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Conserved domains on  [gi|488923011|ref|WP_002834086|]
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MULTISPECIES: UTP--glucose-1-phosphate uridylyltransferase GalU [Pediococcus]

Protein Classification

UTP--glucose-1-phosphate uridylyltransferase( domain architecture ID 10003115)

UTP--glucose-1-phosphate uridylyltransferase catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP, which is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG)

CATH:  3.90.550.10
EC:  2.7.7.9
Gene Ontology:  GO:0009225|GO:0003983
PubMed:  15020755

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-289 0e+00

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


:

Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 513.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   2 KKVRKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAK 81
Cdd:COG1210    1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  82 GKKEMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLP 160
Cdd:COG1210   81 GKEELLEEVRSISPLaNIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 161 VPHEEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKK 240
Cdd:COG1210  161 VPPEEVSKYGIVDG-EEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488923011 241 QRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPETKDELKTYIKELAKE 289
Cdd:COG1210  240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-289 0e+00

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 513.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   2 KKVRKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAK 81
Cdd:COG1210    1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  82 GKKEMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLP 160
Cdd:COG1210   81 GKEELLEEVRSISPLaNIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 161 VPHEEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKK 240
Cdd:COG1210  161 VPPEEVSKYGIVDG-EEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488923011 241 QRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPETKDELKTYIKELAKE 289
Cdd:COG1210  240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 5-271 7.67e-149

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: 417.70  E-value: 7.67e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAKGKK 84
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  85 EMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLPVPH 163
Cdd:cd02541   81 DLLEEVRIISDLaNIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 164 EEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKKQRV 243
Cdd:cd02541  161 EDVSKYGIVKG-EKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239

                        250       260
                 ....*....|....*....|....*...
gi 488923011 244 FAKVFNGDRYDVGNKFGFLKTNIEYGLK 271
Cdd:cd02541  240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 5-264 2.92e-131

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: 372.84  E-value: 2.92e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011    5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAKGKK 84
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   85 EMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLPVPH 163
Cdd:TIGR01099  81 ELLEEVRKISNLaTIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  164 EEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKKQRV 243
Cdd:TIGR01099 161 EEVSKYGVIDG-EGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239

                         250       260
                  ....*....|....*....|.
gi 488923011  244 FAKVFNGDRYDVGNKFGFLKT 264
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-286 1.36e-77

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 238.27  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   2 KKVRKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAK 81
Cdd:PRK13389   6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  82 GKKEMLKMVEETT--GLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGD--------DLMEDKVpltKQLVDSFEET 151
Cdd:PRK13389  86 VKRQLLDEVQSICppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDvildeyesDLSQDNL---AEMIRRFDET 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 152 GASTLAVLPVphEEVSKYGVID-------PSEEVEkdlynVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGE 224
Cdd:PRK13389 163 GHSQIMVEPV--ADVTAYGVVDckgvelaPGESVP-----MVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGA 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923011 225 GNEVQLTDAIDTLNKKQRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPETKDELKTYIKEL 286
Cdd:PRK13389 236 GDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-257 5.96e-32

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: 118.51  E-value: 5.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011    6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDK-PTIQYIVEEARKSGIEDILIITGKGKRaiedhfdavPELEENLKAKGKK 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHR---------FMLNELLGDGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   85 emlkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNE--PFVVMLGDDLMEDKVpltKQLVDSFEETGAS-TLAVLPV 161
Cdd:pfam00483  72 ----------GVQITYALQPEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDL---EQAVKFHIEKAADaTVTFGIV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  162 PHEEVSKYGVIDPSEEvekdlYNVSKFVEKPAVDEApSNLAIIGRYVLTPEIFNILEKQgLGEGNEVQL--TDAI-DTLN 238
Cdd:pfam00483 139 PVEPPTGYGVVEFDDN-----GRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKY-LEELKRGEDeiTDILpKALE 211

                         250       260
                  ....*....|....*....|
gi 488923011  239 KKQRVFAKVFNGDR-YDVGN 257
Cdd:pfam00483 212 DGKLAYAFIFKGYAwLDVGT 231
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-289 0e+00

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 513.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   2 KKVRKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAK 81
Cdd:COG1210    1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  82 GKKEMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLP 160
Cdd:COG1210   81 GKEELLEEVRSISPLaNIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 161 VPHEEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKK 240
Cdd:COG1210  161 VPPEEVSKYGIVDG-EEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488923011 241 QRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPETKDELKTYIKELAKE 289
Cdd:COG1210  240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 5-271 7.67e-149

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: 417.70  E-value: 7.67e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAKGKK 84
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  85 EMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLPVPH 163
Cdd:cd02541   81 DLLEEVRIISDLaNIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 164 EEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKKQRV 243
Cdd:cd02541  161 EDVSKYGIVKG-EKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239

                        250       260
                 ....*....|....*....|....*...
gi 488923011 244 FAKVFNGDRYDVGNKFGFLKTNIEYGLK 271
Cdd:cd02541  240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 5-264 2.92e-131

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: 372.84  E-value: 2.92e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011    5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAKGKK 84
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   85 EMLKMVEETTGL-NMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLTKQLVDSFEETGASTLAVLPVPH 163
Cdd:TIGR01099  81 ELLEEVRKISNLaTIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  164 EEVSKYGVIDPsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTLNKKQRV 243
Cdd:TIGR01099 161 EEVSKYGVIDG-EGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239

                         250       260
                  ....*....|....*....|.
gi 488923011  244 FAKVFNGDRYDVGNKFGFLKT 264
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-286 1.36e-77

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 238.27  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   2 KKVRKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAK 81
Cdd:PRK13389   6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  82 GKKEMLKMVEETT--GLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGD--------DLMEDKVpltKQLVDSFEET 151
Cdd:PRK13389  86 VKRQLLDEVQSICppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDvildeyesDLSQDNL---AEMIRRFDET 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 152 GASTLAVLPVphEEVSKYGVID-------PSEEVEkdlynVSKFVEKPAVDEAPSNLAIIGRYVLTPEIFNILEKQGLGE 224
Cdd:PRK13389 163 GHSQIMVEPV--ADVTAYGVVDckgvelaPGESVP-----MVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGA 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923011 225 GNEVQLTDAIDTLNKKQRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPETKDELKTYIKEL 286
Cdd:PRK13389 236 GDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
6-286 2.83e-70

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 219.37  E-value: 2.83e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELEENLKAKGKKE 85
Cdd:PRK10122   5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 MLKMVEETT--GLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKV--PLTKQL---VDSFEETGASTLAV 158
Cdd:PRK10122  85 LLAEVQSICppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASadPLRYNLaamIARFNETGRSQVLA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 159 LPVPhEEVSKYGVIDPSE--EVEKDLYNVSKFVEKPAVDEA-PSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAID 235
Cdd:PRK10122 165 KRMP-GDLSEYSVIQTKEplDREGKVSRIVEFIEKPDQPQTlDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488923011 236 TLNKKQRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPETKDELKTYIKEL 286
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKL 294
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 7-256 3.95e-58

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: 185.48  E-value: 3.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   7 AIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELeenlkakgkkem 86
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  87 lkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEdkVPLTKQLVDSFEETGASTLAVLPVPHeeV 166
Cdd:cd04181   69 --------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTD--LDLSELLRFHREKGADATIAVKEVED--P 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 167 SKYGVIdpseeVEKDLYNVSKFVEKPavDEAPSNLAIIGRYVLTPEIFNILEKqgLGEGNEVQLTDAIDTLNKKQRVFAK 246
Cdd:cd04181  137 SRYGVV-----ELDDDGRVTRFVEKP--TLPESNLANAGIYIFEPEILDYIPE--ILPRGEDELTDAIPLLIEEGKVYGY 207

                        250
                 ....*....|
gi 488923011 247 VFNGDRYDVG 256
Cdd:cd04181  208 PVDGYWLDIG 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-265 4.18e-55

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: 178.15  E-value: 4.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELeenlkakgkke 85
Cdd:cd04189    2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 mlkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVpltKQLVDSFEETGASTLAVLpVPHEE 165
Cdd:cd04189   71 ---------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGI---SPLVRDFLEEDADASILL-AEVED 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 166 VSKYGVIDPSEEvekdlyNVSKFVEKPAvdEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTL-NKKQRVF 244
Cdd:cd04189  138 PRRFGVAVVDDG------RIVRLVEKPK--EPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLiDRGRRVG 209

                        250       260
                 ....*....|....*....|.
gi 488923011 245 AKVFNGDRYDVGNKFGFLKTN 265
Cdd:cd04189  210 YSIVTGWWKDTGTPEDLLEAN 230
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
5-265 6.37e-46

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 156.40  E-value: 6.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGkgkraiedhfdavPELEENLKAK-GK 83
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST-------------PEDGPQFERLlGD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  84 KEMLkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVpLTKQLVDSFEETGASTLAVLPVPH 163
Cdd:COG1209   68 GSQL-------GIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDG-LSELLREAAARESGATIFGYKVED 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 164 EEvsKYGVIdpseEVEKDlYNVSKFVEKPAvdEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTDAIDTL--NKKQ 241
Cdd:COG1209  140 PE--RYGVV----EFDED-GRVVSLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYleRGKL 210

                        250       260
                 ....*....|....*....|....
gi 488923011 242 RVFAKVFNGDRYDVGNKFGFLKTN 265
Cdd:COG1209  211 VVELLGRGFAWLDTGTHESLLEAN 234
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 6-257 6.77e-46

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: 154.54  E-value: 6.77e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFdavpeleenlkAKGKKE 85
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYF-----------GDGSRF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 mlkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEdkVPLTKqLVDSFEETGAS-TLAVlpVPHE 164
Cdd:COG1208   70 ---------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD--LDLAA-LLAFHREKGADaTLAL--VPVP 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 165 EVSKYGVIdpseEVEKDlYNVSKFVEKPavDEAPSNLAIIGRYVLTPEIFNILEkqglgEGNEVQLTDAIDTLNKKQRVF 244
Cdd:COG1208  136 DPSRYGVV----ELDGD-GRVTRFVEKP--EEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVY 203

                        250
                 ....*....|...
gi 488923011 245 AKVFNGDRYDVGN 257
Cdd:COG1208  204 GYVHDGYWLDIGT 216
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-257 5.96e-32

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: 118.51  E-value: 5.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011    6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDK-PTIQYIVEEARKSGIEDILIITGKGKRaiedhfdavPELEENLKAKGKK 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHR---------FMLNELLGDGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   85 emlkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNE--PFVVMLGDDLMEDKVpltKQLVDSFEETGAS-TLAVLPV 161
Cdd:pfam00483  72 ----------GVQITYALQPEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDL---EQAVKFHIEKAADaTVTFGIV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  162 PHEEVSKYGVIDPSEEvekdlYNVSKFVEKPAVDEApSNLAIIGRYVLTPEIFNILEKQgLGEGNEVQL--TDAI-DTLN 238
Cdd:pfam00483 139 PVEPPTGYGVVEFDDN-----GRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKY-LEELKRGEDeiTDILpKALE 211

                         250       260
                  ....*....|....*....|
gi 488923011  239 KKQRVFAKVFNGDR-YDVGN 257
Cdd:pfam00483 212 DGKLAYAFIFKGYAwLDVGT 231
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 5-216 1.18e-26

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: 104.58  E-value: 1.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGkraiedhfdAVPELEENLKaKGKK 84
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPE---------DLPLFKELLG-DGSD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  85 emlkmveetTGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDkvPLTKQLVDSFE--ETGASTLAVlPVP 162
Cdd:cd02538   71 ---------LGIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYG--QGLSPILQRAAaqKEGATVFGY-EVN 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923011 163 HEEvsKYGVIdpseEVEKDlYNVSKFVEKPAvdEAPSNLAIIGRYVLTPEIFNI 216
Cdd:cd02538  139 DPE--RYGVV----EFDEN-GRVLSIEEKPK--KPKSNYAVTGLYFYDNDVFEI 183
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-232 2.60e-17

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 80.10  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   3 KVRKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKgkraiedhfDAVPELEEnLKAKG 82
Cdd:PRK15480   2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTP---------QDTPRFQQ-LLGDG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  83 KKemlkmveetTGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLM--EDKVPLTKQLVDsfEETGASTLAVlp 160
Cdd:PRK15480  72 SQ---------WGLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFygHDLPKLMEAAVN--KESGATVFAY-- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923011 161 vpH-EEVSKYGVIdpseEVEKDLYNVSkFVEKPAvdEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVQLTD 232
Cdd:PRK15480 139 --HvNDPERYGVV----EFDQNGTAIS-LEEKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 7-256 3.16e-17

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: 78.36  E-value: 3.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   7 AIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFdavpeleenlkAKGKKEm 86
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF-----------GDGYRG- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  87 lkmveettGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVMLGDDLMEdkVPLtKQLVDSFEETGA-STLAVLPVPHee 165
Cdd:cd06915   69 --------GIRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFD--VDL-LALLAALRASGAdATMALRRVPD-- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 166 VSKYGVIDpseeVEKDlYNVSKFVEKPAVDEApsnlAII--GRYVLTPEIFNILEKQGLgegneVQLTDAIDTLNKKQRV 243
Cdd:cd06915  136 ASRYGNVT----VDGD-GRVIAFVEKGPGAAP----GLIngGVYLLRKEILAEIPADAF-----SLEADVLPALVKRGRL 201

                        250
                 ....*....|...
gi 488923011 244 FAKVFNGDRYDVG 256
Cdd:cd06915  202 YGFEVDGYFIDIG 214
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 6-263 7.92e-17

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: 77.64  E-value: 7.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIitgkgkraiedhfdAVPELEENLkakgkKE 85
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIIL--------------AVNYRPEDM-----VP 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 MLKMVEETTGLNMYFKRQSHPRGLGDAVLTAKSFVG--NEPFVVmLGDDLMEDkVPLtKQLVDSFEETGA-STLAVLPVp 162
Cdd:cd06425   63 FLKEYEKKLGIKITFSIETEPLGTAGPLALARDLLGddDEPFFV-LNSDVICD-FPL-AELLDFHKKHGAeGTILVTKV- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 163 hEEVSKYGVIdpseEVEKDLYNVSKFVEKPAvdEAPSNLAIIGRYVLTPEIFNILEKQGLGEGNEVqltdaIDTLNKKQR 242
Cdd:cd06425  139 -EDPSKYGVV----VHDENTGRIERFVEKPK--VFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMASEGQ 206

                        250       260
                 ....*....|....*....|.
gi 488923011 243 VFAKVFNGDRYDVGNKFGFLK 263
Cdd:cd06425  207 LYAYELPGFWMDIGQPKDFLK 227
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-265 1.37e-15

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: 74.09  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   7 AIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFdavpeleenlkAKGKKem 86
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF-----------GDGSK-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  87 lkmveetTGLNMYFKRQSHPRGLGDAVLTAKSFVgNEPFVVMLGDDLMEDKVpltKQLVDSFEETGAS-TLAV----LPV 161
Cdd:cd06426   68 -------FGVNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLNY---EHLLDFHKENNADaTVCVreyeVQV 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 162 PheevskYGVIDpSEEVEkdlynVSKFVEKPAVdeapSNLAIIGRYVLTPEIFNILEKqglgeGNEVQLTDAID-TLNKK 240
Cdd:cd06426  137 P------YGVVE-TEGGR-----ITSIEEKPTH----SFLVNAGIYVLEPEVLDLIPK-----NEFFDMPDLIEkLIKEG 195

                        250       260
                 ....*....|....*....|....*
gi 488923011 241 QRVFAKVFNGDRYDVGNKFGFLKTN 265
Cdd:cd06426  196 KKVGVFPIHEYWLDIGRPEDYEKAN 220
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 7-246 2.79e-15

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: 73.42  E-value: 2.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   7 AIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPELE--ENLKAkgkk 84
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKfvYNPDY---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  85 emlkmveETTGlNMYfkrqshprglgdAVLTAKSFVgNEPFVVMLGDDLmedkvpLTKQLVDSFEETGASTLAVLPVPHE 164
Cdd:cd02523   77 -------AETN-NIY------------SLYLARDFL-DEDFLLLEGDVV------FDPSILERLLSSPADNAILVDKKTK 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 165 EvskygvidpsEEVEKDLYNVSKFVEKPAVDEAPSNLAIIGRYV----LTPEIFNILEK--QGLGEGNEVQL--TDAIDT 236
Cdd:cd02523  130 E----------WEDEYVKDLDDAGVLLGIISKAKNLEEIQGEYVgiskFSPEDADRLAEalEELIEAGRVNLyyEDALQR 199

                        250
                 ....*....|
gi 488923011 237 LNKKQRVFAK 246
Cdd:cd02523  200 LISEEGVKVK 209
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-158 4.35e-14

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 69.88  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFdavpeleenlkaKGKKE 85
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL------------ARPGP 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923011  86 MLKMVE----ETTGlNMYfkrqShprglgdaVLTAKSFVgNEPFVVMLGDDLMEDKVPltKQLVDSfeeTGASTLAV 158
Cdd:COG1213   69 DVTFVYnpdyDETN-NIY----S--------LWLAREAL-DEDFLLLNGDVVFDPAIL--KRLLAS---DGDIVLLV 126
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-257 2.04e-12

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: 64.90  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAvpeleenlKAKGKKe 85
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD--------SRFGLR- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 mLKMVEETTGLnmyfkrqshpRGLGDAVLTAKSFVGNEPFVVMLGDDLMEDKVPLtkqLVDSFEETGASTLAVLPVpHEE 165
Cdd:cd06422   72 -ITISDEPDEL----------LETGGGIKKALPLLGDEPFLVVNGDILWDGDLAP---LLLLHAWRMDALLLLLPL-VRN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 166 VSKYGVIDPSEEVEKDLynvskfveKPAVDEAPSNLAIIGRYVLTPEIFnilekQGLGEGnEVQLTDAIDTLNKKQRVFA 245
Cdd:cd06422  137 PGHNGVGDFSLDADGRL--------RRGGGGAVAPFTFTGIQILSPELF-----AGIPPG-KFSLNPLWDRAIAAGRLFG 202

                        250
                 ....*....|..
gi 488923011 246 KVFNGDRYDVGN 257
Cdd:cd06422  203 LVYDGLWFDVGT 214
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-172 5.57e-12

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: 65.43  E-value: 5.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   5 RKAIIPAAGLGTRFlpvtK-ASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVPeleenlkakgk 83
Cdd:COG1207    3 LAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLD----------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  84 kemLKMVEettglnmyfkrQSHPRGLGDAVLTAKSFVG--NEPFVVMLGDdlmedkVPLT-----KQLVDSFEETGAS-T 155
Cdd:COG1207   68 ---VEFVL-----------QEEQLGTGHAVQQALPALPgdDGTVLVLYGD------VPLIraetlKALLAAHRAAGAAaT 127

                        170
                 ....*....|....*....
gi 488923011 156 L--AVLPVPHeevsKYGVI 172
Cdd:COG1207  128 VltAELDDPT----GYGRI 142
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 7-180 4.39e-11

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: 61.38  E-value: 4.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   7 AIIPAAGLGTRFlpvtKAS-PKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFdavpeleenlkakgkke 85
Cdd:cd02540    1 AVILAAGKGTRM----KSDlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKAL----------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 mlkmveetTGLNMYFKRQSHPRGLGDAVLTAKSFVG--NEPFVVMLGDdlmedkVPL----T-KQLVDSFEETGAS-TL- 156
Cdd:cd02540   60 --------ANPNVEFVLQEEQLGTGHAVKQALPALKdfEGDVLVLYGD------VPLitpeTlQRLLEAHREAGADvTVl 125

                        170       180
                 ....*....|....*....|....*..
gi 488923011 157 -AVLPVPHEevskYG--VIDPSEEVEK 180
Cdd:cd02540  126 tAELEDPTG----YGriIRDGNGKVLR 148
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 6-67 2.36e-10

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: 59.19  E-value: 2.36e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDH 67
Cdd:cd02507    2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEH 63
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-197 3.14e-10

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 59.51  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRFLPV-TKASPKEMLPIV-DKPTIQYIVEEARK-SGIEDILIITGkgkraiEDHFDAVpelEENLKAKG 82
Cdd:cd02509    2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKGlVPPDRILVVTN------EEYRFLV---REQLPEGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  83 KKEmlKMVEETTGLN----MYFkrqshprglgdAVLTAKSFVGNEPFVVMLGDDLMEDkvpltkqlVDSFEETGAS---- 154
Cdd:cd02509   73 PEE--NIILEPEGRNtapaIAL-----------AALYLAKRDPDAVLLVLPSDHLIED--------VEAFLKAVKKavea 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488923011 155 -------TLAVlpVPHEEVSKYGVIDPSEEVEKDLYNVSKFVEKPAVDEA 197
Cdd:cd02509  132 aeegylvTFGI--KPTRPETGYGYIEAGEKLGGGVYRVKRFVEKPDLETA 179
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-240 4.19e-10

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 59.85  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   5 RKAIIPAAGLGTRFlpvtKAS-PKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKraiedhfdavpeleenlkakgk 83
Cdd:PRK14354   3 RYAIILAAGKGTRM----KSKlPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGA---------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  84 kemlKMVEETTGLNMYFKRQSHPRGLGDAVLTAKSFVGNEPFVVML--GDdlmedkVPLT-----KQLVDSFEETGAS-T 155
Cdd:PRK14354  57 ----EEVKEVLGDRSEFALQEEQLGTGHAVMQAEEFLADKEGTTLVicGD------TPLItaetlKNLIDFHEEHKAAaT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 156 L--AVLPVPHeevsKYGVIdpseeVEKDLYNVSKFVE-KPAVDEapsNLAII----GRYVL-TPEIFNILEK------QG 221
Cdd:PRK14354 127 IltAIAENPT----GYGRI-----IRNENGEVEKIVEqKDATEE---EKQIKeintGTYCFdNKALFEALKKisndnaQG 194

                        250
                 ....*....|....*....
gi 488923011 222 lgegnEVQLTDAIDTLNKK 240
Cdd:PRK14354 195 -----EYYLTDVIEILKNE 208
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 5-58 4.70e-09

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 55.61  E-value: 4.70e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923011   5 RKAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITG 58
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVG 54
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 6-57 1.04e-08

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: 54.20  E-value: 1.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488923011   6 KAIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIIT 57
Cdd:cd04198    2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV 53
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-72 1.22e-08

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 53.63  E-value: 1.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923011   1 MKKVRkAIIPAAGLGTRFlpvtkASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVP 72
Cdd:COG2068    1 MSKVA-AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLG 66
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 7-131 7.24e-08

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: 51.84  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   7 AIIPAAGLGTRFLPVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFdavpeleENLKAKGKKEM 86
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI-------EKSKWSKPKSS 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488923011  87 LKMVEettglnmyFKRQSHPRGLGDAV--LTAKSFVGNePFVVMLGD 131
Cdd:cd04197   76 LMIVI--------IIMSEDCRSLGDALrdLDAKGLIRG-DFILVSGD 113
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 8-197 1.33e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 52.29  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   8 IIPAAGLGTRflpVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEdhfdavpeleenlkakgkkeml 87
Cdd:PRK14358  11 VILAAGQGTR---MKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVE---------------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  88 kmvEETTGLNMYFKRQSHPRGLGDAVLTAKSFV--GNEPFVVMLGDDLMEDKVPLtKQLVDSFEETGaSTLAVLPVPHEE 165
Cdd:PRK14358  66 ---AALQGSGVAFARQEQQLGTGDAFLSGASALteGDADILVLYGDTPLLRPDTL-RALVADHRAQG-SAMTILTGELPD 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 488923011 166 VSKYGVIDPSEEvekdlYNVSKFVEKPAVDEA 197
Cdd:PRK14358 141 ATGYGRIVRGAD-----GAVERIVEQKDATDA 167
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 7-72 3.03e-07

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: 49.48  E-value: 3.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923011   7 AIIPAAGLGTRFlpvtkASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHFDAVP 72
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLP 63
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-68 9.73e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.74  E-value: 9.73e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923011   7 AIIPAAGLGTRflpVTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDHF 68
Cdd:PRK14355   6 AIILAAGKGTR---MKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF 64
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 15-219 6.36e-06

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. 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 that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH 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 including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 46.48  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  15 GTRFLPVTKASPKEMLPIVDKPTIQYIVEEARK-SGIEDILIItgkGKRAIEDHFDAVPELEENLKAKgkkemLKMVEET 93
Cdd:cd06428   11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLI---GFYPESVFSDFISDAQQEFNVP-----IRYLQEY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  94 TGLN----MYFKRqshprglgDAVLTaksfvGN-EPFVVMLGDDLMEdkVPLtKQLVDSFEETGAS-TLAVLPVPHEEVS 167
Cdd:cd06428   83 KPLGtaggLYHFR--------DQILA-----GNpSAFFVLNADVCCD--FPL-QELLEFHKKHGASgTILGTEASREQAS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488923011 168 KYG--VIDPSEevekdlYNVSKFVEKPA--VdeapSNLAIIGRYVLTPEIFNILEK 219
Cdd:cd06428  147 NYGciVEDPST------GEVLHYVEKPEtfV----SDLINCGVYLFSPEIFDTIKK 192
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 143-274 1.45e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 46.01  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011 143 QLVDSFEETGAS-TLAVLPVPHEEVSKYGVIDPSEEVEkdlynVSKFVEKPAvdEAPSNLAIIGRYvltpeIFN--ILeK 219
Cdd:PRK05293 135 KMLDYHKEKEADvTIAVIEVPWEEASRFGIMNTDENMR-----IVEFEEKPK--NPKSNLASMGIY-----IFNwkRL-K 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923011 220 QGLGEGNEvqltDAIDT-----------LNKKQRVFAKVFNGDRYDVGNKFGFLKTNIEYGLKHPE 274
Cdd:PRK05293 202 EYLIEDEK----NPNSShdfgknviplyLEEGEKLYAYPFKGYWKDVGTIESLWEANMELLRPENP 263
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 142-213 9.40e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 43.28  E-value: 9.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923011 142 KQLVDSFEETGAS-TLAVLPVPHEEVSKYGVIDPSEEvekdlYNVSKFVEKPA----VDEAPSN-LAIIGRYVLTPEI 213
Cdd:PRK00844 134 RQMVDFHIESGAGvTVAAIRVPREEASAFGVIEVDPD-----GRIRGFLEKPAdppgLPDDPDEaLASMGNYVFTTDA 206
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-172 1.23e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.21  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011   6 KAIIPAAGLGTRflpVTKASPKEMLPIVDKPTIQYIVEEARKSGIEdILIITGKGKRAIEDHfdavpeLEENLKAKGKKE 85
Cdd:PRK14357   2 RALVLAAGKGTR---MKSKIPKVLHKISGKPMINWVIDTAKKVAQK-VGVVLGHEAELVKKL------LPEWVKIFLQEE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923011  86 MLkmveettglnmyfkrqshprGLGDAVLTAKSFVG-NEPFVVMLGDdlmedkVPLT-----KQLVDSFEETGASTlAVL 159
Cdd:PRK14357  72 QL--------------------GTAHAVMCARDFIEpGDDLLILYGD------VPLIsentlKRLIEEHNRKGADV-TIL 124

                        170
                 ....*....|...
gi 488923011 160 PVPHEEVSKYGVI 172
Cdd:PRK14357 125 VADLEDPTGYGRI 137
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 7-60 8.96e-04

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: 39.81  E-value: 8.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488923011   7 AIIPAAGLGTRFlpvTKASPKEMLPIVDKPTIQYIVEEARKSG-IEDILIITGKG 60
Cdd:cd02516    3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPD 54
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-67 9.16e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.62  E-value: 9.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923011   1 MKKVRKAIIPAAGLGTRFlpvtKAS-PKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKGKRAIEDH 67
Cdd:PRK14353   2 TDRTCLAIILAAGEGTRM----KSSlPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAA 65
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 150-219 9.60e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 40.21  E-value: 9.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923011 150 ETGAS-TLAVLPVPHEEVSKYGVIdpseEVEKDlYNVSKFVEKPAVDEA-PSN----LAIIGRYVLTPE-IFNILEK 219
Cdd:PRK00725 154 ESGADcTVACLEVPREEASAFGVM----AVDEN-DRITAFVEKPANPPAmPGDpdksLASMGIYVFNADyLYELLEE 225
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 8-57 3.42e-03

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: 38.00  E-value: 3.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488923011   8 IIPAAGLGTRFlpvTKAS---PKEMLPIVDKPTIQYIVEEARKSGIEDILIIT 57
Cdd:cd04183    2 IIPMAGLGSRF---KKAGytyPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC 51
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 7-58 4.78e-03

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 36.79  E-value: 4.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488923011    7 AIIPAAGLGTRFlpvtkASPKEMLPIVDKPTIQYIVEEARKSGiEDILIITG 58
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAN 46
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 7-79 5.00e-03

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: 37.65  E-value: 5.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923011    7 AIIPAAGLGTRFlpvTKASPKEMLPIVDKPTIQYIVEEARKSGIEDILIITGKgkraiEDHFDAVPELEENLK 79
Cdd:TIGR00453   2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVS-----PDDTEFFQKYLVARA 66
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 8-60 7.74e-03

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: 37.03  E-value: 7.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923011   8 IIPAAGLGTRFlpvTKASPKEMLPIVDKPTIQYIVEEARKSG-IEDILIITGKG 60
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPD 51
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-79 9.93e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 37.28  E-value: 9.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923011   8 IIPAAGLGTRFLPVTkasPKEMLPIVDKPTIQYIVEEARKSGiEDILIITG----KGKRAIEDHFDAVPELEENLK 79
Cdd:PRK14359   6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHhqkeRIKEAVLEYFPGVIFHTQDLE 77
 
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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