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Conserved domains on  [gi|1277488664|gb|PIS75951|]
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glycosyl transferase [Escherichia coli O55:H7 str. USDA 5905]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
wcaI super family cl33229
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ...
1-407 0e+00

colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


The actual alignment was detected with superfamily member TIGR04007:

Pssm-ID: 188522 [Multi-domain]  Cd Length: 407  Bit Score: 871.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007   1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007  81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADVDVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400

                  ....*..
gi 1277488664 401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
 
Name Accession Description Interval E-value
wcaI TIGR04007
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ...
1-407 0e+00

colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


Pssm-ID: 188522 [Multi-domain]  Cd Length: 407  Bit Score: 871.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007   1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007  81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADVDVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400

                  ....*..
gi 1277488664 401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
1-407 0e+00

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 730.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKRE-EGAATVWRCPLYVPKQPS 79
Cdd:PRK10307    1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRREsEGGVTVWRCPLYVPKQPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  80 TLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMlglGLAGKGKGGKV 159
Cdd:PRK10307   81 GLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQDYEVDAA---FGLGLLKGGKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 160 AQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADVDVDALRNQLGLPDNKKIILYSGN 239
Cdd:PRK10307  158 ARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 240 IGEKQGLENVIEAADRLRDEP-LIFAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAAD 318
Cdd:PRK10307  238 IGEKQGLELVIDAARRLRDRPdLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 319 AVLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGI----RQALLLPKHNTVAREYAERTLDK 394
Cdd:PRK10307  318 LVLPSKLTNMLASGRNVVATAEPGTELGQLVE---GIGVCVEPESVEALVAAIaalaRQALLRPKLGTVAREYAERTLDK 394
                         410
                  ....*....|...
gi 1277488664 395 ENVLRQFINDIRG 407
Cdd:PRK10307  395 ENVLRQFIADIRG 407
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-402 5.49e-81

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 253.80  E-value: 5.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWqvgenYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03794     1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLG-----RIFAGATETKDGIRVIRVKLGPIKKNGLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  82 KRLLHLGSFAVSSFFPLMAqRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQ 161
Cdd:cd03794    76 RRLLNYLSFALAALLKLLV-REERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKLLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 162 LataFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQhvaDVDVDALRnQLGLPDNKKIILYSGNIG 241
Cdd:cd03794   155 K---LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFK---PPPKDELR-KKLGLDDKFVVVYAGNIG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 242 EKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAA-DA 319
Cdd:cd03794   228 KAQGLETLLEAAERLKRRPDIrFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPAnRG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 320 VLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGIRQALLlpkhNTV--------AREYAERT 391
Cdd:cd03794   308 SSPSKLFEYMAAGKPILASDDGGSDLAVEIN---GCGLVVEPGDPEALADAILELLD----DPElrramgenGRELAEEK 380
                         410
                  ....*....|.
gi 1277488664 392 LDKENVLRQFI 402
Cdd:cd03794   381 FSREKLADRLL 391
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
230-390 7.92e-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: 93.88  E-value: 7.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 230 NKKIILYSGNIGEKQGLENVIEAADRLR--DEPLIFAIVGQGGGKARLEKMAQQRGLHNMQFFPL-QSYDALPALLKMgd 306
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfVSDEDLPELLKI-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 307 CHLVVQKrgAADAVLPSKLTNILAVGGnAVITAEAHTELGQLCETFPGiaVCVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:pfam00534  79 ADVFVLP--SRYEGFGIVLLEAMACGL-PVIASDVGGPPEVVKDGETG--FLVKPNNAEALAEAIDKLLEDEELRERLGE 153

                  ....
gi 1277488664 387 YAER 390
Cdd:pfam00534 154 NARK 157
 
Name Accession Description Interval E-value
wcaI TIGR04007
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ...
1-407 0e+00

colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


Pssm-ID: 188522 [Multi-domain]  Cd Length: 407  Bit Score: 871.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007   1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007  81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADVDVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400

                  ....*..
gi 1277488664 401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
1-407 0e+00

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 730.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKRE-EGAATVWRCPLYVPKQPS 79
Cdd:PRK10307    1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRREsEGGVTVWRCPLYVPKQPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  80 TLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMlglGLAGKGKGGKV 159
Cdd:PRK10307   81 GLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQDYEVDAA---FGLGLLKGGKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 160 AQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADVDVDALRNQLGLPDNKKIILYSGN 239
Cdd:PRK10307  158 ARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 240 IGEKQGLENVIEAADRLRDEP-LIFAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAAD 318
Cdd:PRK10307  238 IGEKQGLELVIDAARRLRDRPdLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 319 AVLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGI----RQALLLPKHNTVAREYAERTLDK 394
Cdd:PRK10307  318 LVLPSKLTNMLASGRNVVATAEPGTELGQLVE---GIGVCVEPESVEALVAAIaalaRQALLRPKLGTVAREYAERTLDK 394
                         410
                  ....*....|...
gi 1277488664 395 ENVLRQFINDIRG 407
Cdd:PRK10307  395 ENVLRQFIADIRG 407
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-402 5.49e-81

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 253.80  E-value: 5.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWqvgenYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03794     1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLG-----RIFAGATETKDGIRVIRVKLGPIKKNGLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  82 KRLLHLGSFAVSSFFPLMAqRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQ 161
Cdd:cd03794    76 RRLLNYLSFALAALLKLLV-REERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKLLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 162 LataFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQhvaDVDVDALRnQLGLPDNKKIILYSGNIG 241
Cdd:cd03794   155 K---LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFK---PPPKDELR-KKLGLDDKFVVVYAGNIG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 242 EKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHLVVQKRGAA-DA 319
Cdd:cd03794   228 KAQGLETLLEAAERLKRRPDIrFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPAnRG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 320 VLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGIRQALLlpkhNTV--------AREYAERT 391
Cdd:cd03794   308 SSPSKLFEYMAAGKPILASDDGGSDLAVEIN---GCGLVVEPGDPEALADAILELLD----DPElrramgenGRELAEEK 380
                         410
                  ....*....|.
gi 1277488664 392 LDKENVLRQFI 402
Cdd:cd03794   381 FSREKLADRLL 391
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
230-390 7.92e-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: 93.88  E-value: 7.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 230 NKKIILYSGNIGEKQGLENVIEAADRLR--DEPLIFAIVGQGGGKARLEKMAQQRGLHNMQFFPL-QSYDALPALLKMgd 306
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfVSDEDLPELLKI-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 307 CHLVVQKrgAADAVLPSKLTNILAVGGnAVITAEAHTELGQLCETFPGiaVCVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:pfam00534  79 ADVFVLP--SRYEGFGIVLLEAMACGL-PVIASDVGGPPEVVKDGETG--FLVKPNNAEALAEAIDKLLEDEELRERLGE 153

                  ....
gi 1277488664 387 YAER 390
Cdd:pfam00534 154 NARK 157
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
15-204 5.07e-20

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 86.30  E-value: 5.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQvgenysawrykREEGAATVWRCPL-YVPKQPSTLKRLLHLGSFAvs 93
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPE-----------LVGDGVRVHRLPVpPRPSPLADLAALRRLRRLL-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  94 sffplmaqRRWKPDRIIGVVPTLFctPGMRLLAKLSGARTVLHIQDYEVDamlglglagkGKGGKVAQLATAFERSGLHN 173
Cdd:pfam13579  68 --------RAERPDVVHAHSPTAG--LAARLARRRRGVPLVVTVHGLALD----------YGSGWKRRLARALERRLLRR 127
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1277488664 174 VDNVSTISRSMMNKAIEKGVAAENVIFFPNW 204
Cdd:pfam13579 128 ADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-406 3.51e-19

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: 88.36  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADP-------------GEPPEELEDGVIVPLLPSLAALLRA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  82 KRLLHLGSFAVssffplmaqRRWKPDRIIgvVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKggkvaq 161
Cdd:cd03801    68 RRLLRELRPLL---------RLRKFDVVH--AHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL------ 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 162 LATAFERsgLHNVDNVSTISRSMMNKAIEKGVA-AENVIFFPNWSEIARFQhvadvdvDALRNQLGLPDNKKIILYSGNI 240
Cdd:cd03801   131 LARAEAL--LRRADAVIAVSEALRDELRALGGIpPEKIVVIPNGVDLERFS-------PPLRRKLGIPPDRPVLLFVGRL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDChlvvqkrgaad 318
Cdd:cd03801   202 SPRKGVDLLLEALAKLLRRgpDVRLVIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADV----------- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 319 AVLPSKLTNIlavgGNAVITAEAH------TELGQLCETFP--GIAVCVEPESVEALVAGIRQAL----LLPKHNTVARE 386
Cdd:cd03801   271 FVLPSRYEGF----GLVVLEAMAAglpvvaTDVGGLPEVVEdgEGGLVVPPDDVEALADALLRLLadpeLRARLGRAARE 346
                         410       420
                  ....*....|....*....|
gi 1277488664 387 YAERTLDKENVLRQFINDIR 406
Cdd:cd03801   347 RVAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
15-375 3.72e-17

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: 82.43  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPqwqvgenySAWRYKREEGAATVWRCPLYVPKQPStlKRLLHLGSFAVSS 94
Cdd:cd03798    14 PGRGIFVRRQVRALSRRGVDVEVLAPAPWGP--------AAARLLRKLLGEAVPPRDGRRLLPLK--PRLRLLAPLRAPS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  95 FFPLMAQ-RRWKPDRI--IGVVPTLFctpGMRLLAKLSGARTVL-----HIQDYEVDamlglglagkgkggkvaQLATAF 166
Cdd:cd03798    84 LAKLLKRrRRGPPDLIhaHFAYPAGF---AAALLARLYGVPYVVtehgsDINVFPPR-----------------SLLRKL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 167 ERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADvdvdalrnQLGLPDNKKIILYSGNIGEKQGL 246
Cdd:cd03798   144 LRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDR--------GLGLPLDAFVILFVGRLIPRKGI 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 247 ENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGL-HNMQFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLP 322
Cdd:cd03798   216 DLLLEAFARLAKArpDVVLLIVGDGPLREALRALAEDLGLgDRVTFTGRLPHEQVPAYYR------------ACDVfVLP 283
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277488664 323 SkltniLAVG-GNAVITAEA------HTELGQLCE--TFPGIAVCVEPESVEALVAGIRQAL 375
Cdd:cd03798   284 S-----RHEGfGLVLLEAMAcglpvvATDVGGIPEvvGDPETGLLVPPGDADALAAALRRAL 340
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
26-390 3.05e-14

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: 73.47  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  26 EWLAAQGHEVRVITapPYYPQWQVGENYSAWRYKREEGAATVWRCpLYVPKQPSTLKRLlhlgsfavssffplmaqRRWK 105
Cdd:cd03817    25 RALEKRGHEVYVIT--PSDPGAEDEEEVVRYRSFSIPIRKYHRQH-IPFPFKKAVIDRI-----------------KELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 106 PDRI-------IGVVptlfctpGMRLlAKLSGARTV--LHIQdYEVDAmLGLGLAGKGKGGKVAQLATAFersgLHNVDN 176
Cdd:cd03817    85 PDIIhthtpfsLGKL-------GLRI-ARKLKIPIVhtYHTM-YEDYL-HYIPKGKLLVKAVVRKLVRRF----YNHTDA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 177 VSTISRSMMNKAIEKGVAAE-NVIffPNWSEIARFQhvaDVDVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADR 255
Cdd:cd03817   151 VIAPSEKIKDTLREYGVKGPiEVI--PNGIDLDKFE---KPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 256 LRDEPLIFA-IVGQGGGKARLEKMAQQRGL-HNMQFFPLQSYDALPALLKMGDCH----------LVVQKrgAADAVLPs 323
Cdd:cd03817   226 LKKEPNIKLvIVGDGPEREELKELARELGLaDKVIFTGFVPREELPEYYKAADLFvfasttetqgLVYLE--AMAAGLP- 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277488664 324 kltnILAVGGNAVITAEAHTELGQLCETfpgiavcvEPESVEALVAGIRQAL-LLPKHNTVAREYAER 390
Cdd:cd03817   303 ----VVAAKDPAASELVEDGENGFLFEP--------NDETLAEKLLHLRENLeLLRKLSKNAEISARE 358
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
7-379 3.73e-10

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: 60.84  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   7 GINYSPE---LTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawryKREEGAATVWRCPLYVPKQPSTLKR 83
Cdd:cd03809     3 LIDGRSLaqrLTGIGRYTRELLKALAKNDPDESVLAVPPL---------------PGELLRLLREYPELSLGVIKIKLWR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  84 LLHLgsfavssffplmaQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQLA 163
Cdd:cd03809    68 ELAL-------------LRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPI 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 164 TafersgLHNVDNVSTISRSMMNKAIEK-GVAAENVIFFPNwsEIARFQHVADVDvDALRNQLGLPDnkKIILYSGNIGE 242
Cdd:cd03809   135 S------LRRADAIITVSEATRDDIIKFyGVPPEKIVVIPL--GVDPSFFPPESA-AVLIAKYLLPE--PYFLYVGTLEP 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 243 KQGLENVIEAADRLRDE--PLIFAIVGQGGGK-ARLEKMAQQRGLH-NMQFFPLQSYDALPALLKmgdchlvvqkrgAAD 318
Cdd:cd03809   204 RKNHERLLKAFALLKKQggDLKLVIVGGKGWEdEELLDLVKKLGLGgRVRFLGYVSDEDLPALYR------------GAR 271
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277488664 319 A-VLPSkltniLAVG-----------GNAVITA--EAHTELGqlcetfPGIAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03809   272 AfVFPS-----LYEGfglpvleamacGTPVIASniSVLPEVA------GDAALYFDPLDPESIADAILRLLEDPS 335
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
164-395 3.30e-09

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: 58.15  E-value: 3.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 164 TAFERSGLHNVDNVSTISrSMMNKAIEKGVAAENVIFFPNWSEIARFQhvadvDVDALRNQLGLPDNKKIILYSGNIGEK 243
Cdd:cd03821   143 HLIERRNLNNAALVHFTS-EQEADELRRFGLEPPIAVIPNGVDIPEFD-----PGLRDRRKHNGLEDRRIILFLGRIHPK 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 244 QGLENVIEAADRLRDEPL--IFAIVGQGGGkARLEKMAQQR--GLHNMQFFPLQSY-DALPALLKMGDCHlvvqkrgaad 318
Cdd:cd03821   217 KGLDLLIRAARKLAEQGRdwHLVIAGPDDG-AYPAFLQLQSslGLGDRVTFTGPLYgEAKWALYASADLF---------- 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 319 aVLPSKLTNI-------LAVGGNAVITAEAHtelgqLCETF-PGIAVCVEPEsVEALVAGIRQALLLPKHNTVAREYAER 390
Cdd:cd03821   286 -VLPSYSENFgnvvaeaLACGLPVVITDKCG-----LSELVeAGCGVVVDPN-VSSLAEALAEALRDPADRKRLGEMARR 358

                  ....*
gi 1277488664 391 TLDKE 395
Cdd:cd03821   359 ARQVE 363
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
2-278 1.89e-08

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: 55.76  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVIT-APPYYPQWQVGENYSAWRykreegaatvWRCPLY------V 74
Cdd:cd03814     1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApGPFDEAESAEGRVVSVPS----------FPLPFYpeyrlaL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  75 PKQPSTLKR-------LLHLGSFAVSSFFPLMAQRRWKPDrIIGVVPTLFCTPGM-RLLAKLSGartvlhiqdyevdaml 146
Cdd:cd03814    71 PLPRRVRRLikefqpdIIHIATPGPLGLAALRAARRLGLP-VVTSYHTDFPEYLSyYTLGPLSW---------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 147 glglagkgkggkvaqLATAFERSgLHN-VDNVSTISRSMMNKAIEKGvaAENVIFFPNWSEIARFqHVADVDvDALRNQL 225
Cdd:cd03814   134 ---------------LAWAYLRW-FHNpFDTTLVPSPSIARELEGHG--FERVRLWPRGVDTELF-HPSRRD-AALRRRL 193
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277488664 226 GlPDNKKIILYSGNIGEKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKM 278
Cdd:cd03814   194 G-PPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVrLVVVGDGPARAELEAR 246
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
191-391 3.14e-08

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 55.08  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 191 KGVAAENVIFFPNWSEIARFQHVADvdvdalRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRLRDE--PLIFAIVG- 267
Cdd:cd03822   153 KLIPAVNIEVIPHGVPEVPQDPTTA------LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVIAGe 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 268 ------QGGGKARLEKMAQQRGLHNMQFFPLQSY--DALPALLKMgdCHLVVQ-----KRGAADAVlpskltnILAVG-G 333
Cdd:cd03822   227 lhpslaRYEGERYRKAAIEELGLQDHVDFHNNFLpeEEVPRYISA--ADVVVLpylntEQSSSGTL-------SYAIAcG 297
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277488664 334 NAVITaeahTELGQLCETFPGIA-VCVEPESVEALVAGIRQALLLPKHntvAREYAERT 391
Cdd:cd03822   298 KPVIS----TPLRHAEELLADGRgVLVPFDDPSAIAEAILRLLEDDER---RQAIAERA 349
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
190-388 5.23e-07

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: 51.16  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 190 EKGVAAENVIFFPNWSEIARFqHVADVDVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRLRDEP--LIFAIVG 267
Cdd:cd03807   150 EQGYAKNKIVVIYNGIDLFKL-SPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHpdLRLLLVG 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 268 QGGGKARLEKMAQQRGLHNMQFFPLQSYDaLPALLKmgdchlvvqkrgAADA-VLPSK---LTNILA------------- 330
Cdd:cd03807   229 RGPERPNLERLLLELGLEDRVHLLGERSD-VPALLP------------AMDIfVLSSRtegFPNALLeamacglpvvatd 295
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277488664 331 VGGNAVItaeahtelgqLCetfPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYA 388
Cdd:cd03807   296 VGGAAEL----------VD---DGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAA 340
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
8-379 1.02e-06

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: 50.43  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   8 INYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgenysawrykreeGAATVWRCPLYVPKQPSTLKRLLHL 87
Cdd:cd03819     4 LTPALEIGGAETYILDLARALAERGHRVLVVTA----------------------GGPLLPRLRQIGIGLPGLKVPLLRA 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  88 GSFAVSSFFPLmaqRRWKPDrIIGV---VPTLFCtpgmRLLAKLSGARTVLHIQDyevdamlglglagkgkGGKVAQLAT 164
Cdd:cd03819    62 LLGNVRLARLI---RRERID-LIHAhsrAPAWLG----WLASRLTGVPLVTTVHG----------------SYLATYHPK 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 165 AFERSGLHNVDNVSTISRSMMNKAIEK-GVAAENVIFFPNWSEIARFQHVADvdvDALRNQLGLPDNKKIILYSGNIGEK 243
Cdd:cd03819   118 DFALAVRARGDRVIAVSELVRDHLIEAlGVDPERIRVIPNGVDTDRFPPEAE---AEERAQLGLPEGKPVVGYVGRLSPE 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 244 QGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLHNmQFFPLQSYDALPALlkMGDCHLVvqkrgaadaVLP 322
Cdd:cd03819   195 KGWLLLVDAAAELKDEPDFrLLVAGDGPERDEIRRLVERLGLRD-RVTFTGFREDVPAA--LAASDVV---------VLP 262
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277488664 323 SkLTNILavgGNAVITAEAH------TELGQLCETFPG--IAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03819   263 S-LHEEF---GRVALEAMACgtpvvaTDVGGAREIVVHgrTGLLVPPGDAEALADAIRAAKLLPE 323
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
2-310 2.72e-06

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: 48.86  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   2 KILVYGINYSPELT-GIGKYTGEMVEWLAAQGHEVRVITAPPYyPQWQVGENYSAWRYKReegaatvwrcPLYVPKQPST 80
Cdd:cd03823     1 KILLVNSLYPPQRVgGAEISVHDLAEALVAEGHEVAVLTAGVG-PPGQATVARSVVRYRR----------APDETLPLAL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  81 LKRLLHLGSFAVSSFFPLMAQ--RRWKPDRI-----IGVvptlfctpGMRLL--AKLSGARTVLHIQDYEVDAMlglgla 151
Cdd:cd03823    70 KRRGYELFETYNPGLRRLLARllEDFRPDVVhthnlSGL--------GASLLdaARDLGIPVVHTLHDYWLLCP------ 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 152 gkgkggkvaqlatafeRSGL--HNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARfqhvadvdvdALRNQLGLPD 229
Cdd:cd03823   136 ----------------RQFLfkKGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDL----------APPPRRRPGT 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 230 NKKIILYSGNIGEKQGLENVIEAADRLRDEPLIFAIVgqggGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDCHL 309
Cdd:cd03823   190 ERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIA----GHGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLV 265

                  .
gi 1277488664 310 V 310
Cdd:cd03823   266 V 266
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
2-284 2.89e-06

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: 48.89  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664   2 KILVygINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgeNYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03811     1 KILF--VIPSLSGGGAERVLLNLANALDKRGYDVTLVLL-----------RDEGDLDKQLNGDVKLIRLLIRVLKLIKLG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  82 KRLLHLgsfavssFFPLMAQRRwKPDRIIGvvptlFCTPGMRLLAKLSGARTVLHIqdYEVDAMLGLGLAgkgkggkvaQ 161
Cdd:cd03811    68 LLKAIL-------KLKRILKRA-KPDVVIS-----FLGFATYIVAKLAAARSKVIA--WIHSSLSKLYYL---------K 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 162 LATAFERSGLHNVDNVSTISRSMMNKAIEKG-VAAENVIFFPNwseiarFQHVADVDVDALRNQLGLPDNKKIILYSGNI 240
Cdd:cd03811   124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRLGpSPPEKIEVIYN------PIDIDRIRALAKEPILNEPEDGPVILAVGRL 197
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1277488664 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGL 284
Cdd:cd03811   198 DPQKGHDLLIEAFAKLRKKypDVKLVILGDGPLREELEKLAKELGL 243
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
180-335 1.17e-05

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: 47.06  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 180 ISRSMMNKAIEKGVAAENVIFFPNWSEIARFqHVADVDVDALRnqlglpdnkkiILYSGNIGEKQGLENVIEA----ADR 255
Cdd:cd05844   150 VSGFIRDRLLARGLPAERIHVHYIGIDPAKF-APRDPAERAPT-----------ILFVGRLVEKKGCDVLIEAfrrlAAR 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 256 LRDEPLIfaIVGQGGGKARLEKMAqqRGLHNMQFFPLQSYDALPALLkmgdchlvvqkRGAADAVLPSkltnILAVGGNA 335
Cdd:cd05844   218 HPTARLV--IAGDGPLRPALQALA--AALGRVRFLGALPHAEVQDWM-----------RRAEIFCLPS----VTAASGDS 278
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
16-203 1.78e-05

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 44.83  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  16 GIGKYTGEMVEWLAAQGHEVRVIT---APPYYPQWQVGENYSAWRYKREEGaatvwrcPLYVPKQPSTLKRLLhlgsfav 92
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTpggPGPLAEEVVRVVRVPRVPLPLPPR-------LLRSLAFLRRLRRLL------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  93 ssffplmaqRRWKPDRIIGVVPTLFCTpGMRLLAKLSGARTV--LHiqdyevdAMLGLGLAGKGKGGKVAQLATAFERSG 170
Cdd:pfam13439  68 ---------RRERPDVVHAHSPFPLGL-AALAARLRLGIPLVvtYH-------GLFPDYKRLGARLSPLRRLLRRLERRL 130
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1277488664 171 LHNVDNVSTISRSMMNKAIEK-GVAAENVIFFPN 203
Cdd:pfam13439 131 LRRADRVIAVSEAVADELRRLyGVPPEKIRVIPN 164
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
231-307 5.77e-04

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: 41.88  E-value: 5.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277488664 231 KKIILYSGNIGEKQGLENVIEAADRLrDEPLIfaIVGQGGGKARLEKMAQQRGLHNMQFFPLQSYDALPALLKMGDC 307
Cdd:cd03795   191 KKIFLFIGRLVYYKGLDYLIEAAQYL-NYPIV--IGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDV 264
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
231-375 7.29e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 39.42  E-value: 7.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 231 KKIILYSGNIGEKQ-GLENVIEAADRLRDEP--LIFAIVGqGGGKARLEKMAqqRGL-HNMQFFPLQsyDALPALLKMGD 306
Cdd:pfam13692   1 RPVILFVGRLHPNVkGVDYLLEAVPLLRKRDndVRLVIVG-DGPEEELEELA--AGLeDRVIFTGFV--EDLAELLAAAD 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277488664 307 ChlvvqkrgaadAVLPSKLTNIlavgGNAVITAEAH------TELGQLCETFPGIA-VCVEPESVEALVAGIRQAL 375
Cdd:pfam13692  76 V-----------FVLPSLYEGF----GLKLLEAMAAglpvvaTDVGGIPELVDGENgLLVPPGDPEALAEAILRLL 136
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
28-390 7.74e-04

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 41.20  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664  28 LAAQGHEVRVITAPPYyPQWQVGENYSAWRYKReegaatVWRCPlyvPKQPSTLKRLLHLGSFAVSSFFPLMAQRRWKPD 107
Cdd:cd04950    29 LAKLGHRVLFVEEPGN-RDESRTISPTGRIWDR------VWKFL---VKKLGRPARVGLTPDFSAFLLRSLLDALLADSR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 108 RIIGVVPTLFCTPGMRLLAKLSGARTVLHiqdyevDAMLGLGLAGKGKGGKVAQLATAFERsglhnVDNVSTISRsmmnk 187
Cdd:cd04950    99 LGFRRVVLWYYTPMTLLFSDHLQASLVVY------DCMDELAAFPGMPPELIEQERRLIKR-----ADVVFTTSP----- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 188 AIEKGVAA--ENVIFFPNWSEIARFQHvADVDVDALRNQLGLPdnkKIIL-YSGNIGEKQGLENVIEAAdRLRDEpLIFA 264
Cdd:cd04950   163 ALYEAKRPlhENVHPIPNGVDVEHFAA-ARQPLDDPIDLREIP---GPVLgFFGAIDEKLDFDLIEELA-KARPQ-WNFV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 265 IVGQGG--GKARLEKMAqqrglhNMQFFPLQSYDALPALLKMGDCHLV-VQKRGAADAVLPSKLTNILAVGGNAVITAEA 341
Cdd:cd04950   237 FIGPVVkiDPSSLPRAP------NIHWLGPKPYKELPAYLAGFDVALLpFALNEYTRFISPLKLFEYLAAGKPVVATSIP 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1277488664 342 HTELGQLCEtfpgiavCVEPESVEALVAGIRQALLLPKHNTVAREYAER 390
Cdd:cd04950   311 SVVRFYGEA-------VLCGDDPDEFSAAIEKALALKGDARDKRLARAL 352
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
159-401 7.97e-04

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 41.31  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 159 VAQLATAFERSGLHNvdNVSTISRSMMNKAI-EKGVAAENVIFFPNWSEIARFQHVADvdvDALRNQLGLPDNKKIILYS 237
Cdd:PRK15484  125 VMHMHNAFEPELLDK--NAKIIVPSQFLKKFyEERLPNADISIVPNGFCLETYQSNPQ---PNLRQQLNISPDETVLLYA 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 238 GNIGEKQGLENVIEAADRLRDEP--LIFAIVGQGGGKARLEKMAQQRGLHNM--------------------QFFPLQSY 295
Cdd:PRK15484  200 GRISPDKGILLLMQAFEKLATAHsnLKLVVVGDPTASSKGEKAAYQKKVLEAakrigdrcimlggqppekmhNYYPLADL 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 296 DALPALLKMGDCHLVVQKRGAADAVLPSKLTNIlavggnavitaeahTELGQLCETFPGIAvcvEPESVEALVAGIRQAL 375
Cdd:PRK15484  280 VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGI--------------TEFVLEGITGYHLA---EPMTSDSIISDINRTL 342
                         250       260
                  ....*....|....*....|....*....
gi 1277488664 376 LLPKHNTVAREYAERTLDK---ENVLRQF 401
Cdd:PRK15484  343 ADPELTQIAEQAKDFVFSKyswEGVTQRF 371
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
217-386 2.39e-03

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: 39.92  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 217 DVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAA--DRLRDEPLIFAIVG--QGGGKAR----LEKMAQQRGLHNM- 287
Cdd:cd03800   206 RAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFaqLPELRELANLVLVGgpSDDPLSMdreeLAELAEELGLIDRv 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 288 QFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLPSK-----LTNILA-----------VGGNAVITAEAHTelGQLce 350
Cdd:cd03800   286 RFPGRVSRDDLPELYR------------AADVfVVPSLyepfgLTAIEAmacgtpvvataVGGLQDIVRDGRT--GLL-- 349
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1277488664 351 tfpgiavcVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:cd03800   350 --------VDPHDPEALAAALRRLLDDPALWQRLSR 377
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
168-309 3.63e-03

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: 39.26  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277488664 168 RSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADvdvDALRNQLGLPDNKKIILYSGNIGEKQGLE 247
Cdd:cd04962   136 RFSINKSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPA---GALKRRLLAPPDEKVVIHVSNFRPVKRID 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277488664 248 NVIEAADRLRDE-PLIFAIVGQGGGKARLEKMAQQRGLHNMQFFpLQSYDALPALLKMGDCHL 309
Cdd:cd04962   213 DVVRVFARVRRKiPAKLLLVGDGPERVPAEELARELGVEDRVLF-LGKQDDVEELLSIADLFL 274
 
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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