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Conserved domains on  [gi|727188414|ref|WP_033650221|]
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MULTISPECIES: UTP--glucose-1-phosphate uridylyltransferase GalU [Serratia]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
1-304 0e+00

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


The actual alignment was detected with superfamily member PRK13389:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 302  Bit Score: 576.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   1 MPAVNRKVRKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEA 80
Cdd:PRK13389   1 MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  81 MLEKRVKRQLLDEVQSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSADPKKDNLHDMLQRFE 160
Cdd:PRK13389  81 MLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 161 TTGISQIMVEPVphKDVGNYGVADCKGVELHPGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 240
Cdd:PRK13389 161 ETGHSQIMVEPV--ADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727188414 241 IQLTDSIEMLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVAADK 304
Cdd:PRK13389 239 IQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK 302
 
Name Accession Description Interval E-value
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
1-304 0e+00

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 576.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   1 MPAVNRKVRKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEA 80
Cdd:PRK13389   1 MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  81 MLEKRVKRQLLDEVQSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSADPKKDNLHDMLQRFE 160
Cdd:PRK13389  81 MLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 161 TTGISQIMVEPVphKDVGNYGVADCKGVELHPGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 240
Cdd:PRK13389 161 ETGHSQIMVEPV--ADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727188414 241 IQLTDSIEMLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVAADK 304
Cdd:PRK13389 239 IQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK 302
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-301 1.32e-178

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 494.17  E-value: 1.32e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   6 RKVRKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85
Cdd:COG1210    1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  86 VKRQLLDEVQSICPkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILdeysaDPKKDNLHDMLQRFETTGIS 165
Cdd:COG1210   81 GKEELLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLI-----DSEKPCLKQMIEVYEETGGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 166 QIMVEPVPHKDVGNYGVADCKGVElhpGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 245
Cdd:COG1210  155 VIAVQEVPPEEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTD 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727188414 246 SIEMLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVA 301
Cdd:COG1210  232 AIAALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLK 287
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
9-277 2.56e-156

UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273443 [Multi-domain]  Cd Length: 260  Bit Score: 436.79  E-value: 2.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414    9 RKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   89 QLLDEVQSICPKgVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSAdpkkdNLHDMLQRFETTGISQIM 168
Cdd:TIGR01099  81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP-----ALKQMIKAYEKTGCSIIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  169 VEPVPHKDVGNYGVADCKGVELHPGEsapMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:TIGR01099 155 VQEVPKEEVSKYGVIDGEGIEKDLYK---VKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
                         250       260
                  ....*....|....*....|....*....
gi 727188414  249 MLMQQETVEAYHLKGVSHDCGNKLGYMQA 277
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
9-284 3.83e-154

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 431.57  E-value: 3.83e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   9 RKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  89 QLLDEVqSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILdeysaDPKKDNLHDMLQRFETTGISQIM 168
Cdd:cd02541   81 DLLEEV-RIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLI-----DSKEPCLKQLIEAYEKTGASVIA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 169 VEPVPHKDVGNYGVADCKGVElhpGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:cd02541  155 VEEVPPEDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 727188414 249 MLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMR 284
Cdd:cd02541  232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
10-261 3.00e-21

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 90.39  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDK-PLIQYVVNECIAAGINEIVLVThssknsieNHFDtSFELEamlekrvkR 88
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH-RFMLN--------E 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   89 QLLDEVQsicpKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPV-AVVLPDVILdeYsadpkKDNLHDMLQRF-ETTGISQ 166
Cdd:pfam00483  64 LLGDGSK----FGVQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHI--Y-----RMDLEQAVKFHiEKAADAT 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  167 IMVEPVPHKDVGNYGVADckgvelhPGESAPMVSVVEKPSPEKApSNLAIVGRYVLSADIWPLLAKT---PPGAGDEIql 243
Cdd:pfam00483 133 VTFGIVPVEPPTGYGVVE-------FDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKYleeLKRGEDEI-- 202
                         250
                  ....*....|....*...
gi 727188414  244 TDSIEMLMQQETVEAYHL 261
Cdd:pfam00483 203 TDILPKALEDGKLAYAFI 220
 
Name Accession Description Interval E-value
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
1-304 0e+00

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 576.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   1 MPAVNRKVRKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEA 80
Cdd:PRK13389   1 MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  81 MLEKRVKRQLLDEVQSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSADPKKDNLHDMLQRFE 160
Cdd:PRK13389  81 MLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 161 TTGISQIMVEPVphKDVGNYGVADCKGVELHPGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 240
Cdd:PRK13389 161 ETGHSQIMVEPV--ADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727188414 241 IQLTDSIEMLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVAADK 304
Cdd:PRK13389 239 IQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK 302
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-301 1.32e-178

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 494.17  E-value: 1.32e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   6 RKVRKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85
Cdd:COG1210    1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  86 VKRQLLDEVQSICPkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILdeysaDPKKDNLHDMLQRFETTGIS 165
Cdd:COG1210   81 GKEELLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLI-----DSEKPCLKQMIEVYEETGGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 166 QIMVEPVPHKDVGNYGVADCKGVElhpGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 245
Cdd:COG1210  155 VIAVQEVPPEEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTD 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727188414 246 SIEMLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVA 301
Cdd:COG1210  232 AIAALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLK 287
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
9-277 2.56e-156

UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273443 [Multi-domain]  Cd Length: 260  Bit Score: 436.79  E-value: 2.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414    9 RKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   89 QLLDEVQSICPKgVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSAdpkkdNLHDMLQRFETTGISQIM 168
Cdd:TIGR01099  81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP-----ALKQMIKAYEKTGCSIIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  169 VEPVPHKDVGNYGVADCKGVELHPGEsapMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:TIGR01099 155 VQEVPKEEVSKYGVIDGEGIEKDLYK---VKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
                         250       260
                  ....*....|....*....|....*....
gi 727188414  249 MLMQQETVEAYHLKGVSHDCGNKLGYMQA 277
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
9-284 3.83e-154

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 431.57  E-value: 3.83e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   9 RKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  89 QLLDEVqSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILdeysaDPKKDNLHDMLQRFETTGISQIM 168
Cdd:cd02541   81 DLLEEV-RIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLI-----DSKEPCLKQLIEAYEKTGASVIA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 169 VEPVPHKDVGNYGVADCKGVElhpGESAPMVSVVEKPSPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:cd02541  155 VEEVPPEDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 727188414 249 MLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMR 284
Cdd:cd02541  232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
10-301 5.19e-136

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 386.94  E-value: 5.19e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
Cdd:PRK10122   5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  90 LLDEVQSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSADPKKDNLHDMLQRFETTGISQIMV 169
Cdd:PRK10122  85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRSQVLA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 170 EPVPhKDVGNYGVADCKGVELHPGESAPMVSVVEKP-SPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:PRK10122 165 KRMP-GDLSEYSVIQTKEPLDREGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727188414 249 MLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVA 301
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLS 296
galF TIGR01105
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ...
10-301 2.26e-120

UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a non-catalytic subunit of the UTP-glucose pyrophosphorylase modulating the enzyme activity to increase the formation of UDP-glucose [Regulatory functions, Protein interactions]


Pssm-ID: 130175  Cd Length: 297  Bit Score: 347.40  E-value: 2.26e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
Cdd:TIGR01105   5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   90 LLDEVQSICPKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSADPKKDNLHDMLQRFETTGISQIMV 169
Cdd:TIGR01105  85 LLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATADPLRYNLAAMIARFNETGRSQVLA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  170 EPVPhKDVGNYGVADCKGVELHPGESAPMVSVVEKP-SPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:TIGR01105 165 KRMP-GDLSEYSVIQTKEPLDREGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIA 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727188414  249 MLMQQETVEAYHLKGVSHDCGNKLGYMQAFVEYGMRHASLGKEFSQWLQQVVA 301
Cdd:TIGR01105 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEKLLS 296
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
11-269 1.37e-53

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 174.31  E-value: 1.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELeamlekrvkrql 90
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  91 ldevqsicpkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDeysadpkkDNLHDMLQRF-ETTGISQIMV 169
Cdd:cd04181   69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTD--------LDLSELLRFHrEKGADATIAV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 170 EPVPhkDVGNYGVADCKGVELhpgesapMVSVVEKPSPEkaPSNLAIVGRYVLSADIWPLLAKTPPGAGDEiqLTDSIEM 249
Cdd:cd04181  131 KEVE--DPSRYGVVELDDDGR-------VTRFVEKPTLP--ESNLANAGIYIFEPEILDYIPEILPRGEDE--LTDAIPL 197
                        250       260
                 ....*....|....*....|
gi 727188414 250 LMQQETVEAYHLKGVSHDCG 269
Cdd:cd04181  198 LIEEGKVYGYPVDGYWLDIG 217
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
9-280 2.72e-41

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 144.85  E-value: 2.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   9 RKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVThssknsienhfdTSFELEamlekRVKR 88
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDGP-----QFER 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  89 QLLDEVQsicpKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEysadpkkDNLHDMLQRF-ETTGISQI 167
Cdd:COG1209   64 LLGDGSQ----LGIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG-------DGLSELLREAaARESGATI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 168 MVEPVphKDVGNYGVadckgVELHPGESApmVSVVEKPspEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSI 247
Cdd:COG1209  133 FGYKV--EDPERYGV-----VEFDEDGRV--VSLEEKP--KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDAN 201
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 727188414 248 EMLMQQETVEAYHLkgVSH----DCGNKLGYMQA--FVE 280
Cdd:COG1209  202 QAYLERGKLVVELL--GRGfawlDTGTHESLLEAnrFVL 238
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
10-277 5.04e-40

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 139.63  E-value: 5.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELeamlekrvkrq 89
Cdd:cd04189    2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  90 lldevqsicpkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEysadpkkdNLHDMLQRFETTGIS-QIM 168
Cdd:cd04189   71 -----------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE--------GISPLVRDFLEEDADaSIL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 169 VEPVPhkDVGNYGVADCKGVELhpgesapmVSVVEKPSPEkaPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIE 248
Cdd:cd04189  132 LAEVE--DPRRFGVAVVDDGRI--------VRLVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQ 199
                        250       260       270
                 ....*....|....*....|....*....|
gi 727188414 249 MLMQQ-ETVEAYHLKGVSHDCGNKLGYMQA 277
Cdd:cd04189  200 WLIDRgRRVGYSIVTGWWKDTGTPEDLLEA 229
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
10-269 8.56e-40

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 143.12  E-value: 8.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELeamlekrvkrq 89
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRG----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   90 lldevqsicpkGVTVMQVRQGNAKGLGHAIMCAYPMVgDEPVAVVLPDVILDEysadpkkDNLHDMLQRFETTgisqimV 169
Cdd:TIGR03992  71 -----------GVPIEYVVQEEQLGTADALGSAKEYV-DDEFLVLNGDVLLDS-------DLLERLIRAEAPA------I 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  170 EPVPHKDVGNYGVadckgVELHPGEsapMVSVVEKpsPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDSIEM 249
Cdd:TIGR03992 126 AVVEVDDPSDYGV-----VETDGGR---VTGIVEK--PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQL 195
                         250       260
                  ....*....|....*....|
gi 727188414  250 LMQQETVEAYHLKGVSHDCG 269
Cdd:TIGR03992 196 LIDEGKVKAVELDGFWLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
10-277 1.03e-37

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 133.74  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELeamlekrvkrq 89
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  90 lldevqsicpkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEysadpkkdNLHDMLQRFETTG-ISQIM 168
Cdd:COG1208   70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDL--------DLAALLAFHREKGaDATLA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 169 VepVPHKDVGNYGVADCKGVELhpgesapMVSVVEKpsPEKAPSNLAIVGRYVLSADIWPLLAKtppgaGDEIQLTDSIE 248
Cdd:COG1208  131 L--VPVPDPSRYGVVELDGDGR-------VTRFVEK--PEEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLP 194
                        250       260
                 ....*....|....*....|....*....
gi 727188414 249 MLMQQETVEAYHLKGVSHDCGNKLGYMQA 277
Cdd:COG1208  195 RLIAEGRVYGYVHDGYWLDIGTPEDLLEA 223
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
10-261 3.00e-21

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 90.39  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDK-PLIQYVVNECIAAGINEIVLVThssknsieNHFDtSFELEamlekrvkR 88
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH-RFMLN--------E 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   89 QLLDEVQsicpKGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPV-AVVLPDVILdeYsadpkKDNLHDMLQRF-ETTGISQ 166
Cdd:pfam00483  64 LLGDGSK----FGVQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHI--Y-----RMDLEQAVKFHiEKAADAT 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  167 IMVEPVPHKDVGNYGVADckgvelhPGESAPMVSVVEKPSPEKApSNLAIVGRYVLSADIWPLLAKT---PPGAGDEIql 243
Cdd:pfam00483 133 VTFGIVPVEPPTGYGVVE-------FDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKYleeLKRGEDEI-- 202
                         250
                  ....*....|....*...
gi 727188414  244 TDSIEMLMQQETVEAYHL 261
Cdd:pfam00483 203 TDILPKALEDGKLAYAFI 220
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
9-245 2.17e-19

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 84.93  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   9 RKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVthssknSIENHFDtsfeleamlekRVKR 88
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII------STPEDLP-----------LFKE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  89 QLLDEVQSicpkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILDEYSadpkkdnLHDMLQRFET-TGISQI 167
Cdd:cd02538   64 LLGDGSDL----GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQG-------LSPILQRAAAqKEGATV 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727188414 168 MVEPVphKDVGNYGVADCKgvelhpgESAPMVSVVEKpsPEKAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 245
Cdd:cd02538  133 FGYEV--NDPERYGVVEFD-------ENGRVLSIEEK--PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
10-277 1.83e-15

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 73.76  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFeleamleKRVKRQ 89
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSR-------FGLRIT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  90 LLDEVQSIcpkgvtvmqvrQGNAKGLGHAImcayPMVGDEPVAVVLPDVILDeysaDPKKDNLHDMLQRFETTGISQIMV 169
Cdd:cd06422   74 ISDEPDEL-----------LETGGGIKKAL----PLLGDEPFLVVNGDILWD----GDLAPLLLLHAWRMDALLLLLPLV 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 170 EPVPHKDVGNYGVADCKGVelhpgesapmvsvveKPSPEKAPSNLAIVGRYVLSADiwpLLAKTPPGAGDEIQLTDSiem 249
Cdd:cd06422  135 RNPGHNGVGDFSLDADGRL---------------RRGGGGAVAPFTFTGIQILSPE---LFAGIPPGKFSLNPLWDR--- 193
                        250       260
                 ....*....|....*....|....*...
gi 727188414 250 LMQQETVEAYHLKGVSHDCGNKLGYMQA 277
Cdd:cd06422  194 AIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
11-277 4.16e-14

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 69.85  E-value: 4.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHF-DTSfeleamlEKRVKRQ 89
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgDGS-------KFGVNIS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  90 LLDEvqsicpkgvtvmQVRQGNAKGLGHAimcayPMVGDEPVAVVLPDVILDEysadpkkdNLHDMLQRFETTGISQIMV 169
Cdd:cd06426   74 YVRE------------DKPLGTAGALSLL-----PEKPTDPFLVMNGDILTNL--------NYEHLLDFHKENNADATVC 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 170 epVPHKDVGN-YGVADCKGVELHpgesapmvSVVEKPSpEKAPSNLAIvgrYVLSADIWPLLAKtppgaGDEIQLTDSIE 248
Cdd:cd06426  129 --VREYEVQVpYGVVETEGGRIT--------SIEEKPT-HSFLVNAGI---YVLEPEVLDLIPK-----NEFFDMPDLIE 189
                        250       260       270
                 ....*....|....*....|....*....|
gi 727188414 249 MLMQQ-ETVEAYHLKGVSHDCGNKLGYMQA 277
Cdd:cd06426  190 KLIKEgKKVGVFPIHEYWLDIGRPEDYEKA 219
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
7-253 7.23e-14

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 70.47  E-value: 7.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   7 KVRKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSknsienhfDTSfeleamlekRV 86
Cdd:PRK15480   2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DTP---------RF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  87 KRQLLDEVQSicpkGVTVMQVRQGNAKGLGHAIMCAYPMVGDEPVAVVLPDVILdeYSADPKKdnlhdmLQRFETTGISQ 166
Cdd:PRK15480  65 QQLLGDGSQW----GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIF--YGHDLPK------LMEAAVNKESG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414 167 IMVEPVPHKDVGNYGVadckgVELHPGESApmVSVVEKPSPEKapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDS 246
Cdd:PRK15480 133 ATVFAYHVNDPERYGV-----VEFDQNGTA--ISLEEKPLQPK--SNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDI 203

                 ....*..
gi 727188414 247 IEMLMQQ 253
Cdd:PRK15480 204 NRIYMEQ 210
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
10-73 1.97e-13

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 68.34  E-value: 1.97e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFD 73
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
11-79 2.63e-12

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 64.95  E-value: 2.63e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727188414  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSFELE 79
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK 69
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
10-76 4.92e-12

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 64.20  E-value: 4.92e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTSF 76
Cdd:cd02507    2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSK 68
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
10-77 7.59e-12

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 63.45  E-value: 7.59e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEI-VLVTHSSKNSIENHFDTSFE 77
Cdd:cd04198    2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLRSFPL 70
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
11-73 3.94e-10

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 58.72  E-value: 3.94e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727188414  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFD 73
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFG 63
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
9-163 1.63e-09

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 58.50  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   9 RKAVIPVAGLGTRMlpatK-AIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDtsfeleamlEKRVK 87
Cdd:COG1207    3 LAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA---------DLDVE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  88 rqlldevqsicpkgvTVMQVRQgnaKGLGHAIMCAYPMVG--DEPVAVVLPDVildeysadP--KKDNLHDMLQRFETTG 163
Cdd:COG1207   70 ---------------FVLQEEQ---LGTGHAVQQALPALPgdDGTVLVLYGDV--------PliRAETLKALLAAHRAAG 123
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
9-134 1.02e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 55.99  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   9 RKAVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVT-HSSknsienhfdtsfeleamleKRVK 87
Cdd:PRK14354   3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGA-------------------EEVK 60
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 727188414  88 RQLLDEVQsicpkgvTVMQVRQgnaKGLGHAIMCAYPMVGDEP--VAVV 134
Cdd:PRK14354  61 EVLGDRSE-------FALQEEQ---LGTGHAVMQAEEFLADKEgtTLVI 99
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
11-163 1.89e-08

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 54.06  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  11 AVIPVAGLGTRMlpatK-AIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKnsienhfdtsfeleamlekrvkrq 89
Cdd:cd02540    1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA------------------------ 52
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727188414  90 llDEVQSICPK-GVTVmqVRQGNAKGLGHAIMCAYPMVGD--EPVAVVLPDVildeysadP--KKDNLHDMLQRFETTG 163
Cdd:cd02540   53 --EQVKKALANpNVEF--VLQEEQLGTGHAVKQALPALKDfeGDVLVLYGDV--------PliTPETLQRLLEAHREAG 119
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
10-59 2.12e-08

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 53.75  E-value: 2.12e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 727188414  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVL 59
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIIL 51
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
11-75 3.10e-07

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 50.30  E-value: 3.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727188414  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFDTS 75
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS 67
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
11-62 4.94e-06

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 46.75  E-value: 4.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727188414  11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAG-INEIVLVTH 62
Cdd:cd02516    3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
11-124 1.06e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 46.66  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHF----DTSFELEAmlekrv 86
Cdd:PRK14355   6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFagdgDVSFALQE------ 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727188414  87 kRQLldevqsicpkgvtvmqvrqgnakGLGHAIMCAYP 124
Cdd:PRK14355  77 -EQL-----------------------GTGHAVACAAP 90
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
11-90 1.43e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 45.36  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414   11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVnECIAA--GINEIVLVTHSsknsienhfDTSFELEAMLEKRVKR 88
Cdd:TIGR00453   2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHAL-DAFLAhpAIDEVVVVVSP---------DDTEFFQKYLVARAVP 68

                  ..
gi 727188414   89 QL 90
Cdd:TIGR00453  69 KI 70
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
12-62 3.62e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 43.97  E-value: 3.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727188414  12 VIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAG-INEIVLVTH 62
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
11-73 4.45e-05

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.61  E-value: 4.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727188414  11 AVIPVAGLGTRMlpatkAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIENHFD 73
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
11-61 9.12e-05

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 42.55  E-value: 9.12e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 727188414  11 AVIPVAGLGTRMLPatkaiPKEMLPLVDKPLIQYVVNECIAAGINEIVLVT 61
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVL 48
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
11-140 1.25e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 43.31  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVTHSSKNSIEnhfdtsfeleamlekrvkrql 90
Cdd:PRK14353   8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA--------------------- 63
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727188414  91 lDEVQSICPKGVTVMQVRQgnaKGLGHAIMCAYPMV--GDEPVAVVLPDVIL 140
Cdd:PRK14353  64 -AAAAKIAPDAEIFVQKER---LGTAHAVLAAREALagGYGDVLVLYGDTPL 111
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
11-62 2.44e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 41.66  E-value: 2.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 727188414  11 AVIPVAGLGTRMlpatKA-IPKEMLPLVDKPLIQYVVNECIAAG-INEIVLVTH 62
Cdd:PRK00155   6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
12-61 4.29e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 41.09  E-value: 4.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 727188414  12 VIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVT 61
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC 51
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
12-140 1.28e-03

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.35  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188414  12 VIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVT-HSSKnsienhfdtsfELEAMLEKrvkrql 90
Cdd:PRK14358  11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTgHGAE-----------QVEAALQG------ 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727188414  91 ldevqsicpKGVTVmqVRQGNAKGLGHAIMCAYPMV--GDEPVAVVLPDVIL 140
Cdd:PRK14358  71 ---------SGVAF--ARQEQQLGTGDAFLSGASALteGDADILVLYGDTPL 111
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
17-67 1.86e-03

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 38.72  E-value: 1.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 727188414  17 GLGTRMlpatKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLVThsSKNS 67
Cdd:COG2266    4 GKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAV--SPNT 48
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
11-59 3.60e-03

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 38.32  E-value: 3.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 727188414  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVL 59
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
11-63 5.05e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 38.29  E-value: 5.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 727188414  11 AVIPVAGLGTRmlpATKAIPKEMLPLVDKPLIQYVVNECIAAG-INEIVLVTHS 63
Cdd:PRK09382   8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHP 58
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
11-60 5.24e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.08  E-value: 5.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 727188414  11 AVIPVAGLGTRMLpatKAIPKEMLPLVDKPLIQYVVNECIAAGINEIVLV 60
Cdd:PRK09451   8 VVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLV 54
 
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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