NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|573000598|gb|AHF66941|]
View 

sugar transferase [Pseudomonas cichorii JBC1]

Protein Classification

sugar transferase( domain architecture ID 11496316)

sugar transferase similar to Xanthomonas campestris UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase that catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P), forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
5-453 0e+00

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


:

Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 603.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598    5 LLDLTIIV----LIGYWQSQQQPAASTAEIWFQIILAVLVFHWLSEFHQLYGSWRGERILRELAKVFNYWALTFVILLSV 80
Cdd:TIGR03023   1 LLDLLLIAlallLAYLLRFGSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   81 DYLLLSSFRMPDNSHMTWFALVLAALCGYRLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFY 160
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  161 DSHPRQMELNNndhHVPVLGNLEQLIDDAREGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPDVFMFELLHARSE 240
Cdd:TIGR03023 161 DDRPDARTSVR---GVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  241 SINGLASISIFDSPMDGAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMN 320
Cdd:TIGR03023 238 EIGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  321 VQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLRHKVKPGITGW 400
Cdd:TIGR03023 318 VHAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGW 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 573000598  401 AQINGWRGETDTLDKMQKRVEFDLEYIEHWSVWLDLKIILLTLFKGFLNKNAF 453
Cdd:TIGR03023 398 AQVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
5-453 0e+00

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 603.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598    5 LLDLTIIV----LIGYWQSQQQPAASTAEIWFQIILAVLVFHWLSEFHQLYGSWRGERILRELAKVFNYWALTFVILLSV 80
Cdd:TIGR03023   1 LLDLLLIAlallLAYLLRFGSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   81 DYLLLSSFRMPDNSHMTWFALVLAALCGYRLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFY 160
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  161 DSHPRQMELNNndhHVPVLGNLEQLIDDAREGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPDVFMFELLHARSE 240
Cdd:TIGR03023 161 DDRPDARTSVR---GVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  241 SINGLASISIFDSPMDGAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMN 320
Cdd:TIGR03023 238 EIGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  321 VQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLRHKVKPGITGW 400
Cdd:TIGR03023 318 VHAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGW 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 573000598  401 AQINGWRGETDTLDKMQKRVEFDLEYIEHWSVWLDLKIILLTLFKGFLNKNAF 453
Cdd:TIGR03023 398 AQVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-453 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 525.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   1 MAHRLLDLTIIVlIGYWQSQQQPAASTAEIWFQIILAVLV-FHWLSEFHQLYGSWRGERILRELAKVFNYWALTFVILLS 79
Cdd:PRK10124  18 MVQRFSDITIMF-AGLWLVCEVSGLSFLYMHLLVALITLVvFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  80 VdYLLLSSFRMPDNSHMTWFALVLAALCGYRLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGF 159
Cdd:PRK10124  97 L-VAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 160 YDshprqmELNNNDHHVPVLGNLEQLIDDAREGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPDVFMFELLHARS 239
Cdd:PRK10124 176 YH------DPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 240 ESINGLASISIFDSPMDGAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSM 319
Cdd:PRK10124 250 EEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSM 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 320 NVQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLRHKVKPGITG 399
Cdd:PRK10124 330 KVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITG 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 573000598 400 WAQINGWRGETDTLDKMQKRVEFDLEYIEHWSVWLDLKIILLTLFKGFLNKNAF 453
Cdd:PRK10124 410 WAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
116-452 4.73e-99

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 299.73  E-value: 4.73e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 116 VLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFYDSHPRQMELNNNDHHVPVLGNLEQLIDDAREGRID 195
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 196 KVYITLAFSGEPHLRELITGLSDTTASvylipdvfmFELLHARSESINGLASISIFDSPMDGAWSLVKRAEDILLSILIL 275
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 276 LLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMNVQ-ENGAVVRQATRNDARITPLGAFLRRTSLDELP 354
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 355 QFLNVLRGDMSIVGPRPHAVAHNEQYRKQvsGYMLRHKVKPGITGWAQINGWRGETdtldkMQKRVEFDLEYIEHWSVWL 434
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEEE--EYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 573000598 435 DLKIILLTLFKGFLNKNA 452
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
286-447 7.77e-89

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 268.07  E-value: 7.77e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  286 AIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMNVQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMS 365
Cdd:pfam02397  24 AIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVGRFLRKTSLDELPQLINVLKGDMS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  366 IVGPRPHAVAHneQYRKQVSGYMLRHKVKPGITGWAQINGWRGETDtldkMQKRVEFDLEYIEHWSVWLDLKIILLTLFK 445
Cdd:pfam02397 104 LVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLELDLYYIENWSLWLDLKILLKTVKV 177

                  ..
gi 573000598  446 GF 447
Cdd:pfam02397 178 VL 179
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
5-453 0e+00

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 603.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598    5 LLDLTIIV----LIGYWQSQQQPAASTAEIWFQIILAVLVFHWLSEFHQLYGSWRGERILRELAKVFNYWALTFVILLSV 80
Cdd:TIGR03023   1 LLDLLLIAlallLAYLLRFGSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   81 DYLLLSSFRMPDNSHMTWFALVLAALCGYRLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFY 160
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  161 DSHPRQMELNNndhHVPVLGNLEQLIDDAREGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPDVFMFELLHARSE 240
Cdd:TIGR03023 161 DDRPDARTSVR---GVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  241 SINGLASISIFDSPMDGAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMN 320
Cdd:TIGR03023 238 EIGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  321 VQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLRHKVKPGITGW 400
Cdd:TIGR03023 318 VHAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGW 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 573000598  401 AQINGWRGETDTLDKMQKRVEFDLEYIEHWSVWLDLKIILLTLFKGFLNKNAF 453
Cdd:TIGR03023 398 AQVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-453 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 525.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   1 MAHRLLDLTIIVlIGYWQSQQQPAASTAEIWFQIILAVLV-FHWLSEFHQLYGSWRGERILRELAKVFNYWALTFVILLS 79
Cdd:PRK10124  18 MVQRFSDITIMF-AGLWLVCEVSGLSFLYMHLLVALITLVvFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  80 VdYLLLSSFRMPDNSHMTWFALVLAALCGYRLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGF 159
Cdd:PRK10124  97 L-VAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 160 YDshprqmELNNNDHHVPVLGNLEQLIDDAREGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPDVFMFELLHARS 239
Cdd:PRK10124 176 YH------DPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 240 ESINGLASISIFDSPMDGAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSM 319
Cdd:PRK10124 250 EEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSM 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 320 NVQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLRHKVKPGITG 399
Cdd:PRK10124 330 KVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITG 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 573000598 400 WAQINGWRGETDTLDKMQKRVEFDLEYIEHWSVWLDLKIILLTLFKGFLNKNAF 453
Cdd:PRK10124 410 WAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
5-453 1.90e-169

exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model.


Pssm-ID: 274398 [Multi-domain]  Cd Length: 445  Bit Score: 483.63  E-value: 1.90e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598    5 LLDLTIIVLIGYWQSQQQPAASTAEIWFQ---IILAVLVFHWLSEFHQLYGSWRGERILRELAKVFNYWALTFVILLSVD 81
Cdd:TIGR03025   1 LADLLALVLAFLLAFLLLGLGLLPPPDFYsllLLLLLLLFLILFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   82 YLLLSsFRMPDNSHMTWFALVLAALCGYRLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFYD 161
Cdd:TIGR03025  81 FLFKS-FDFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  162 SHPrqmELNNNDHHVPVLGNLEQLIDDAREGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPDVFMFELLHARSES 241
Cdd:TIGR03025 160 DRP---SDRVEVAGLPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  242 INGLASISIFDSPMDGAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMNV 321
Cdd:TIGR03025 237 LGGVPLLSLSNFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  322 -QENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLRHKVKPGITGW 400
Cdd:TIGR03025 317 dAEEGGGPVQATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGW 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 573000598  401 AQINGwRGETDTldkMQKRVEFDLEYIEHWSVWLDLKIILLTLFKGFLNKNAF 453
Cdd:TIGR03025 397 AQVSG-RGETST---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
116-452 4.73e-99

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 299.73  E-value: 4.73e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 116 VLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFYDSHPRQMELNNNDHHVPVLGNLEQLIDDAREGRID 195
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 196 KVYITLAFSGEPHLRELITGLSDTTASvylipdvfmFELLHARSESINGLASISIFDSPMDGAWSLVKRAEDILLSILIL 275
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 276 LLIALPMLLIAIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMNVQ-ENGAVVRQATRNDARITPLGAFLRRTSLDELP 354
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 355 QFLNVLRGDMSIVGPRPHAVAHNEQYRKQvsGYMLRHKVKPGITGWAQINGWRGETdtldkMQKRVEFDLEYIEHWSVWL 434
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEEE--EYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 573000598 435 DLKIILLTLFKGFLNKNA 452
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
286-447 7.77e-89

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 268.07  E-value: 7.77e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  286 AIAIKLTSPGPILFRQRRYGLDGRPIMVWKFRSMNVQENGAVVRQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMS 365
Cdd:pfam02397  24 AIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVGRFLRKTSLDELPQLINVLKGDMS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  366 IVGPRPHAVAHneQYRKQVSGYMLRHKVKPGITGWAQINGWRGETDtldkMQKRVEFDLEYIEHWSVWLDLKIILLTLFK 445
Cdd:pfam02397 104 LVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLELDLYYIENWSLWLDLKILLKTVKV 177

                  ..
gi 573000598  446 GF 447
Cdd:pfam02397 178 VL 179
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
70-445 2.12e-53

sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the family of bacterial sugar transferases (pfam02397). Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria (notable exceptions appear to include Magnetococcus sp. MC-1 and Myxococcus xanthus DK 1622 ). These genes are generally found near one or more of the PrsK, PrsR or PrsT genes that have been related to the PEP-CTERM system by phylogenetic profiling methods. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species. These proteins are homologs of the EpsB protein found in Methylobacillus sp. strain 12S, which is also associated with a PEP-CTERM system, but of a distinct type. A name which appears attached to a number of genes (by transitive annotation) in this family is "undecaprenyl-phosphate galactose phosphotransferase", which comes from relatively distant characterized enterobacterial homologs, and is considerably more specific than warranted from the currently available evidence.


Pssm-ID: 274390 [Multi-domain]  Cd Length: 442  Bit Score: 184.90  E-value: 2.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   70 WALTFVILLSVDYLLLSSFRMPD---NSHMTWFALVLA--ALCGYRLLIRRVLHglrrHGFNTRRVAIVGTGQVGARLAQ 144
Cdd:TIGR03013  66 ARLAISLLVSFLALSFIFYFYPEfylGRGLLALAIVLAgsLVLLSRLFFLKILG----LQGLKRRILVLGTGPRAREIAR 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  145 SISSAPWMGLNLLGFydshprqMELNNNDHHVP---VLGNLEQLIDDAREGRIDKVYITLA-FSGEPHLRELitgLSDTT 220
Cdd:TIGR03013 142 LRRSSDRRGHEIVGF-------VPLPDEPAYVPsehVIENGDGLVEYVLRHRIDEIVIALDeRRGSLPVDEL---LECKL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  221 ASVYLIpDVFMFELLHARSESINGL-ASISIFDSPMD--GAWSLVKRAEDILLSILILLLIALPMLLIAIAIKLTSPGPI 297
Cdd:TIGR03013 212 SGIEVV-DAPSFFERETGKIAIDLIyPSWLIFSNGFRnsSLRRITKRSFDVVASLILLILTLPVMLFTALAIKLESGGPV 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  298 LFRQRRYGLDGRPIMVWKFRSMNV--QENGAVvrQATRNDARITPLGAFLRRTSLDELPQFLNVLRGDMSIVGPRPHAVA 375
Cdd:TIGR03013 291 LYRQERVGLNGRPFNLIKFRSMRAdaEKNGAV--WAQKDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPE 368
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 573000598  376 HNEQYRKQVSGYMLRHKVKPGITGWAQINGWRG--ETDTLDKMQkrveFDLEYIEHWSVWLDLkIILLTLFK 445
Cdd:TIGR03013 369 FVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGasVADAKEKLR----YDLYYIKNMSLLLDL-IILIQTFE 435
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
62-442 3.43e-34

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 133.59  E-value: 3.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  62 ELAKVFNywalTFVILLSVDyLLLSSFRMPDNSHMTW-----FALVLAALcgYRLLIRRVLHGLrrhGFNTRRVAIVGTG 136
Cdd:PRK15204  86 ELKEIFR----TIVIFAIFD-LALIAFTKWQFSRYVWvfcwtFALILVPF--FRALTKHLLNKL---GIWKKKTIILGSG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 137 QVGARLAQSISSAPWMGLNLLGFYDSHPRQMELNNndhhVPVLGNLEQLIDDAREGridKVYITLAFSGEpHLRELITGL 216
Cdd:PRK15204 156 QNARGAYSALQSEEMMGFDVIAFFDTDASDAEINM----LPVIKDTEIIWDLNRTG---DVHYILAYEYT-ELEKTHFWL 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 217 SDTTASvylipdvfmfellHARSES-INGLASISIFDSPMDGAWS----LVKRAEDILLSILILLLIALPMLLIAIAIKL 291
Cdd:PRK15204 228 RELSKH-------------HCRSVTvVPSFRGLPLYNTDMSFIFShevmLLRIQNNLAKRSSRFLKRTFDIVCSIMILII 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 292 TSP-------------GPILFRQRRYGLDGRPIMVWKFRSM--NVQE-------NGAVVRQ------ATRNDARITPLGA 343
Cdd:PRK15204 295 ASPlmiylwykvtrdgGPAIYGHQRVGRHGKLFPCYKFRSMvmNSQEvlkellaNDPIARAewekdfKLKNDPRITAVGR 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 344 FLRRTSLDELPQFLNVLRGDMSIVGPRPHAVAHNEQYRKQVSGYMLrhkVKPGITGWAQINGwRGETDtldkMQKRVEFD 423
Cdd:PRK15204 375 FIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG-RNDVD----YDTRVYFD 446
                        410
                 ....*....|....*....
gi 573000598 424 LEYIEHWSVWLDLKIILLT 442
Cdd:PRK15204 447 SWYVKNWTLWNDIAILFKT 465
CoA_binding_3 pfam13727
CoA-binding domain;
50-227 2.15e-32

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 121.22  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598   50 LYGSWRGERILRELAKVFNYWALTFVILLSVDYLLLSSFrmpdnSHM---TWFALVLAALCGYRLLIRRVLHGLRRHGFN 126
Cdd:pfam13727   5 VYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDIF-----SRLwlaYWAVSGIALLILSRLLLRAVLRRYRRHGRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  127 TRRVAIVGTGQvgaRLAQSISSAPWMGLNLLGFYDSHP--RQMELNNndhhVPVLGNLEQLIDDAREGRIDKVYITLAFS 204
Cdd:pfam13727  80 NRRVVAVGGGL---ELARQIRANPWLGFRVVGVFDDRDddRVPEVAG----VPVLGNLADLVEYVRETRVDEVYLALPLS 152
                         170       180
                  ....*....|....*....|...
gi 573000598  205 GEPHLRELITGLSDTTASVYLIP 227
Cdd:pfam13727 153 AEARILRLVKELRDDPVNIRLIP 175
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
110-228 5.14e-28

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 107.32  E-value: 5.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598 110 RLLIRRVLHGLRRHGFNTRRVAIVGTGQVGARLAQSISSAPWMGLNLLGFYDSHPRqmELNNNDHHVPVLGNLEQLIDDA 189
Cdd:COG1086    4 RLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDDDPD--KRGRRIEGVPVLGTLDDLPELV 81
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 573000598 190 REGRIDKVYITLAFSGEPHLRELITGLSDTTASVYLIPD 228
Cdd:COG1086   82 RRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPD 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
129-200 1.25e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 43.76  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 573000598 129 RVAIVGTGQVGARLAQSISSAPwmGLNLLGFYDSHPRQMELNNNDHHVPVLGNLEQLIDDAregRIDKVYIT 200
Cdd:COG0673    5 RVGIIGAGGIGRAHAPALAALP--GVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADP---DIDAVVIA 71
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
128-213 1.60e-04

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 41.04  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573000598  128 RRVAIVGTGQVGARLAQSIsSAPWMGLNLLGFYDSHPRQMELNNNDHHVPVLGNLEQLIDDareGRIDKVYITL-AFSGE 206
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARAL-NASQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLND---PEIDAVIVATpNGLHY 76

                  ....*..
gi 573000598  207 PHLRELI 213
Cdd:pfam01408  77 DLAIAAL 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH