|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-286 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 524.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 2 KPIKKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEMR 81
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 82 HKDKLLEHVRNILPPnITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSILGVE 161
Cdd:COG1210 81 GKEELLEEVRSISPL-ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 162 TVEPSQTGSYGIVETEQL-KQFQRITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDGIAKLLDH 240
Cdd:COG1210 160 EVPPEEVSKYGIVDGEEIeGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1067578651 241 EFVLAHPFEGTRYDCGSKLGYLEATVAYGLKHPETGEPFRRLLEKY 286
Cdd:COG1210 240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-264 |
9.73e-165 |
|
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: 457.59 E-value: 9.73e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 5 KKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEMRHKD 84
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 85 KLLEHVRNILPPnITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSILGVETVE 164
Cdd:TIGR01099 81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 165 PSQTGSYGIVETEQLKQFQ-RITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDGIAKLLDHEFV 243
Cdd:TIGR01099 160 KEEVSKYGVIDGEGIEKDLyKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239
|
250 260
....*....|....*....|.
gi 1067578651 244 LAHPFEGTRYDCGSKLGYLEA 264
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-271 |
1.01e-161 |
|
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: 450.06 E-value: 1.01e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 5 KKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEMRHKD 84
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 85 KLLEHVRnILPPNITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSILGVETVE 164
Cdd:cd02541 81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 165 PSQTGSYGIVETEQL-KQFQRITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDGIAKLLDHEFV 243
Cdd:cd02541 160 PEDVSKYGIVKGEKIdGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
|
250 260
....*....|....*....|....*...
gi 1067578651 244 LAHPFEGTRYDCGSKLGYLEATVAYGLK 271
Cdd:cd02541 240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-284 |
9.31e-104 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 304.52 E-value: 9.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 2 KPIKKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEMR 81
Cdd:PRK13389 6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 82 HKDKLLEHVRNILPPNITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQ-----MVEVYGRSGNS 156
Cdd:PRK13389 86 VKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 157 ILGVETVEpsQTGSYGIVETE--QLKQFQR--ITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTD 232
Cdd:PRK13389 166 QIMVEPVA--DVTAYGVVDCKgvELAPGESvpMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1067578651 233 GIAKLLDHEFVLAHPFEGTRYDCGSKLGYLEATVAYGLKHPETGEPFRRLLE 284
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLE 295
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
6-285 |
9.65e-88 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 263.67 E-value: 9.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEMRHKDK 85
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 86 LLEHVRNILPPNITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKG-----ALKQMVEVYGRSGNSILGV 160
Cdd:PRK10122 85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASAdplryNLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 161 ETVePSQTGSYGIVETEQL----KQFQRITGIVEKP-KPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDGIA 235
Cdd:PRK10122 165 KRM-PGDLSEYSVIQTKEPldreGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1067578651 236 KLLDHEFVLAHPFEGTRYDCGSKLGYLEATVAYGLKHPETGEPFRRLLEK 285
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEK 293
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
7-256 |
2.51e-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: 185.86 E-value: 2.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 7 AVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEmrhkdkl 86
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 87 lehvrnilppnitclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPkgaLKQMVEVYGRSGN--SILGVETVE 164
Cdd:cd04181 74 ---------------YVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHREKGAdaTIAVKEVED 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 165 PSQtgsYGIVETEqlkQFQRITGIVEKPKPEdaPSNLAVVGRYILTPRIFDLLtgLPRGAGNEIQLTDGIAKLLDHEFVL 244
Cdd:cd04181 136 PSR---YGVVELD---DDGRVTRFVEKPTLP--ESNLANAGIYIFEPEILDYI--PEILPRGEDELTDAIPLLIEEGKVY 205
|
250
....*....|..
gi 1067578651 245 AHPFEGTRYDCG 256
Cdd:cd04181 206 GYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-264 |
1.95e-52 |
|
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: 171.21 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 5 KKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYEletklemrhkd 84
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSR----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 85 kllehvrniLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPkgaLKQMVEVYGRSG--NSILGVET 162
Cdd:cd04189 70 ---------FGVRIT--YILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDadASILLAEV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 163 VEPSQtgsYGIVETEQlkqfQRITGIVEKPKPEdaPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDGIAKLLDHEF 242
Cdd:cd04189 136 EDPRR---FGVAVVDD----GRIVRLVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGR 206
|
250 260
....*....|....*....|...
gi 1067578651 243 -VLAHPFEGTRYDCGSKLGYLEA 264
Cdd:cd04189 207 rVGYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-264 |
4.67e-46 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 156.79 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTG-RNKRSIEDHFDKAYELETKLEmrhkd 84
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGSQLGIKIS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 85 kllehvrnilppnitclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDApkGALKQMVEVY--GRSGNSILGVET 162
Cdd:COG1209 77 -----------------YAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG--DGLSELLREAaaRESGATIFGYKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 163 VEPSQtgsYGIVEteqLKQFQRITGIVEKPKpeDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDGIAKLLDHEF 242
Cdd:COG1209 138 EDPER---YGVVE---FDEDGRVVSLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGK 209
|
250 260
....*....|....*....|....
gi 1067578651 243 -VLAHPFEGTR-YDCGSKLGYLEA 264
Cdd:COG1209 210 lVVELLGRGFAwLDTGTHESLLEA 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-264 |
4.12e-44 |
|
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: 149.92 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYEletklemrhkdk 85
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSR------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 86 llehvrniLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPkgaLKQMVEVYGRSGN--SILGVETV 163
Cdd:COG1208 69 --------FGVRIT--YVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLD---LAALLAFHREKGAdaTLALVPVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 164 EPSQtgsYGIVETEqlkQFQRITGIVEkpKPEDAPSNLAVVGRYILTPRIFDLLTglprgAGNEIQLTDGIAKLLDHEFV 243
Cdd:COG1208 136 DPSR---YGVVELD---GDGRVTRFVE--KPEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRV 202
|
250 260
....*....|....*....|.
gi 1067578651 244 LAHPFEGTRYDCGSKLGYLEA 264
Cdd:COG1208 203 YGYVHDGYWLDIGTPEDLLEA 223
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-268 |
2.00e-27 |
|
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: 106.57 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDK-PLIQYAVEEAVEAGCTEMVFVTG-RNKRSIEDHFDKAYELEtklemrhk 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGDGSKFG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 84 dkllehvrnilppnITCLYIRQAEALGLGHAVLCARAAIGDEPF-AVILADDLI--DAPKGALKQMVEVYGRSGNSILGV 160
Cdd:pfam00483 73 --------------VQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIyrMDLEQAVKFHIEKAADATVTFGIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 161 ETVEPSqtgSYGIVETEQLkqfQRITGIVEKPKpEDAPSNLAVVGRYILTPRIFDLLTG----LPRGAgNEIqlTDGIAK 236
Cdd:pfam00483 139 PVEPPT---GYGVVEFDDN---GRVIRFVEKPK-LPKASNYASMGIYIFNSGVLDFLAKyleeLKRGE-DEI--TDILPK 208
|
250 260 270
....*....|....*....|....*....|....
gi 1067578651 237 LL-DHEFVLAHPFEGTR-YDCGSKLGYLEATVAY 268
Cdd:pfam00483 209 ALeDGKLAYAFIFKGYAwLDVGTWDSLWEANLFL 242
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-232 |
3.50e-22 |
|
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: 92.25 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 5 KKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRnkrsiEDhfdkayeletkleMRHKD 84
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP-----ED-------------LPLFK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 85 KLLEHVRNiLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAP--KGALKQMVEVygRSGNSILGVET 162
Cdd:cd02538 63 ELLGDGSD-LGIRIT--YAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQglSPILQRAAAQ--KEGATVFGYEV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 163 VEPSQtgsYGIVEteqLKQFQRITGIVEKPKpeDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTD 232
Cdd:cd02538 138 NDPER---YGVVE---FDENGRVLSIEEKPK--KPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-268 |
4.52e-15 |
|
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: 72.63 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTgrNKRSiEDHFDKAYELETKLEMRhkdk 85
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAV--NYRP-EDMVPFLKEYEKKLGIK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 86 llehvrnilppnITClyIRQAEALGLGHAVLCARAAIG--DEPFAVILADDLIDAPkgaLKQMVEVYGRSGN--SILGVE 161
Cdd:cd06425 75 ------------ITF--SIETEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFP---LAELLDFHKKHGAegTILVTK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 162 TVEPSQtgsYGIVETEQLKqfQRITGIVEKPKpeDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIqltdgIAKLLDHE 241
Cdd:cd06425 138 VEDPSK---YGVVVHDENT--GRIERFVEKPK--VFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMASEG 205
|
250 260
....*....|....*....|....*..
gi 1067578651 242 FVLAHPFEGTRYDCGSKLGYLEATVAY 268
Cdd:cd06425 206 QLYAYELPGFWMDIGQPKDFLKGMSLY 232
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-249 |
5.39e-14 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 71.70 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 7 AVFPVAGMGTRFlpatKAN-PKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLemrhkdk 85
Cdd:PRK14355 6 AIILAAGKGTRM----KSDlVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 86 llehvrnilppnitclyirQAEALGLGHAVLCARAAIgdEPFA---VILADD--LIDApkGALKQMVEVYGRSGnSILGV 160
Cdd:PRK14355 75 -------------------QEEQLGTGHAVACAAPAL--DGFSgtvLILCGDvpLLRA--ETLQGMLAAHRATG-AAVTV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 161 ETVEPSQTGSYGIVeteqLKQFQ-RITGIVEK--PKPEDAPSNLAVVGRY-ILTPRIFDLLTGLPR-GAGNEIQLTDGIA 235
Cdd:PRK14355 131 LTARLENPFGYGRI----VRDADgRVLRIVEEkdATPEERSIREVNSGIYcVEAAFLFDAIGRLGNdNAQGEYYLTDIVA 206
|
250
....*....|....*
gi 1067578651 236 KLLDHEF-VLAHPFE 249
Cdd:PRK14355 207 MAAAEGLrCLAFPVA 221
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
12-190 |
8.91e-14 |
|
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: 70.83 E-value: 8.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFLPATkanPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFdkayeletklemrhkdkllehvr 91
Cdd:COG1207 10 AGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 92 nilpPNITCLYIRQAEALGLGHAVLCARAAI-GDEPFAVILADD--LIDApkGALKQMVEVYGRSGNSiLGVETVEPSQT 168
Cdd:COG1207 64 ----ADLDVEFVLQEEQLGTGHAVQQALPALpGDDGTVLVLYGDvpLIRA--ETLKALLAAHRAAGAA-ATVLTAELDDP 136
|
170 180
....*....|....*....|...
gi 1067578651 169 GSYG-IVETEQlkqfQRITGIVE 190
Cdd:COG1207 137 TGYGrIVRDED----GRVLRIVE 155
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
12-235 |
9.86e-14 |
|
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: 68.70 E-value: 9.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFlpatKAN-PKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedhfdkayeletklemrHKdklLEHV 90
Cdd:cd02540 6 AGKGTRM----KSDlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVG-----------------------HG---AEQV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 91 RNILP-PNITclYIRQAEALGLGHAVLCARAAIGDEPFAV-ILADD--LIDApkGALKQMVEVYGRSGNSIlGVETVEPS 166
Cdd:cd02540 56 KKALAnPNVE--FVLQEEQLGTGHAVKQALPALKDFEGDVlVLYGDvpLITP--ETLQRLLEAHREAGADV-TVLTAELE 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578651 167 QTGSYG-IVeteqLKQFQRITGIVEKpkpEDA-PSNLAVV----GRYIL-TPRIFDLLTGL-PRGAGNEIQLTDGIA 235
Cdd:cd02540 131 DPTGYGrII----RDGNGKVLRIVEE---KDAtEEEKAIRevnaGIYAFdAEFLFEALPKLtNNNAQGEYYLTDIIA 200
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
13-240 |
1.27e-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: 68.31 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 13 GMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEmrhkdkllehvrn 92
Cdd:cd06426 7 GKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNIS------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 93 ilppnitclYIRQAEALGLGHAVLCARAAIgDEPFAVILADDLIDAPKGALKQmvevYGRSGNSILGVETVEPSQTGSYG 172
Cdd:cd06426 74 ---------YVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLNYEHLLD----FHKENNADATVCVREYEVQVPYG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578651 173 IVETEQlkqfQRITGIVEKPKpedaPSNLAVVGRYILTPRIFDLLTglprgAGNEIQLTDGIAKLLDH 240
Cdd:cd06426 140 VVETEG----GRITSIEEKPT----HSFLVNAGIYVLEPEVLDLIP-----KNEFFDMPDLIEKLIKE 194
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-76 |
4.31e-12 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 64.18 E-value: 4.31e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 7 AVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELET 76
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF 70
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-148 |
6.68e-12 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 63.72 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedhfdkaYeletklemrHKDK 85
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTG-------------Y---------KAEL 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578651 86 LLEHVRNIlPPNITCLYIRQAEALGLGHAVLCARAAIgDEPFAVILADDLIDapKGALKQMVE 148
Cdd:COG1213 59 IEEALARP-GPDVTFVYNPDYDETNNIYSLWLAREAL-DEDFLLLNGDVVFD--PAILKRLLA 117
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
5-265 |
2.15e-11 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 63.15 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 5 KKAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFV-----TGRNKRSIEDHFDKAYELETKLe 79
Cdd:PRK15480 4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIstpqdTPRFQQLLGDGSQWGLNLQYKV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 80 mrhkdkllehvrnilppnitclyirQAEALGLGHAVLCARAAIGDEPFAVILADDLI---DAPKgalKQMVEVYGRSGNS 156
Cdd:PRK15480 83 -------------------------QPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFyghDLPK---LMEAAVNKESGAT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 157 ILGVETVEPSQtgsYGIVETEqlkqfQRITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAGNEIQLTDgIAK 236
Cdd:PRK15480 135 VFAYHVNDPER---YGVVEFD-----QNGTAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD-INR 205
|
250 260 270
....*....|....*....|....*....|..
gi 1067578651 237 LLDHEFVLAHPFEGTRY---DCGSKLGYLEAT 265
Cdd:PRK15480 206 IYMEQGRLSVAMMGRGYawlDTGTHQSLIEAS 237
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
13-264 |
6.25e-11 |
|
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: 60.64 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 13 GMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEmrhkdkllehvrn 92
Cdd:cd06915 7 GLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIY------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 93 ilppnitclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDApkgALKQMVEVYGRSG--NSILGVETVEPSQtgs 170
Cdd:cd06915 74 ---------YVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDV---DLLALLAALRASGadATMALRRVPDASR--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 171 YGIVETEqlkQFQRITGIVEkpKPEDAPSNLAVVGRYILTPRIFDLLTGLPRGAgneiqLTDGIAKLLDHEFVLAHPFEG 250
Cdd:cd06915 139 YGNVTVD---GDGRVIAFVE--KGPGAAPGLINGGVYLLRKEILAEIPADAFSL-----EADVLPALVKRGRLYGFEVDG 208
|
250
....*....|....
gi 1067578651 251 TRYDCGSKLGYLEA 264
Cdd:cd06915 209 YFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-264 |
2.42e-10 |
|
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: 59.12 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVfvtgrnkrsIEDHFdkayeletklemrHKDK 85
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIV---------VNTHH-------------LADQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 86 LLEHVRN-ILPPNITclYIR-QAEALGLGHAVLCARAAIGDEPFAVILAD-----DLIDAPKGALKQMvevygrSGNSIL 158
Cdd:cd06422 59 IEAHLGDsRFGLRIT--ISDePDELLETGGGIKKALPLLGDEPFLVVNGDilwdgDLAPLLLLHAWRM------DALLLL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 159 GVETVEPSQTGsYGIVETEQLKQFQRitgivekpKPEDAPSNLAVVGRYILTPRIFDlltGLPRGAGNEIQLTDgiaKLL 238
Cdd:cd06422 131 LPLVRNPGHNG-VGDFSLDADGRLRR--------GGGGAVAPFTFTGIQILSPELFA---GIPPGKFSLNPLWD---RAI 195
|
250 260
....*....|....*....|....*.
gi 1067578651 239 DHEFVLAHPFEGTRYDCGSKLGYLEA 264
Cdd:cd06422 196 AAGRLFGLVYDGLWFDVGTPERLLAA 221
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-188 |
3.63e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 60.16 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 6 KAVFPVAGMGTRFlpaTKANPKEMLPIVDKPLIQYAVEEAVEAGcTEMVFVTGRNKrsiedhfdkayeletklemrhkdk 85
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEA------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 86 llEHVRNILPPNITcLYIrQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNS--ILGVETV 163
Cdd:PRK14357 54 --ELVKKLLPEWVK-IFL-QEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADvtILVADLE 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 1067578651 164 EPS-------QTGSYGIVE----TEQLKQFQRI-TGI 188
Cdd:PRK14357 130 DPTgygriirDGGKYRIVEdkdaPEEEKKIKEInTGI 166
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
12-190 |
4.66e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 59.88 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFLPATkanPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRnkrsiedhfdkayeletklemrHKDKLLEHVR 91
Cdd:PRK14353 13 AGEGTRMKSSL---PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP----------------------GAEAVAAAAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 92 NILPPNITCLyirQAEALGLGHAVLCARAAI--GDEPFAVILADD-LIDAPkgALKQMVEvYGRSGNSI--LGVETVEPs 166
Cdd:PRK14353 68 KIAPDAEIFV---QKERLGTAHAVLAAREALagGYGDVLVLYGDTpLITAE--TLARLRE-RLADGADVvvLGFRAADP- 140
|
170 180
....*....|....*....|....*.
gi 1067578651 167 qtGSYG--IVETEQLkqfqriTGIVE 190
Cdd:PRK14353 141 --TGYGrlIVKGGRL------VAIVE 158
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
8-232 |
5.79e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 53.44 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 8 VFPVAGMGTRFlpaTKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNkrsiedhfdkAYELETKLEMrhkdkll 87
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHG----------AEQVEAALQG------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 88 ehvrnilpPNITclYIRQAEALGLGHAVLCARAAI--GDEPFAVILADDLIDAPKgALKQMVEVYgRSGNSILGVETVE- 164
Cdd:PRK14358 71 --------SGVA--FARQEQQLGTGDAFLSGASALteGDADILVLYGDTPLLRPD-TLRALVADH-RAQGSAMTILTGEl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 165 PSQTGsYG------------IVETEQLKQFQRITG-------IVEKPKPEDAP--SNLAVVGRYILTprifDLLtGLPRG 223
Cdd:PRK14358 139 PDATG-YGrivrgadgaverIVEQKDATDAEKAIGefnsgvyVFDARAPELARriGNDNKAGEYYLT----DLL-GLYRA 212
|
250
....*....|..
gi 1067578651 224 AGNEI---QLTD 232
Cdd:PRK14358 213 GGAQVrafKLSD 224
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
15-217 |
7.70e-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: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 15 GTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedhfdkaYELETKLEmrhkdKLLEHVRNil 94
Cdd:cd06428 11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIG-------------FYPESVFS-----DFISDAQQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 95 PPNITCLYIRQAEALGLGHAVLCARAAI---GDEPFAVILADDLIDAPkgaLKQMVEVYGRSGNS--ILGVEtVEPSQTG 169
Cdd:cd06428 71 EFNVPIRYLQEYKPLGTAGGLYHFRDQIlagNPSAFFVLNADVCCDFP---LQELLEFHKKHGASgtILGTE-ASREQAS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067578651 170 SYG-IVETEQLkqfQRITGIVEKPkpEDAPSNLAVVGRYILTPRIFDLL 217
Cdd:cd06428 147 NYGcIVEDPST---GEVLHYVEKP--ETFVSDLINCGVYLFSPEIFDTI 190
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-73 |
2.15e-06 |
|
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: 47.65 E-value: 2.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTE-MVFVTGRNKRSIEDHFDKAYE 73
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDvIVVVPEEEQAEISTYLRSFPL 70
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-82 |
3.13e-06 |
|
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: 46.86 E-value: 3.13e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578651 6 KAVFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETKLEMRH 82
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIV 78
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
12-158 |
3.15e-06 |
|
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: 46.78 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFlpatkANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedHfdkayeletklemrHKDKLLEHVR 91
Cdd:cd04182 8 AGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG--------A--------------EADAVRAALA 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 92 NILPPNITCLYirqaEALGLGHAVLCARAAIGDEP--FAVILAD-DLIDApkGALKQMVEVYGRSGNSIL 158
Cdd:cd04182 61 GLPVVVVINPD----WEEGMSSSLAAGLEALPADAdaVLILLADqPLVTA--ETLRALIDAFREDGAGIV 124
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
12-158 |
3.19e-06 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 46.69 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFlpatkANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDkayeletklemrhkdkllehvr 91
Cdd:COG2068 11 AGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA---------------------- 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 92 nilPPNITCLYIRQAEaLGLGHAVLCARAAIGDEPFAVILAddLIDAP---KGALKQMVEVYGRSGNSIL 158
Cdd:COG2068 64 ---GLGVRVVVNPDWE-EGMSSSLRAGLAALPADADAVLVL--LGDQPlvtAETLRRLLAAFRESPASIV 127
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-191 |
6.26e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 47.13 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 5 KKAVFPVAGMGTRFlpatKAN-PKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHfdkayeLETKLEmrhk 83
Cdd:PRK14354 3 RYAIILAAGKGTRM----KSKlPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEV------LGDRSE---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 84 dkllehvrnilppnitclYIRQAEALGLGHAVLCARAAIGDEPFAV-ILADD--LIDApkGALKQMVEVYGRSGNS--IL 158
Cdd:PRK14354 69 ------------------FALQEEQLGTGHAVMQAEEFLADKEGTTlVICGDtpLITA--ETLKNLIDFHEEHKAAatIL 128
|
170 180 190
....*....|....*....|....*....|....
gi 1067578651 159 GVETVEPsqTGsYG-IVETEQlkqfqritGIVEK 191
Cdd:PRK14354 129 TAIAENP--TG-YGrIIRNEN--------GEVEK 151
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
124-250 |
7.96e-05 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 43.53 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 124 DEPFAVILADDLI---DapkgaLKQMVEVYGRSGNSI-LGVETVEPSQTGSYGIVET-EQlkqfQRITGIVEKPKpeDAP 198
Cdd:COG0448 114 DPDYVLILSGDHIykmD-----YRQMLDFHIESGADItVACIEVPREEASRFGVMEVdED----GRITEFEEKPK--DPK 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578651 199 SNLAVVGRYILTPRIF-DLLTglpRGAGNEIQ--LTDGIAKLLDHEFVLAHPFEG 250
Cdd:COG0448 183 SALASMGIYVFNKDVLiELLE---EDAPNSSHdfGKDIIPRLLDRGKVYAYEFDG 234
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
12-203 |
1.74e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 42.62 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFLPATkanPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedHfdkayeletklemrHKDKLLEHVR 91
Cdd:PRK14352 12 AGAGTRMRSDT---PKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVG--------H--------------DRERVAPAVA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 92 NILPPNITCLyirQAEALGLGHAVLCARAAIGDEPFA--VILADD--LIDApkGALKQMVEVYGRSGNSILGVETVEPSQ 167
Cdd:PRK14352 67 ELAPEVDIAV---QDEQPGTGHAVQCALEALPADFDGtvVVTAGDvpLLDG--ETLADLVATHTAEGNAVTVLTTTLDDP 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 1067578651 168 TGsYG-IVETEQlkqfQRITGIVEKpkpEDA-PSNLAV 203
Cdd:PRK14352 142 TG-YGrILRDQD----GEVTAIVEQ---KDAtPSQRAI 171
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
15-70 |
2.17e-04 |
|
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: 41.44 E-value: 2.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578651 15 GTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDK 70
Cdd:cd04197 11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEK 66
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
8-137 |
5.82e-04 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 40.31 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 8 VFPVAGMGTRFLPATKANPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTgrnkrsIEDHFDKaYELETKLEMRHKdkll 87
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC------RDEHNTK-FHLDESLKLLAP---- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1067578651 88 eHVRNILPPNITclyirqaeaLGLGHAVLCARAAI-GDEPFAVILADDLID 137
Cdd:cd04183 71 -NATVVELDGET---------LGAACTVLLAADLIdNDDPLLIFNCDQIVE 111
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-158 |
1.79e-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: 38.33 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578651 12 AGMGTRFlpatkANPKEMLPIVDKPLIQYAVEEAveAGCTEMVFVTGRNKRSIEDHFDKAYELetklemrhkdkllehVR 91
Cdd:pfam12804 6 GGRSSRM-----GGDKALLPLGGKPLLERVLERL--RPAGDEVVVVANDEEVLAALAGLGVPV---------------VP 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578651 92 NILPpnitclyirqaeALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSIL 158
Cdd:pfam12804 64 DPDP------------GQGPLAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
|
|
| |
