03801     1 KILLLSPELppPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873  85 RGIQVVIIP-IALPNDQLAYLRSAGLRLIYWCHSSPLWELIDRRERagykphhpwhkniysllirrtrrllvpdRARLIK 163
Cdd:cd03801    81 RKFDVVHAHgLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAA----------------------------ERRLLA 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 164 WYQHLVSEVDCFITLAPGYIKIFADSLGLSEEeqkKFVSLPNMV------RPPKGEVTLLDRPKKIIFMGRLSyADKRAD 237
Cdd:cd03801   133 RAEALLRRADAVIAVSEALRDELRALGGIPPE---KIVVIPNGVdlerfsPPLRRKLGIPPDRPVLLFVGRLS-PRKGVD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 238 RLIYIWEQIHRELPEWSVEIYGQ-GKEEKYLRALIEDKQlPRISLRGYAPDPSL--IYPQSSVLAMTSTYEGWGLVLTEA 314
Cdd:cd03801   209 LLLEALAKLLRRGPDVRLVIVGGdGPLRAELEELELGLG-DRVRFLGFVPDEELpaLYAAADVFVLPSRYEGFGLVVLEA 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 315 QSYGVVPIAFgCSDGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYF-PERNIPRWQGIF 393
Cdd:cd03801   288 MAAGLPVVAT-DVGGLPEVVEDGE-GGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFsWERVAERLLDLY 365
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 220-373 1.14e-23

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 96.19  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 220 PKKIIFMGRLSYaDKRADRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLI--YPQSS 296
Cdd:pfam00534   2 KKIILFVGRLEP-EKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPelLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2236564873 297 VLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSdGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEAS 373
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVG-GPPEVVKDGET-GFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
220-359 1.60e-22

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 92.19  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 220 PKKIIFMGRLSYADKRADRLIYIWEQIHRELPEWSVEIYGQGKEEKyLRALIEDKQlPRISLRGYAPDPSLIYPQSSVLA 299
Cdd:pfam13692   1 RPVILFVGRLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLE-DRVIFTGFVEDLAELLAAADVFV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 300 MTSTYEGWGLVLTEAQSYGVVPIAFGCsDGVKEIIgTGEQyGRLVTPFDLDEYATKLREL 359
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGLPVVATDV-GGIPELV-DGEN-GLLVPPGDPEALAEAILRL 135
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 291-396 5.43e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.57  E-value: 5.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 291 IYPQSSVLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSdGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLA 370
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGE-TGLLVPPGDPEALAEAILRLLEDPELRRRLG 94

                          90       100
                  ....*....|....*....|....*..
gi 2236564873 371 EASMRRVEEYF-PERNIPRWQGIFDQL 396
Cdd:COG0438    95 EAARERAEERFsWEAIAERLLALYEEL 121
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 218-389 1.20e-16

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 80.50  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 218 DRPKKIIFMGRLsYADKRADRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQL-PRISLRGYAP--DPSLIYPQ 294
Cdd:cd03798   198 LDAFVILFVGRL-IPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLgDRVTFTGRLPheQVPAYYRA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 295 SSVLAMTSTYEGWGLVLTEAQSYGVVPIAFGCsDGVKEIIGTGEqYGRLVTPFDLDEYATKLRELCLREELRQSLAEASM 374
Cdd:cd03798   277 CDVFVLPSRHEGFGLVLLEAMACGLPVVATDV-GGIPEVVGDPE-TGLLVPPGDADALAAALRRALAEPYLRELGEAARA 354

                         170
                  ....*....|....*
gi 2236564873 375 RRVEEYFPERNIPRW 389
Cdd:cd03798   355 RVAERFSWVKAADRI 369
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 173-386 9.15e-15

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 74.94  E-value: 9.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 173 DCFITLAPGYIKIFADSLGLSEEeqKKFVSLPNMV----RPPKGEVTLLDRPKkIIFMGRLSYaDKRADRLIYIWEQIHR 248
Cdd:cd03808   141 DKVIFVNEDDRDLAIKKGIIKKK--KTVLIPGSGVdldrFQYSPESLPSEKVV-FLFVARLLK-DKGIDELIEAAKILKK 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 249 ELPEWSVEIYGQGKEEKYLRALIEDKQL-PRISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQSYGVVPIAfgcS 327
Cdd:cd03808   217 KGPNVRFLLVGDGELENPSEILIEKLGLeGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVIT---T 293

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2236564873 328 D--GVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYFPERNI 386
Cdd:cd03808   294 DvpGCRELVIDGVN-GFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKV 353
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 223-381 1.56e-14

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 74.28  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 223 IIFMGRLsYADKRADRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLIYPQSSVLAMT 301
Cdd:cd03807   193 IGIVGRL-HPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEdRVHLLGERSDVPALLPAMDIFVLS 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 302 STYEGWGLVLTEAQSYGVVPIAfgcSD--GVKEIIGTGEqyGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEE 379
Cdd:cd03807   272 SRTEGFPNALLEAMACGLPVVA---TDvgGAAELVDDGT--GFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIAN 346


                  ..
gi 2236564873 380 YF 381
Cdd:cd03807   347 EF 348
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 234-380 3.43e-13

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 70.08  E-value: 3.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 234 KRADRLIYIWEQIHRELPEWSVEIYG-QGKEEKYLRALIEDKQL-PRISLRGYAPDPSLI--YPQSSVLAMTSTYEGWGL 309
Cdd:cd03809   205 KNHERLLKAFALLKKQGGDLKLVIVGgKGWEDEELLDLVKKLGLgGRVRFLGYVSDEDLPalYRGARAFVFPSLYEGFGL 284

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2236564873 310 VLTEAQSYGvVPIAfgCSDG--VKEIIGtgeQYGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEY 380
Cdd:cd03809   285 PVLEAMACG-TPVI--ASNIsvLPEVAG---DAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKF 351
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
218-356 1.91e-12

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 67.81  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 218 DRPKKIIFMGRL-SYADKRADRLIYIWEQIHrelPEWSVEIYGQGKEEKYLRALIEDKQLP-RISLRGYAPDPSLIYPQS 295
Cdd:PRK09922  178 DKPAVFLYVGRLkFEGQKNVKELFDGLSQTT---GEWQLHIIGDGSDFEKCKAYSRELGIEqRIIWHGWQSQPWEVVQQK 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2236564873 296 ----SVLAMTSTYEGWGLVLTEAQSYGVVPIAFGCSDGVKEIIGTGEQyGRLVTPFDLDEYATKL 356
Cdd:PRK09922  255 iknvSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGLN-GELYTPGNIDEFVGKL 318
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 194-381 2.74e-12

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 67.30  E-value: 2.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 194 EEEQKKFVSLP---NMVRPPKGEVTLL------DRPKKIIFMGRLSYAdKRADRLIYIwEQIHRelpeWSVEIYGQGKEE 264
Cdd:cd03795   156 REFKNKVRVIPlgiDKNVYNIPRVDFEnikrekKGKKIFLFIGRLVYY-KGLDYLIEA-AQYLN----YPIVIGGEGPLK 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 265 KYLRALIEDKQLPRISLRGYAPDPSLI--YPQSSVLAMTSTY--EGWGLVLTEAQSYGVvPIafgcsdgVKEIIGTGEQY 340
Cdd:cd03795   230 PDLEAQIELNLLDNVKFLGRVDDEEKViyLHLCDVFVFPSVLrsEAFGIVLLEAMMCGK-PV-------ISTNIGTGVPY 301

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2236564873 341 -------GRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYF 381
Cdd:cd03795   302 vnnngetGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELF 349
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 197-380 4.82e-12

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 66.92  E-value: 4.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 197 QKKFVSLPNMV------RPPKGEV----TLLDRPKKIIFMGRLSYaDKRADRLIYIWEQIHRElPEWSVEIYGQGKEEKY 266
Cdd:cd03817   168 KGPIEVIPNGIdldkfeKPLNTEErrklGLPPDEPILLYVGRLAK-EKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 267 LRALIEDKQLP-RISLRGYAPDPSLI--YPQSSVLAMTSTYEGWGLVLTEAQSYGvVPIAFGCSDGVKEIIGTGEQyGRL 343
Cdd:cd03817   246 LKELARELGLAdKVIFTGFVPREELPeyYKAADLFVFASTTETQGLVYLEAMAAG-LPVVAAKDPAASELVEDGEN-GFL 323

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2236564873 344 VTPFDlDEYATKLRELCLREELRQSLAEASMRRVEEY 380
Cdd:cd03817   324 FEPND-ETLAEKLLHLRENLELLRKLSKNAEISAREF 359
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 224-343 1.02e-11

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 64.35  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 224 IFMGRLSYaDKRADRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDKQL----PRISLRGYAPDPSLIYPQSSVLA 299
Cdd:cd01635   114 VSVGRLVP-EKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLlervVIIGGLVDDEVLELLLAAADVFV 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2236564873 300 MTSTYEGWGLVLTEAQSYGVVPIAFGCSdGVKEIIGTGEQYGRL 343
Cdd:cd01635   193 LPSRSEGFGLVLLEAMAAGKPVIATDVG-GIPEFVVDGENGLLV 235
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 188-379 1.02e-11

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 65.45  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 188 DSLGLSEEeqkKFVSLPNMVRPPK-------GEVTLL---DRPKKIIFMGRLSyADKRADRLIYIWEQIHRELPeWSVEI 257
Cdd:cd03819   143 EALGVDPE---RIRVIPNGVDTDRfppeaeaEERAQLglpEGKPVVGYVGRLS-PEKGWLLLVDAAAELKDEPD-FRLLV 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 258 YGQGKEEKYLRALIEDKQL-PRISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQSYG--VVPIAFGcsdGVKEII 334
Cdd:cd03819   218 AGDGPERDEIRRLVERLGLrDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGtpVVATDVG---GAREIV 294

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2236564873 335 GTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEASM--RRVEE 379
Cdd:cd03819   295 VHGRT-GLLVPPGDAEALADAIRAAKLLPEAREKLQAAAAltEAVRE 340
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 198-380 1.05e-09

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 59.65  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 198 KKFVSLPNMVRP---PKGEVTLLDRPKKIIFMGRLSYAdKRADRLIYIWEQIHRelPEWSVEIYGQGKEEKYLRALIEdk 274
Cdd:cd03823   166 ARISVIPNAVEPdlaPPPRRRPGTERLRFGYIGRLTEE-KGIDLLVEAFKRLPR--EDIELVIAGHGPLSDERQIEGG-- 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 275 qlPRISLRGYAP--DPSLIYPQSSVLAMTST-YEGWGLVLTEAQSYGVVPIAfgcSD--GVKEIIGTGEQyGRLVTPFDL 349
Cdd:cd03823   241 --RRIAFLGRVPtdDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIA---SDlgGIAELIQPGVN-GLLFAPGDA 314

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2236564873 350 DEYATKLRELCLREELRQSLA------EASMRRVEEY 380
Cdd:cd03823   315 EDLAAAMRRLLTDPALLERLRagaeppRSTESQAEEY 351
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 219-380 1.44e-09

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 59.34  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 219 RPKK--IIFMGRLSyADKRADRLIYIWEQihreLPEWSVEIYGQGKEEKYLRALIEDkqLPRI---SLRGyaPDPSLIYP 293
Cdd:PLN02871  260 EPEKplIVYVGRLG-AEKNLDFLKRVMER----LPGARLAFVGDGPYREELEKMFAG--TPTVftgMLQG--DELSQAYA 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 294 QSSVLAMTSTYEGWGLVLTEAQSYGVvPIAFGCSDGVKEIIgTGEQYGR---LVTPFDLDEYATKLRELCLREELRQSLA 370
Cdd:PLN02871  331 SGDVFVMPSESETLGFVVLEAMASGV-PVVAARAGGIPDII-PPDQEGKtgfLYTPGDVDDCVEKLETLLADPELRERMG 408

                         170
                  ....*....|
gi 2236564873 371 EASMRRVEEY 380
Cdd:PLN02871  409 AAAREEVEKW 418
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 291-396 1.49e-09

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 59.18  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 291 IYPQSSVLAMTSTYEGWGLVLTEAQSYGVvPIAFGCSDGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLA 370
Cdd:cd03800   299 LYRAADVFVVPSLYEPFGLTAIEAMACGT-PVVATAVGGLQDIVRDGRT-GLLVDPHDPEALAAALRRLLDDPALWQRLS 376

                          90       100
                  ....*....|....*....|....*.
gi 2236564873 371 EASMRRVEEYFpernipRWQGIFDQL 396
Cdd:cd03800   377 RAGLERARAHY------TWESVADQL 396
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 234-396 6.60e-09

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 56.98  E-value: 6.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 234 KRADRLIYIWEQIHRELPEWSVEIyGQGKE----EKYLRAL-IEDkqlpRISLRGYAPDPSLIYPQSSVLAMTSTYEGWG 308
Cdd:cd04962   209 KRIDDVVRVFARVRRKIPAKLLLV-GDGPErvpaEELARELgVED----RVLFLGKQDDVEELLSIADLFLLPSEKESFG 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 309 LVLTEAQSYGVVPIAFGcSDGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEASMRRVEEYF-PERNIP 387
Cdd:cd04962   284 LAALEAMACGVPVVSSN-AGGIPEVVKHGET-GFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFdPERIVP 361


                  ....*....
gi 2236564873 388 RWQGIFDQL 396
Cdd:cd04962   362 QYEAYYRRL 370
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 217-386 5.77e-08

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 54.26  E-value: 5.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 217 LDRPKKIIFMGRLSYADKRADrLIYIWEQIHRELPEWSVEIYGQGKeekyLRALIEDKQLPRISLrGYAPDPS---LIYP 293
Cdd:cd03825   189 IPQDKKVILFGAESVTKPRKG-FDELIEALKLLATKDDLLLVVFGK----NDPQIVILPFDIISL-GYIDDDEqlvDIYS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 294 QSSVLAMTSTYEGWGLVLTEAQSYGVVPIAFGcSDGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEAS 373
Cdd:cd03825   263 AADLFVHPSLADNLPNTLLEAMACGTPVVAFD-TGGSPEIVQHGVT-GYLVPPGDVQALAEAIEWLLANPKERESLGERA 340

                         170
                  ....*....|...
gi 2236564873 374 MRRVEEYFPERNI 386
Cdd:cd03825   341 RALAENHFDQRVQ 353
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 291-394 1.04e-07

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 53.49  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 291 IYPQSSVLAMTSTYEGWGLVLTEAQSYGVVPIAfgcSD--GVKEII-GTGEQYGR---LVTPFDLDEYATKLRELCLREE 364
Cdd:cd03813   367 YYPKLGLLVLTSISEGQPLVILEAMASGVPVVA---TDvgSCRELIyGADDALGQaglVVPPADPEALAEALIKLLRDPE 443

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2236564873 365 LRQSLAEASMRRVEEYFP-ERNIPRWQGIFD 394
Cdd:cd03813   444 LRQAFGEAGRKRVEKYYTlEGMIDSYRKLYL 474
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 218-396 2.00e-07

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 52.30  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 218 DRPKkIIFMGRLSyADKRADRLIYIWEQIHRELPEWSVeIYGQGKEEKYLRAliedkQLPRISLRGYAPDPSL--IYPQS 295
Cdd:cd03814   197 GRPL-LLYVGRLA-PEKNLEALLDADLPLAASPPVRLV-VVGDGPARAELEA-----RGPDVIFTGFLTGEELarAYASA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 296 SVLAMTSTYEGWGLVLTEAQSYGVVPIAFGcSDGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSLAEASMR 375
Cdd:cd03814   269 DVFVFPSRTETFGLVVLEAMASGLPVVAAD-AGGPRDIVRPGGT-GALVEPGDAAAFAAALRALLEDPELRRRMAARARA 346

                         170       180
                  ....*....|....*....|.
gi 2236564873 376 RVEEYfpernipRWQGIFDQL 396
Cdd:cd03814   347 EAERY-------SWEAFLDNL 360
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 219-394 1.04e-06

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 50.14  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 219 RPKKIIFMGRLsyADKRA-DRLIYIWEQIHRELPEWSVEIYGQGKEEKYLRALIEDkqLPRISLRGYAPDPSL------- 290
Cdd:cd05844   188 RAPTILFVGRL--VEKKGcDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAA--LGRVRFLGALPHAEVqdwmrra 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 291 -IYPQSSVLAMTSTYEGWGLVLTEAQSYGvVPIAFGCSDGVKEIIGTGEQyGRLVTPFDLDEYATKLRELCLREELRQSL 369
Cdd:cd05844   264 eIFCLPSVTAASGDSEGLGIVLLEAAACG-VPVVSSRHGGIPEAILDGET-GFLVPEGDVDALADALQALLADRALADRM 341

                         170       180
                  ....*....|....*....|....*
gi 2236564873 370 AEASMRRVEEYFperNIPRWQGIFD 394
Cdd:cd05844   342 GGAARAFVCEQF---DIRVQTAKLE 363
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 192-369 2.19e-06

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 49.21  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 192 LSEEEQKKFVSLPNMV-----------RPPKGEVTLLDRPKKIIFMGRLSYAdKRADRLIYIWEQIHRELPEWSVEIYGQ 260
Cdd:cd03812   152 FGEVENGKFKVIPNGIdiekykfnkekRRKRRKLLILEDKLVLGHVGRFNEQ-KNHSFLIDIFEELKKKNPNVKLVLVGE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 261 GKEEKYLRALIEDKQL-PRISLRGYAPDPSLIYPQSSVLAMTSTYEGWGLVLTEAQSYGVVPIafgcsdgVKEIIGTGEQ 339
Cdd:cd03812   231 GELKEKIKEKVKELGLeDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL-------LSDTITKECD 303

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2236564873 340 YGRLVTPFDLDE----YATKLRELCLREELRQSL 369
Cdd:cd03812   304 ITNNVEFLPLNEtpstWAEKILKLIKRKRRINKE 337
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 49-319 2.82e-05

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 45.82  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873  49 EWVLPTCPEISLTLFPEGVRLWTREsadvilresKARGIQVVII-----PIALPNDQLAylRSAGLRLIYWCHSS-PLWE 122
Cdd:cd03821    62 ASIPLLRQGAGRTDFSPGLPNWLRR---------NLREYDVVHIhgvwtYTSLAACKLA--RRRGIPYVVSPHGMlDPWA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 123 LidrreragykPHHPWHKNIYSLLIRrtrrllvpDRARLIKWYQHLVSEVDCFITLAPGY-IKIFADSLGLSEEEQKKFV 201
Cdd:cd03821   131 L----------QQKHWKKRIALHLIE--------RRNLNNAALVHFTSEQEADELRRFGLePPIAVIPNGVDIPEFDPGL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 202 SLPNMVRPPKGEvtlldrpKKIIFMGRLsYADKRADRLIYIWEQIHRELPEWSVEIYGQGK-EEKYLRALIEDKQL-PRI 279
Cdd:cd03821   193 RDRRKHNGLEDR-------RIILFLGRI-HPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDgAYPAFLQLQSSLGLgDRV 264

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2236564873 280 SLRGYAPDPSL--IYPQSSVLAMTSTYEGWGLVLTEAQSYGV 319
Cdd:cd03821   265 TFTGPLYGEAKwaLYASADLFVLPSYSENFGNVVAEALACGL 306
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 223-376 1.29e-04

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 44.09  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 223 IIFMGRLSYaDKRADRLIYIWEQIHRElpEWSVEIYGQGKE--EKYLRALiEDKQLPRISLR-GY-APDPSLIYPQSSVL 298
Cdd:cd03791   297 FGFVGRLTE-QKGVDLILDALPELLEE--GGQLVVLGSGDPeyEQAFREL-AERYPGKVAVViGFdEALAHRIYAGADFF 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 299 AMTSTYEGWGLVLTEAQSYGVVPIAF---GCSDGVKEIIG-TGEQYGRLVTPFDLDEYATKLR---ELCLREELRQSLAE 371
Cdd:cd03791   373 LMPSRFEPCGLVQMYAMRYGTLPIVRrtgGLADTVFDYDPeTGEGTGFVFEDYDAEALLAALRralALYRNPELWRKLQK 452


                  ....*
gi 2236564873 372 ASMRR 376
Cdd:cd03791   453 NAMKQ 457
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 225-346 9.76e-03

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 37.65  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236564873 225 FMGRLSyADKRADRLIYIWEQIHRELpewsvEIYGQGKEEKYLRALIEDKQLPRISLRGYAPDP---SLIYPQSSVLAMT 301
Cdd:cd03802   174 FLGRIA-PEKGLEDAIRVARRAGLPL-----KIAGKVRDEDYFYYLQEPLPGPRIEFIGEVGHDekqELLGGARALLFPI 247

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2236564873 302 STYEGWGLVLTEAQSYGVVPIAFGCSdGVKEIIGTGEQyGRLVTP 346
Cdd:cd03802   248 NWDEPFGLVMIEAMACGTPVIAYRRG-GLPEVIQHGET-GFLVDS 290
 
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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