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Conserved domains on  [gi|489305139|ref|WP_003212579|]
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MULTISPECIES: UTP--glucose-1-phosphate uridylyltransferase GalU [Pseudomonas]

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];
1-265 2.29e-161

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


:

Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 449.48  E-value: 2.29e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   1 MIKKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTD 80
Cdd:COG1210    2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  81 KEKYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNleGDGVLTQMVKLYQKYRCTIVAVQ 160
Cdd:COG1210   82 KEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS--EKPCLKQMIEVYEETGGSVIAVQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 161 EVDPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKD 240
Cdd:COG1210  160 EVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260
                 ....*....|....*....|....*
gi 489305139 241 GCVIAYKFKGRRFDCGGAEGYIEAT 265
Cdd:COG1210  240 EPVYAYEFEGKRYDCGDKLGYLKAT 264
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
1-265 2.29e-161

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 449.48  E-value: 2.29e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   1 MIKKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTD 80
Cdd:COG1210    2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  81 KEKYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNleGDGVLTQMVKLYQKYRCTIVAVQ 160
Cdd:COG1210   82 KEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS--EKPCLKQMIEVYEETGGSVIAVQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 161 EVDPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKD 240
Cdd:COG1210  160 EVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260
                 ....*....|....*....|....*
gi 489305139 241 GCVIAYKFKGRRFDCGGAEGYIEAT 265
Cdd:COG1210  240 EPVYAYEFEGKRYDCGDKLGYLKAT 264
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 3-264 1.74e-155

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: 433.70  E-value: 1.74e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139    3 KKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTDKE 82
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   83 KYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEgdGVLTQMVKLYQKYRCTIVAVQEV 162
Cdd:TIGR01099  81 ELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEE--PALKQMIKAYEKTGCSIIAVQEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  163 DPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKDGC 242
Cdd:TIGR01099 159 PKEEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENET 238

                         250       260
                  ....*....|....*....|..
gi 489305139  243 VIAYKFKGRRFDCGGAEGYIEA 264
Cdd:TIGR01099 239 VLAYKFNGKRYDCGSKLGYLEA 260
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-265 8.32e-152

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: 424.64  E-value: 8.32e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   3 KKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTDKE 82
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  83 KYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEgdGVLTQMVKLYQKYRCTIVAVQEV 162
Cdd:cd02541   81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKE--PCLKQLIEAYEKTGASVIAVEEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 163 DPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKDGC 242
Cdd:cd02541  159 PPEDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238

                        250       260
                 ....*....|....*....|...
gi 489305139 243 VIAYKFKGRRFDCGGAEGYIEAT 265
Cdd:cd02541  239 VYAYVFEGKRYDCGNKLGYLKAT 261
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-264 4.48e-71

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 220.93  E-value: 4.48e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   2 IKKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTDK 81
Cdd:PRK13389   8 VKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  82 EKYLVGIRKLLDE-CSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEGD---GVLTQMVKLYQKYRCTIV 157
Cdd:PRK13389  88 RQLLDEVQSICPPhVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDlsqDNLAEMIRRFDETGHSQI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 158 AVQEVdpQETNKYGVI--AGDDI--GDGLIRVrDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDA 233
Cdd:PRK13389 168 MVEPV--ADVTAYGVVdcKGVELapGESVPMV-GVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489305139 234 LLKQAKDGCVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:PRK13389 245 IDMLIEKETVEAYHMKGKSHDCGNKLGYMQA 275
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 9-267 7.44e-29

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: 110.04  E-value: 7.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139    9 AAGYGTRFLPATKAMPKEMLPVVNK-PLIQYGVEEALDAGLNEISIVTGRGKRA-LEDHFDISYELENQIkgtdkekylv 86
Cdd:pfam00483   6 AGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmLNELLGDGSKFGVQI---------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   87 girklldecsfSYTRQTQMKGLGHAILTGRPLIGDEPF-AVVLADDlcvNLEGDGvLTQMVKLYQKY-RCTIVAVQEVDP 164
Cdd:pfam00483  76 -----------TYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGD---HIYRMD-LEQAVKFHIEKaADATVTFGIVPV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  165 QETNKYGVIAGDDIGdgliRVRDMVEKPApEDAPSNLAIIGRYILTPDIF-KLIEETEPGKGGEIQITDALLKQAKDGCV 243
Cdd:pfam00483 141 EPPTGYGVVEFDDNG----RVIRFVEKPK-LPKASNYASMGIYIFNSGVLdFLAKYLEELKRGEDEITDILPKALEDGKL 215

                         250       260
                  ....*....|....*....|....*.
gi 489305139  244 -IAYKFKGRR-FDCGGAEGYIEATNF 267
Cdd:pfam00483 216 aYAFIFKGYAwLDVGTWDSLWEANLF 241
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
1-265 2.29e-161

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 449.48  E-value: 2.29e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   1 MIKKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTD 80
Cdd:COG1210    2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  81 KEKYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNleGDGVLTQMVKLYQKYRCTIVAVQ 160
Cdd:COG1210   82 KEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS--EKPCLKQMIEVYEETGGSVIAVQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 161 EVDPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKD 240
Cdd:COG1210  160 EVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260
                 ....*....|....*....|....*
gi 489305139 241 GCVIAYKFKGRRFDCGGAEGYIEAT 265
Cdd:COG1210  240 EPVYAYEFEGKRYDCGDKLGYLKAT 264
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 3-264 1.74e-155

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: 433.70  E-value: 1.74e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139    3 KKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTDKE 82
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   83 KYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEgdGVLTQMVKLYQKYRCTIVAVQEV 162
Cdd:TIGR01099  81 ELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEE--PALKQMIKAYEKTGCSIIAVQEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  163 DPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKDGC 242
Cdd:TIGR01099 159 PKEEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENET 238

                         250       260
                  ....*....|....*....|..
gi 489305139  243 VIAYKFKGRRFDCGGAEGYIEA 264
Cdd:TIGR01099 239 VLAYKFNGKRYDCGSKLGYLEA 260
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-265 8.32e-152

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: 424.64  E-value: 8.32e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   3 KKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTDKE 82
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  83 KYLVGIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEgdGVLTQMVKLYQKYRCTIVAVQEV 162
Cdd:cd02541   81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKE--PCLKQLIEAYEKTGASVIAVEEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 163 DPQETNKYGVIAGDDIGDGLIRVRDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKDGC 242
Cdd:cd02541  159 PPEDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238

                        250       260
                 ....*....|....*....|...
gi 489305139 243 VIAYKFKGRRFDCGGAEGYIEAT 265
Cdd:cd02541  239 VYAYVFEGKRYDCGNKLGYLKAT 261
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-264 4.48e-71

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 220.93  E-value: 4.48e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   2 IKKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGTDK 81
Cdd:PRK13389   8 VKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  82 EKYLVGIRKLLDE-CSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEGD---GVLTQMVKLYQKYRCTIV 157
Cdd:PRK13389  88 RQLLDEVQSICPPhVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDlsqDNLAEMIRRFDETGHSQI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 158 AVQEVdpQETNKYGVI--AGDDI--GDGLIRVrDMVEKPAPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDA 233
Cdd:PRK13389 168 MVEPV--ADVTAYGVVdcKGVELapGESVPMV-GVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489305139 234 LLKQAKDGCVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:PRK13389 245 IDMLIEKETVEAYHMKGKSHDCGNKLGYMQA 275
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-264 5.42e-65

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 205.12  E-value: 5.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   1 MIK-KCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELENQIKGT 79
Cdd:PRK10122   1 MTNlKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  80 DKEKYLVGIRKLldeCSFSYT----RQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEGDGV---LTQMVKLYQKY 152
Cdd:PRK10122  81 VKRQLLAEVQSI---CPPGVTimnvRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLrynLAAMIARFNET 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 153 RCTIVAVQEVdPQETNKYGVIAGDDIGDG---LIRVRDMVEKP-APEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEI 228
Cdd:PRK10122 158 GRSQVLAKRM-PGDLSEYSVIQTKEPLDRegkVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRI 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489305139 229 QITDALLKQAKDGCVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:PRK10122 237 QLTDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-256 6.34e-55

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: 176.62  E-value: 6.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   8 PAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDisyelenqikgtDKEKYLVG 87
Cdd:cd04181    4 LAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFG------------DGSKFGVN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  88 IRklldecsfsYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCvnlegDGVLTQMVKLYQKYRC--TIVAVQEVDPQ 165
Cdd:cd04181   72 IE---------YVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLT-----DLDLSELLRFHREKGAdaTIAVKEVEDPS 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 166 etnKYGVIAGDDIGdgliRVRDMVEKPAPEdaPSNLAIIGRYILTPDIFKLIEETEPgkGGEIQITDALLKQAKDGCVIA 245
Cdd:cd04181  138 ---RYGVVELDDDG----RVTRFVEKPTLP--ESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG 206

                        250
                 ....*....|.
gi 489305139 246 YKFKGRRFDCG 256
Cdd:cd04181  207 YPVDGYWLDIG 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 3-264 1.20e-51

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: 168.90  E-value: 1.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   3 KKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDisyelenqikgtDKE 82
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALG------------DGS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  83 KYlvgirklldECSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADdlcvNLEGDGvLTQMVKLY--QKYRCTIVAVQ 160
Cdd:cd04189   69 RF---------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGD----NLIQEG-ISPLVRDFleEDADASILLAE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 161 EVDPQEtnkYGVIagdDIGDGliRVRDMVEKPAPEdaPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKD 240
Cdd:cd04189  135 VEDPRR---FGVA---VVDDG--RIVRLVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDR 204

                        250       260
                 ....*....|....*....|....*
gi 489305139 241 G-CVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:cd04189  205 GrRVGYSIVTGWWKDTGTPEDLLEA 229
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
8-267 9.60e-49

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 163.34  E-value: 9.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   8 PAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGrgkraledhfdisyelenqikGTDKEKylvg 87
Cdd:COG1209    6 LAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST---------------------PEDGPQ---- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  88 IRKLLDE-----CSFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCvnlEGDGvLTQMVKLYQKYRC-TIVAVQE 161
Cdd:COG1209   61 FERLLGDgsqlgIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIF---YGDG-LSELLREAAARESgATIFGYK 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 162 V-DPQEtnkYGVIAGDDigDGliRVRDMVEKpaPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKD 240
Cdd:COG1209  137 VeDPER---YGVVEFDE--DG--RVVSLEEK--PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLER 207

                        250       260       270
                 ....*....|....*....|....*....|
gi 489305139 241 GCVIAYkFKGRRF---DCGGAEGYIEATNF 267
Cdd:COG1209  208 GKLVVE-LLGRGFawlDTGTHESLLEANRF 236
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-264 2.22e-42

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: 144.91  E-value: 2.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   4 KCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDisyelenqikgtDKEK 83
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFG------------DGSR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  84 YLVGIRklldecsfsYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLC-VNLEgdgvltQMVKLYQKYR--CTIVAVq 160
Cdd:COG1208   69 FGVRIT---------YVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTdLDLA------ALLAFHREKGadATLALV- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 161 EVDPQEtnKYGVIAGDDIGdgliRVRDMVEKpaPEDAPSNLAIIGRYILTPDIFKLIEEtepgkGGEIQITDALLKQAKD 240
Cdd:COG1208  133 PVPDPS--RYGVVELDGDG----RVTRFVEK--PEEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAE 199

                        250       260
                 ....*....|....*....|....
gi 489305139 241 GCVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:COG1208  200 GRVYGYVHDGYWLDIGTPEDLLEA 223
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 4-264 3.16e-41

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 145.24  E-value: 3.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139    4 KCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVtgrgkraledhfdISYELENQIKGTDKEK 83
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIV-------------VGPVTGEEIKEIVGEG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   84 YLVGIRklldecsFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLcvnLEGDgvLTQMVKLYQK--YRCTIVAVQE 161
Cdd:TIGR01208  68 ERFGAK-------ITYIVQGEPLGLAHAVYTARDFLGDDDFVVYLGDNL---IQDG--ISRFVKSFEEkdYDALILLTKV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  162 VDPQetnKYGVIAGDDiGDGLIRVrdmVEKpaPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITDALLKQAKDG 241
Cdd:TIGR01208 136 RDPT---AFGVAVLED-GKRILKL---VEK--PKEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKG 206

                         250       260
                  ....*....|....*....|....
gi 489305139  242 -CVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:TIGR01208 207 yKVGGSKVTGWWKDTGKPEDLLDA 230
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 9-267 3.03e-30

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: 113.44  E-value: 3.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRG-----KRALEDhfdisyelenqikGTDkek 83
Cdd:cd02538    7 AGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEdlplfKELLGD-------------GSD--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  84 ylVGIRklldecsFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLcvnLEGDGvLTQMVKLY--QKYRCTIVAVQE 161
Cdd:cd02538   71 --LGIR-------ITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNI---FYGQG-LSPILQRAaaQKEGATVFGYEV 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 162 VDPQetnKYGVIAGDDIGdgliRVRDMVEKpaPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITD---ALLKQA 238
Cdd:cd02538  138 NDPE---RYGVVEFDENG----RVLSIEEK--PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDvnnEYLEKG 208

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489305139 239 KdgcvIAYKFKGRRF---DCGGAEGYIEATNF 267
Cdd:cd02538  209 K----LSVELLGRGFawlDTGTHESLLEASNF 236
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 9-267 7.44e-29

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: 110.04  E-value: 7.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139    9 AAGYGTRFLPATKAMPKEMLPVVNK-PLIQYGVEEALDAGLNEISIVTGRGKRA-LEDHFDISYELENQIkgtdkekylv 86
Cdd:pfam00483   6 AGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmLNELLGDGSKFGVQI---------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   87 girklldecsfSYTRQTQMKGLGHAILTGRPLIGDEPF-AVVLADDlcvNLEGDGvLTQMVKLYQKY-RCTIVAVQEVDP 164
Cdd:pfam00483  76 -----------TYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGD---HIYRMD-LEQAVKFHIEKaADATVTFGIVPV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  165 QETNKYGVIAGDDIGdgliRVRDMVEKPApEDAPSNLAIIGRYILTPDIF-KLIEETEPGKGGEIQITDALLKQAKDGCV 243
Cdd:pfam00483 141 EPPTGYGVVEFDDNG----RVIRFVEKPK-LPKASNYASMGIYIFNSGVLdFLAKYLEELKRGEDEITDILPKALEDGKL 215

                         250       260
                  ....*....|....*....|....*.
gi 489305139  244 -IAYKFKGRR-FDCGGAEGYIEATNF 267
Cdd:pfam00483 216 aYAFIFKGYAwLDVGTWDSLWEANLF 241
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-267 3.71e-16

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 76.64  E-value: 3.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   3 KKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIV-----TGRGKRALEDHFDISYELEnqik 77
Cdd:PRK15480   4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIstpqdTPRFQQLLGDGSQWGLNLQ---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  78 gtdkekylvgirklldecsfsYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCVNLEGDGVLTQMVKlyQKYRCTIV 157
Cdd:PRK15480  80 ---------------------YKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVN--KESGATVF 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 158 AVQEVDPQetnKYGVIAGDDIGDGLirvrDMVEKPApeDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIQITD---AL 234
Cdd:PRK15480 137 AYHVNDPE---RYGVVEFDQNGTAI----SLEEKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDinrIY 207

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489305139 235 LKQAKdgcvIAYKFKGRRF---DCGGAEGYIEATNF 267
Cdd:PRK15480 208 MEQGR----LSVAMMGRGYawlDTGTHQSLIEASNF 239
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 4-265 7.55e-16

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: 74.55  E-value: 7.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   4 KCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEIsIVTgrgkraledhfdISYELENQIKGTDKEK 83
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEI-ILA------------VNYRPEDMVPFLKEYE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  84 YLVGIRklldecsFSYTRQTQMKGLGHAILTGRPLIG--DEPFAVVLADDLCvnlegDGVLTQMVKLYQKYRC--TIVaV 159
Cdd:cd06425   69 KKLGIK-------ITFSIETEPLGTAGPLALARDLLGddDEPFFVLNSDVIC-----DFPLAELLDFHKKHGAegTIL-V 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 160 QEVDpqETNKYGVIAGDDIGDgliRVRDMVEKpaPEDAPSNLAIIGRYILTPDIFKLIEETEPGKGGEIqitdaLLKQAK 239
Cdd:cd06425  136 TKVE--DPSKYGVVVHDENTG---RIERFVEK--PKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMAS 203

                        250       260
                 ....*....|....*....|....*.
gi 489305139 240 DGCVIAYKFKGRRFDCGGAEGYIEAT 265
Cdd:cd06425  204 EGQLYAYELPGFWMDIGQPKDFLKGM 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-264 1.67e-13

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: 67.98  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   4 KCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHfdisyeLENQIKGTDkek 83
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAH------LGDSRFGLR--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  84 ylvgIRklldecsFSYTRQTQMkGLGHAILTGRPLIGDEPFAVVLADDLCvnlegDGVLTQMVKLYQKYR----CTIVAV 159
Cdd:cd06422   72 ----IT-------ISDEPDELL-ETGGGIKKALPLLGDEPFLVVNGDILW-----DGDLAPLLLLHAWRMdallLLLPLV 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 160 QEVdpqETNKYGVIAGDdiGDGLIRvrdmvekPAPEDAPSNLAIIGRYILTPDIFKLIEEtepgkgGEIQITDALLKQAK 239
Cdd:cd06422  135 RNP---GHNGVGDFSLD--ADGRLR-------RGGGGAVAPFTFTGIQILSPELFAGIPP------GKFSLNPLWDRAIA 196

                        250       260
                 ....*....|....*....|....*
gi 489305139 240 DGCVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:cd06422  197 AGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 9-264 4.23e-13

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: 66.81  E-value: 4.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDisyelenqikgtdkEKYLVGI 88
Cdd:cd06915    5 AGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFG--------------DGYRGGI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  89 RklldecsFSYTRQTQMKGLGHAILTGRPLIGDEPFAVVLADDLCvnlegDGVLTQMVKLYQKYRCTIV-AVQEVDpqET 167
Cdd:cd06915   71 R-------IYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYF-----DVDLLALLAALRASGADATmALRRVP--DA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 168 NKYGVIAGDDIGdgliRVRDMVEKpaPEDAPSNLAIIGRYILTPDIFKLIEETEPgkGGEiqiTDALLKQAKDGCVIAYK 247
Cdd:cd06915  137 SRYGNVTVDGDG----RVIAFVEK--GPGAAPGLINGGVYLLRKEILAEIPADAF--SLE---ADVLPALVKRGRLYGFE 205

                        250
                 ....*....|....*..
gi 489305139 248 FKGRRFDCGGAEGYIEA 264
Cdd:cd06915  206 VDGYFIDIGIPEDYARA 222
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 9-241 4.74e-13

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: 66.77  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHF--------DISYELENQIKGTd 80
Cdd:cd06426    5 AGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgdgskfgvNISYVREDKPLGT- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  81 kekylVGIRKLLDEcsfsytrqtqmkglghailtgRPligDEPFaVVLADDLCVNLEgdgvLTQMVKLYQKYRCTI-VAV 159
Cdd:cd06426   84 -----AGALSLLPE---------------------KP---TDPF-LVMNGDILTNLN----YEHLLDFHKENNADAtVCV 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 160 QEVDPQetNKYGVIAGDDigdglIRVRDMVEKPapedAPSNLAIIGRYILTPDIFKLIEETEPgkggeIQITDALLKQAK 239
Cdd:cd06426  130 REYEVQ--VPYGVVETEG-----GRITSIEEKP----THSFLVNAGIYVLEPEVLDLIPKNEF-----FDMPDLIEKLIK 193


                 ..
gi 489305139 240 DG 241
Cdd:cd06426  194 EG 195
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-73 1.44e-10

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: 59.94  E-value: 1.44e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489305139   5 CLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFDISYELE 73
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK 69
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-67 2.70e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.10  E-value: 2.70e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489305139   4 KCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFD 67
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 9-246 1.50e-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: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRflpatkaM----PKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRAledhfdisyelenqikgtdkeky 84
Cdd:cd02540    5 AAGKGTR-------MksdlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ----------------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  85 lvgIRKLLDECSFSYTRQTQMKGLGHAILTGRPLIGDepfavvLADDLCVnLEGD------GVLTQMVKLYQKYRCTIV- 157
Cdd:cd02540   55 ---VKKALANPNVEFVLQEEQLGTGHAVKQALPALKD------FEGDVLV-LYGDvplitpETLQRLLEAHREAGADVTv 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 158 --AVQEvDPQEtnkYGVIAGDDIGDglirVRDMVEKpapEDA-PSNLAI----IGRYIL-TPDIFKLIEETEP-GKGGEI 228
Cdd:cd02540  125 ltAELE-DPTG---YGRIIRDGNGK----VLRIVEE---KDAtEEEKAIrevnAGIYAFdAEFLFEALPKLTNnNAQGEY 193

                        250
                 ....*....|....*...
gi 489305139 229 QITDALLKQAKDGCVIAY 246
Cdd:cd02540  194 YLTDIIALAVADGLKVAA 211
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 9-65 2.10e-08

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: 53.41  E-value: 2.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489305139   9 AAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDH 65
Cdd:cd02507    7 ADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEH 63
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 9-55 1.16e-07

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: 51.12  E-value: 1.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489305139   9 AAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVT 55
Cdd:cd04198    7 AGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV 53
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 9-248 1.38e-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: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFlpaTKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRaledhfdisyELENQIKGTdkekylvGI 88
Cdd:PRK14358  14 AAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE----------QVEAALQGS-------GV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  89 RklldecsfsYTRQTQMKGLGHAILTGRPLI--GDEPFAVVLADDLCVNLEgdgVLTQMVKLYQKYRCTIVAVQEVDPQE 166
Cdd:PRK14358  74 A---------FARQEQQLGTGDAFLSGASALteGDADILVLYGDTPLLRPD---TLRALVADHRAQGSAMTILTGELPDA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 167 TNkYGVIAGDDIGdgliRVRDMVEKPAPEDAPSNLAII--GRYIL---TPDIFKLIeeTEPGKGGEIQITDAL-LKQAKD 240
Cdd:PRK14358 142 TG-YGRIVRGADG----AVERIVEQKDATDAEKAIGEFnsGVYVFdarAPELARRI--GNDNKAGEYYLTDLLgLYRAGG 214


                 ....*...
gi 489305139 241 GCVIAYKF 248
Cdd:PRK14358 215 AQVRAFKL 222
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 9-122 4.80e-07

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: 50.41  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFlpatK-AMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHfdisyelenqikgtdkekylvg 87
Cdd:COG1207    9 AAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAA---------------------- 62

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489305139  88 irklLDECSFSYTRQTQMKGLGHAILTGRPLIGDE 122
Cdd:COG1207   63 ----LADLDVEFVLQEEQLGTGHAVQQALPALPGD 93
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
9-67 5.59e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.00  E-value: 5.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489305139   9 AAGYGTRFlpatkAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHFD 67
Cdd:COG2068   10 AAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 13-220 7.69e-07

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: 49.17  E-value: 7.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  13 GTRFLPATKAMPKEMLPVVNKPLIQYGVeEALDA--GLNEISIVTGRGKRALEDHfdISYElenqikgtdKEKYLVGIRK 90
Cdd:cd06428   11 GTRFRPLSLDVPKPLFPVAGKPMIHHHI-EACAKvpDLKEVLLIGFYPESVFSDF--ISDA---------QQEFNVPIRY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  91 LLDECSfsytrqtqmkgLGHA---------ILTGRPligDEPFavVLADDLCVNLEgdgvLTQMVKLYQKYR--CTIVAV 159
Cdd:cd06428   79 LQEYKP-----------LGTAgglyhfrdqILAGNP---SAFF--VLNADVCCDFP----LQELLEFHKKHGasGTILGT 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489305139 160 qEVDPQETNKYGVIAGDDiGDGliRVRDMVEKpaPEDAPSNLAIIGRYILTPDIFKLIEET 220
Cdd:cd06428  139 -EASREQASNYGCIVEDP-STG--EVLHYVEK--PETFVSDLINCGVYLFSPEIFDTIKKA 193
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-191 2.10e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.59  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFlpaTKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHF----DISYELenqikgtdkeky 84
Cdd:PRK14355  10 AAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFagdgDVSFAL------------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  85 lvgirklldecsfsytrQTQMKGLGHAILTGRPLIGDEPFAVVLaddLC--VNLEGDGVLTQMVKLYQKYRcTIVAVQEV 162
Cdd:PRK14355  75 -----------------QEEQLGTGHAVACAAPALDGFSGTVLI---LCgdVPLLRAETLQGMLAAHRATG-AAVTVLTA 133

                        170       180
                 ....*....|....*....|....*....
gi 489305139 163 DPQETNKYGVIAGDdiGDGliRVRDMVEK 191
Cdd:PRK14355 134 RLENPFGYGRIVRD--ADG--RVLRIVEE 158
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 9-66 2.49e-05

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: 44.14  E-value: 2.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489305139   9 AAGYGTRFLPATKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHF 66
Cdd:cd04197    7 ADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 9-56 3.46e-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: 43.32  E-value: 3.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489305139   9 AAGYGTRFlpatkAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTG 56
Cdd:cd04182    7 AAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG 49
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-234 1.14e-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: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   4 KCLFPAAGYGTRFlpaTKAMPKEMLPVVNKPLIQYGVEEALDAGlNEISIVTGRGkraledhfdisYELenqikgtdkek 83
Cdd:PRK14357   2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHE-----------AEL----------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139  84 ylvgIRKLLDECSFSYTRQTQMkGLGHAILTGRPLIGDEPFAVVLADDlcVNLEGDGVLTQMVKLYQKYRC--TIVAVQE 161
Cdd:PRK14357  56 ----VKKLLPEWVKIFLQEEQL-GTAHAVMCARDFIEPGDDLLILYGD--VPLISENTLKRLIEEHNRKGAdvTILVADL 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489305139 162 VDPqetNKYGVIAGDdiGDgliRVRDMVEKPAPEDAPSNLAI-IGRYILTPD-IFKLIEETEP-GKGGEIQITDAL 234
Cdd:PRK14357 129 EDP---TGYGRIIRD--GG---KYRIVEDKDAPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAV 196
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-131 5.63e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   9 AAGYGTRFlpaTKAMPKEMLPVVNKPLIQYGVEEALDAGLNEISIVTGRGKRALEDHfdisyeLENQIKgtdkekylvgi 88
Cdd:PRK14354   9 AAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEV------LGDRSE----------- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489305139  89 rklldecsfsYTRQTQMKGLGHAILTGRPLIGDEPFAV-VLADD 131
Cdd:PRK14354  69 ----------FALQEEQLGTGHAVMQAEEFLADKEGTTlVICGD 102
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-86 3.95e-03

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: 37.50  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139   6 LFPAAGYGTRFlpaTKAMPKEMLPVVNKPLIQYGVEEALDAGL-NEISIVTGRGkraledhfDISYELENQIKGTDKEKY 84
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVPPD--------DIDLAKELAKYGLSKVVK 72


                 ..
gi 489305139  85 LV 86
Cdd:cd02516   73 IV 74
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 157-264 4.77e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.93  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305139 157 VAVQEVDPQETNKYGVIAGDDIGdgliRVRDMVEKPA-PEdapSNLAIIGRYILTPDIFK--LIE-ETEP------GKgg 226
Cdd:PRK05293 149 IAVIEVPWEEASRFGIMNTDENM----RIVEFEEKPKnPK---SNLASMGIYIFNWKRLKeyLIEdEKNPnsshdfGK-- 219

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489305139 227 eiQITDALLKQAKDgcVIAYKFKGRRFDCGGAEGYIEA 264
Cdd:PRK05293 220 --NVIPLYLEEGEK--LYAYPFKGYWKDVGTIESLWEA 253
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-55 9.81e-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: 36.50  E-value: 9.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489305139    6 LFPAAGYGTRFlpaTKAMPKEMLPVVNKPLIQYGVEEALDA-GLNEISIVT 55
Cdd:TIGR00453   3 VIPAAGRGTRF---GSGVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVVV 50
 
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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