|
Name |
Accession |
Description |
Interval |
E-value |
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-288 |
0e+00 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 554.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEQ 80
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 81 PSPDGLAQAFIIGEEFIGDDRVALILGDNIYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISIEEK 160
Cdd:COG1209 81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 161 PAVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGFAWLDTGTHESLLEAAQYIETV 240
Cdd:COG1209 161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 739728420 241 QRLQNAQVANLEEIAYRMGYITKEDVYQLAQSLKKNEYGQYLLRLIGE 288
Cdd:COG1209 241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
|
|
| rmlA |
TIGR01207 |
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ... |
2-285 |
0e+00 |
|
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130274 [Multi-domain] Cd Length: 286 Bit Score: 535.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEQP 81
Cdd:TIGR01207 1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 82 SPDGLAQAFIIGEEFIGDDRVALILGDNIYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISIEEKP 161
Cdd:TIGR01207 81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 162 AVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGFAWLDTGTHESLLEAAQYIETVQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 739728420 242 RLQNAQVANLEEIAYRMGYITKEDVYQLAQSLKKNEYGQYLLRL 285
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
1-240 |
2.47e-176 |
|
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: 485.93 E-value: 2.47e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEQ 80
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 81 PSPDGLAQAFIIGEEFIGDDRVALILGDNIYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISIEEK 160
Cdd:cd02538 81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 161 PAVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGFAWLDTGTHESLLEAAQYIETV 240
Cdd:cd02538 161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-286 |
3.88e-149 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 419.46 E-value: 3.88e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEQP 81
Cdd:PRK15480 5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 82 SPDGLAQAFIIGEEFIGDDRVALILGDNIYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISIEEKP 161
Cdd:PRK15480 85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 162 AVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGFAWLDTGTHESLLEAAQYIETVQ 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 739728420 242 RLQNAQVANLEEIAYRMGYITKEDVYQLAQSLKKNEYGQYLLRLI 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-238 |
1.41e-102 |
|
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: 299.55 E-value: 1.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDK-PMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEQ 80
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 81 PSPDGLAQAFIIGEEFIGDDRV-ALILGDNIYHGNGLTRMLQKAAAKE--KGATVFGYQVKDPERFGVVEFDDEMNAISI 157
Cdd:pfam00483 81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 158 EEKPAVPK-SHFAVTGLYFYDNDVVE-IAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGFAWLDTGTHESLLEAAQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240
|
...
gi 739728420 236 YIE 238
Cdd:pfam00483 241 FLL 243
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
1-237 |
1.23e-72 |
|
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: 222.83 E-value: 1.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDI-LIISTPKDLprFEELLGDGSEFGISLSYKE 79
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIgIVVGPTGEE--IKEALGDGSRFGVRITYIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 80 QPSPDGLAQAFIIGEEFIGDDRVALILGDNIYHGnGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEmNAISIEE 159
Cdd:cd04189 79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 160 KPAVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGD--LSVELMGrgfAWLDTGTHESLLEAAQYI 237
Cdd:cd04189 157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrvGYSIVTG---WWKDTGTPEDLLEANRLL 233
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-225 |
4.94e-64 |
|
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: 200.50 E-value: 4.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDlPRFEELLGDGSEFGISLSYKEQPS 82
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 83 PDGLAQAFIIGEEFIGDDRVALILGDNIYHGNgLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISIEEKPA 162
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739728420 163 VPKSHFAVTGLYFYDNDVVEIAKSIKPsaRGELEITDVNKAYLERGDLSVELMgrGFAWLDTG 225
Cdd:cd04181 159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-237 |
4.93e-61 |
|
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: 197.24 E-value: 4.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEQP 81
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 82 SPDGLAQAFIIGEEFIGDDRVALILGDNIYHGnGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISIEEKP 161
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739728420 162 AVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGFaWLDTGTHESLLEAAQYI 237
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-237 |
1.85e-48 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 165.46 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDlPRFEELLGDGSEFGISLSYKEQ 80
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 81 PSPDGLAQAFIIGEEFIgDDRVALILGDNIYHGNGLTRMLqkaaaKEKGATVFGYQVKDPERFGVVEFDDEmNAISIEEK 160
Cdd:TIGR03992 80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739728420 161 PAVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGRGfaWLDTGTHESLLEAAQYI 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-238 |
1.03e-45 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 154.16 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDIlIISTpKDLP-RFEELLGDGSEFGISLSYKEQ 80
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINV-GYLAeQIEEYFGDGSRFGVRITYVDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 81 PSP----DGLAQAfiigEEFIGDDRVALILGDNIYHGNgLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAIS 156
Cdd:COG1208 79 GEPlgtgGALKRA----LPLLGDEPFLVLNGDILTDLD-LAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 157 IEEKPAVPKSHFAVTGLYFYDNDVVEIAKsikpsARGELEITDVNKAYLERGDLSVELMgRGFaWLDTGTHESLLEAAQY 236
Cdd:COG1208 154 FVEKPEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANAL 226
|
..
gi 739728420 237 IE 238
Cdd:COG1208 227 LL 228
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-233 |
8.14e-30 |
|
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: 113.40 E-value: 8.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTP---------------------KDLP 59
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 60 RFEELLGDGSEfGISLSYKEQPSPDGLAQAFIIGEEFIGDDRVALILGDNIY--HGNGLTRMLQkaAAKEKGATVFGYQV 137
Cdd:cd02541 81 DLLEEVRIISD-LANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIdsKEPCLKQLIE--AYEKTGASVIAVEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 138 KDPE---RFGVVE-FDDEMNAISIE---EKPAV--PKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERG 208
Cdd:cd02541 158 VPPEdvsKYGIVKgEKIDGDVFKVKglvEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEE 237
|
250 260
....*....|....*....|....*.
gi 739728420 209 D-LSVELMGRgfaWLDTGTHESLLEA 233
Cdd:cd02541 238 PvYAYVFEGK---RYDCGNKLGYLKA 260
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-233 |
7.42e-25 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 100.49 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTP-KDL--------PRFEELL---GDGS 69
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgKRAiedhfdrsYELEATLeakGKEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 70 EF--------GISLSYKEQPSPDGLAQAFIIGEEFIGDDRVALILGDNIYHGN--GLTRMLQkaAAKEKGATVFGYQVKD 139
Cdd:COG1210 85 LLeevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQMIE--VYEETGGSVIAVQEVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 140 PE---RFGVV---EFDDEMNAIS-IEEKPAVPK--SHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNKAYLERGD- 209
Cdd:COG1210 163 PEevsKYGIVdgeEIEGGVYRVTgLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEPv 242
|
250 260
....*....|....*....|....
gi 739728420 210 LSVELMGRgfaWLDTGTHESLLEA 233
Cdd:COG1210 243 YAYEFEGK---RYDCGDKLGYLKA 263
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-233 |
9.23e-23 |
|
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: 93.39 E-value: 9.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILI--------IstpkdlprfEELLGDGSEFGISL 75
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLsvgylaeqI---------EEYFGDGYRGGIRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 76 SYKEQPSPDGLAQAFIIGEEFIGDDRVALILGDNIYHGNgLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAI 155
Cdd:cd06915 73 YYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 156 SIEEKPAVPKSHFAVTGLYFYDNDVVEIAKSIKPSargeLEiTDVNKAYLERGDLsvelmgRGFA----WLDTGTHESLL 231
Cdd:cd06915 152 AFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYA 220
|
..
gi 739728420 232 EA 233
Cdd:cd06915 221 RA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-233 |
1.14e-20 |
|
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: 87.95 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDIlIISTPKDLPRFEELLGDGSEFGISLSYKEQPSP 83
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 84 DGLAQAFIIGEEFIgDDRVALILGD---NIYHGNGLTRMLQKAAAKEKGATVFGYQVkdPerFGVVEFDDEmNAISIEEK 160
Cdd:cd06426 81 LGTAGALSLLPEKP-TDPFLVMNGDiltNLNYEHLLDFHKENNADATVCVREYEVQV--P--YGVVETEGG-RITSIEEK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739728420 161 PAVpkSHFAVTGLYFYDNDVVEiakSIKPSARgeLEITDVNKAYLERGDLSVELMGRGFaWLDTGTHESLLEA 233
Cdd:cd06426 155 PTH--SFLVNAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-236 |
3.78e-18 |
|
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: 81.10 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRD-ILIIS-TPKDLPRFEELLGDgsEFGISLSYK 78
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 79 EQPSPDGLAQAFIIGEEFIGDDRVA-LILGDNIYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAI-S 156
Cdd:cd06425 79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIeR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 157 IEEKPAVPKSHFAVTGLYFYDNDV--------VEIAKSIKP--SARGELEITDVNkaylergdlsvelmgrGFaWLDTGT 226
Cdd:cd06425 159 FVEKPKVFVGNKINAGIYILNPSVldriplrpTSIEKEIFPkmASEGQLYAYELP----------------GF-WMDIGQ 221
|
250
....*....|
gi 739728420 227 HESLLEAAQY 236
Cdd:cd06425 222 PKDFLKGMSL 231
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-180 |
5.28e-17 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 80.12 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGGSGTRLYPLT--RAaskqlmpiydKPMIYY---------PLSTLMLAGIRDILIIsTPKdlpRFEEL---LGDG 68
Cdd:COG0448 4 AIILAGGRGSRLGPLTkdRA----------KPAVPFggkyriidfPLSNCVNSGIRRVGVL-TQY---KSHSLndhIGSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 69 SEFGIS--------LSYKEQPSPD----GLAQAFIIGEEFIGDDRV--ALIL-GDNIYHGNgLTRMLQkaAAKEKGA--T 131
Cdd:COG0448 70 KPWDLDrkrggvfiLPPYQQREGEdwyqGTADAVYQNLDFIERSDPdyVLILsGDHIYKMD-YRQMLD--FHIESGAdiT 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739728420 132 VFGYQV--KDPERFGVVEFDDEMNAISIEEKPAVPKSHFAVTGLYFYDNDV 180
Cdd:COG0448 147 VACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
1-58 |
9.27e-16 |
|
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: 74.23 E-value: 9.27e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIIsTPKDL 58
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVV-VPEEE 57
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
2-233 |
2.38e-15 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 73.37 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILI-ISTPKDlpRFEELLGDgSEFGISLSYKEQ 80
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVnTHHLAD--QIEAHLGD-SRFGLRITISDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 81 P-----SPDGLAQAfiigEEFIGDDRVALILGDnIYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFD-DEMNA 154
Cdd:cd06422 78 PdelleTGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSlDADGR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739728420 155 ISIEEKPAVPKSHFavTGLYFYDNDVVEiakSIKPsarGELEITDVNKAYLERGDLSVELMgRGFaWLDTGTHESLLEA 233
Cdd:cd06422 153 LRRGGGGAVAPFTF--TGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-199 |
7.46e-13 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 67.62 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIIS------------TPKDLPRFEE------ 63
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEAMLEkrvkrq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 64 LLGDGSEF---GISLSYKEQPSPDGLAQAFIIGEEFIGDDRVALILGDNI---YHGN----GLTRMLQKaaAKEKGAT-V 132
Cdd:PRK13389 90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeYESDlsqdNLAEMIRR--FDETGHSqI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739728420 133 FGYQVKDPERFGVVEFD-------DEMNAISIEEKPA--VPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITD 199
Cdd:PRK13389 168 MVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-52 |
6.08e-12 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 63.43 E-value: 6.08e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILII 52
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-215 |
3.62e-11 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 62.60 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIIS------------TPKDLPRFEE----- 63
Cdd:PRK10122 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLLEqrvkr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 64 -LLGDGSEF---GISLSYKEQPSPDGLAQAFIIGEEFIGDDRVALILGDNIYHGNGLTRMLQKAAA-----KEKG-ATVF 133
Cdd:PRK10122 84 qLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAmiarfNETGrSQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 134 GYQVK-DPERFGVVEFDDEMNA-------ISIEEKPAVPK---SHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVNK 202
Cdd:PRK10122 164 AKRMPgDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250
....*....|...
gi 739728420 203 AYLERGDLSVELM 215
Cdd:PRK10122 244 ELAKKQSVDAMLM 256
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-233 |
4.17e-11 |
|
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: 61.48 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDlPRFEELLGDgsEFGISLSYKEQPSP 83
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKK--YPNIKFVYNPDYAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 84 DGLAQAFIIGEEFIGDDrVALILGDNIYHGNGLTRMLqkaAAKEKGATVfgYQVKDPE---RFGVVeFDDEMNAISIEEK 160
Cdd:cd02523 79 TNNIYSLYLARDFLDED-FLLLEGDVVFDPSILERLL---SSPADNAIL--VDKKTKEwedEYVKD-LDDAGVLLGIISK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739728420 161 PAVPKS-HFAVTGLYFYDND----VVEIAKSIKPSARGELEITDVNKAYLERGDLSVELMGrGFAWLDTGTHESLLEA 233
Cdd:cd02523 152 AKNLEEiQGEYVGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-233 |
3.89e-10 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 59.88 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAASKQLMPIYDK-PMIYYPLSTLMLAGIRDILIISTPKDLprfeEL---LGDGSEFGIS-- 74
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPL----ELnnhIGIGSPWDLDri 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 75 ------LS-YKEQPSPD---GLAQAFIIGEEFIG--DDRVALIL-GDNIYHGNgLTRMLQKAAAKEKGATVFGYQV--KD 139
Cdd:PRK05293 80 nggvtiLPpYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIYKMD-YDKMLDYHKEKEADVTIAVIEVpwEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 140 PERFGVVEFDDEMNAISIEEKPAVPKSHFAVTGLYFYDNDVVEiaKSIKPSARGELEITDVNK----AYLERGDLSVELM 215
Cdd:PRK05293 159 ASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLK--EYLIEDEKNPNSSHDFGKnvipLYLEEGEKLYAYP 236
|
250
....*....|....*...
gi 739728420 216 GRGFaWLDTGTHESLLEA 233
Cdd:PRK05293 237 FKGY-WKDVGTIESLWEA 253
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-200 |
6.36e-10 |
|
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: 57.91 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLYpltRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIIsTPKDLPRFEELLGDgsefgISLSYKEQPSP 83
Cdd:cd02540 2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNVEFVLQEEQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 84 DGLAQAFIIGEEFIGD--DRVALILGDN--IyHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAISI-E 158
Cdd:cd02540 73 LGTGHAVKQALPALKDfeGDVLVLYGDVplI-TPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIvE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739728420 159 EKPAVP---KSHFAVTGLYFYDNDVVEIA-KSIKPS-ARGELEITDV 200
Cdd:cd02540 152 EKDATEeekAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
2-52 |
2.18e-09 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 56.40 E-value: 2.18e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 739728420 2 KGIILAGGSGTRLYPLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILII 52
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-180 |
7.09e-09 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 56.00 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLYPLT--RAaskqlmpiydKPMIYY---------PLSTLMLAGIRDILII------STPKDLPR----FE 62
Cdd:PRK00725 19 LILAGGRGSRLKELTdkRA----------KPAVYFggkfriidfALSNCINSGIRRIGVLtqykahSLIRHIQRgwsfFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 63 ELLGdgsEFGISLSYKEQPSPD----GLAQAF-----IIGEEfigDDRVALIL-GDNIYHGNgLTRMLqkAAAKEKGA-- 130
Cdd:PRK00725 89 EELG---EFVDLLPAQQRVDEEnwyrGTADAVyqnldIIRRY---DPKYVVILaGDHIYKMD-YSRML--ADHVESGAdc 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739728420 131 TVFGYQV--KDPERFGVVEFDDEMNAISIEEKPAVPKS-------HFAVTGLYFYDNDV 180
Cdd:PRK00725 160 TVACLEVprEEASAFGVMAVDENDRITAFVEKPANPPAmpgdpdkSLASMGIYVFNADY 218
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-132 |
2.15e-08 |
|
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.
Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 53.32 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGGSGTRLYPLTRAASKQLMPI---YDkpMIYYPLSTLMLAGIRDILII------STPKDLPRFEELLGDGSEFGI 73
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLtqyksrSLNDHLGSGKEWDLDRKNGGL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739728420 74 SLSYKEQ-PSPD---GLAQAFIIGEEFIGDDRV--ALIL-GDNIYHGNgLTRMLQKAAAKEKGATV 132
Cdd:cd02508 79 FILPPQQrKGGDwyrGTADAIYQNLDYIERSDPeyVLILsGDHIYNMD-YREMLDFHIESGADITV 143
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-180 |
2.80e-08 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 54.06 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGGSGTRLYPLTRAASKQLMP---IYDkpMIYYPLSTLMLAGIRDILIIStpkdlprfeellgdgsefgislSYKE 79
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLT----------------------QYKS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 80 QpSPD----------GLAQAFI--------IGEE--------------FIGDDR---VALILGDNIYHGNgLTRMLQKAA 124
Cdd:PRK00844 64 H-SLDrhisqtwrlsGLLGNYItpvpaqqrLGKRwylgsadaiyqslnLIEDEDpdyVVVFGADHVYRMD-PRQMVDFHI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739728420 125 AKEKGATVFGYQV--KDPERFGVVEFDDEMNAISIEEKPAVPKS-------HFAVTGLYFYDNDV 180
Cdd:PRK00844 142 ESGAGVTVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDA 206
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-232 |
6.71e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 53.23 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRL---YPltraasKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRfeELLGDGSEFGISlsy 77
Cdd:PRK14357 1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELVK--KLLPEWVKIFLQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 78 KEQPspdGLAQAFIIGEEFIGDDRVALIL-GDN--IYHgNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNA 154
Cdd:PRK14357 70 EEQL---GTAHAVMCARDFIEPGDDLLILyGDVplISE-NTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 155 IsIEEKPAVPKSHFAV---TGLYFYDND-VVEIAKSIKP-SARGELEITDVNKaYLER-----GDLSVELMG----RGFA 220
Cdd:PRK14357 146 I-VEDKDAPEEEKKIKeinTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAVN-FAEKvrvvkTEDLLEITGvntrIQLA 223
|
250
....*....|..
gi 739728420 221 WLDTGTHESLLE 232
Cdd:PRK14357 224 WLEKQLRMRILE 235
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-230 |
1.58e-07 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 51.42 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 1 MKGIILAGGSGTRLYPLTRAAS-KQLMPIY-DKPMIYYPLSTLM-LAGIRDILIIsTPKDLpRF---EELLGDGSEFGIS 74
Cdd:cd02509 1 IYPVILAGGSGTRLWPLSRESYpKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVV-TNEEY-RFlvrEQLPEGLPEENII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 75 LsykeQPSPDGLAQAFIIG----EEFIGDDRVA------LILGDNIYHgngltRMLQKA--AAKEKGATVFGYQVKDPE- 141
Cdd:cd02509 79 L----EPEGRNTAPAIALAalylAKRDPDAVLLvlpsdhLIEDVEAFL-----KAVKKAveAAEEGYLVTFGIKPTRPEt 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 142 RFGVVEFDD--EMNAISIE---EKP--AVPKSHFAvTGLYF-------------------YDNDVVEIAKSIKPSARGEL 195
Cdd:cd02509 150 GYGYIEAGEklGGGVYRVKrfvEKPdlETAKEYLE-SGNYLwnsgiflfraktfleelkkHAPDIYEALEKALAAAGTDD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 739728420 196 EITDVNKAYLERGDLSVE--LMGR---------GFAWLDTGTHESL 230
Cdd:cd02509 229 FLRLLEEAFAKIPSISIDyaVMEKtkkvavvpaDFGWSDLGSWDAL 274
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-216 |
1.67e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 52.05 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLyplTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGsefGISLSYKEQPSP 83
Cdd:PRK14355 7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG---DVSFALQEEQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 84 DGLAQAFIIGEEFIGDDRVALILGDN-IYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFG--VVEFDDEMNAIsIEEK 160
Cdd:PRK14355 81 TGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGriVRDADGRVLRI-VEEK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739728420 161 PAVPKSHFAV---TGLYFYDNDVVEIA-KSIK-PSARGELEITDVNKAYLERG--------DLSVELMG 216
Cdd:PRK14355 160 DATPEERSIRevnSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEGlrclafpvADPDEIMG 228
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
3-201 |
2.05e-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: 51.10 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGG--SGTRLYPLTRAASKQLMPIYDKPMIYYPLSTL-MLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKE 79
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 80 QPSPDGLAQAF-----IIGEEfiGDDRVALILGD-----------NIY--HGNGLTRMLQKAAAKEkgATVFGYQVKDPE 141
Cdd:cd06428 81 EYKPLGTAGGLyhfrdQILAG--NPSAFFVLNADvccdfplqellEFHkkHGASGTILGTEASREQ--ASNYGCIVEDPS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 142 RFGVVEFddemnaisiEEKPAVPKSHFAVTGLYFYDNDVVEIAKSIKPSARGELEITDVN 201
Cdd:cd06428 157 TGEVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDN 207
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-67 |
2.78e-07 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 50.13 E-value: 2.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739728420 4 IILAGGSGTRLyplTRAASKQLMPIYDKPMIYYPLSTLMLAG-IRDILIISTPKDLPRFEELLGD 67
Cdd:COG1211 1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-208 |
4.04e-07 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 50.75 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLyplTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIIStpkdlprfeellGDGSE------FGISLSY 77
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEqveaalQGSGVAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 78 KEQPSPDGLAQAFIIGEEFI--GDDRVALILGDN-IYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFG-VVEFDDEMN 153
Cdd:PRK14358 76 ARQEQQLGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGrIVRGADGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 154 AISIEEKPAVPKSHfAV----TGLYFYDNDVVEIAKSI-KPSARGELEITDVNKAYLERG 208
Cdd:PRK14358 156 ERIVEQKDATDAEK-AIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-209 |
8.33e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 49.83 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRL---YPltraasKQLMPIYDKPMIYYPLSTLMLAGIRDI-LIISTPKDLprFEELLGDGSEFGISlsyKE 79
Cdd:PRK14354 6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIvTVVGHGAEE--VKEVLGDRSEFALQ---EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 80 QPspdGLAQAFIIGEEFIGDDR--VALILGDN-IYHGNGLTRMLQKAAAKEKGATVFGYQVKDPERFGVVEFDDEMNAIS 156
Cdd:PRK14354 75 QL---GTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739728420 157 I-EEKPAVP---KSHFAVTGLYFYDNDV-VEIAKSIKP-SARGELEITDVNKAYLERGD 209
Cdd:PRK14354 152 IvEQKDATEeekQIKEINTGTYCFDNKAlFEALKKISNdNAQGEYYLTDVIEILKNEGE 210
|
|
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-52 |
9.91e-07 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 49.29 E-value: 9.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 739728420 1 MKGIILAGGSGTRLYPLTRAAS-KQLMPIY-DKPMIYyplSTLM----LAGIRDILII 52
Cdd:COG0836 3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ---QTVErlagLVPPENILVV 57
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-70 |
3.29e-06 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 47.13 E-value: 3.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739728420 4 IILAGGSGTRL---YPltraasKQLMPIYDKPMIYYPLSTLM-LAGIRDILIISTPKDLPRFEELLGDGSE 70
Cdd:cd02516 4 IILAAGSGSRMgadIP------KQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
4-65 |
4.52e-06 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 46.67 E-value: 4.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739728420 4 IILAGGSGTRLypltrAAS--KQLMPIYDKPMIYYPLSTLMLAG-IRDILIISTPKDLPRFEELL 65
Cdd:PRK00155 7 IIPAAGKGSRM-----GADrpKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-52 |
4.92e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 47.57 E-value: 4.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 739728420 3 GIILAGGSGTRLYPLTRAASKQLMPIYDK-PMIYYPLSTLMLAGIRDILII 52
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
3-52 |
8.16e-06 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 46.77 E-value: 8.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 739728420 3 GIILAGGSGTRLYPLTRAASKQLMPI---YDkpMIYYPLSTLMLAGIRDILII 52
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-200 |
1.04e-04 |
|
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: 43.48 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLY---PltraasKQLMPIYDKPMIYYPLSTLMLAGIRDILIIstpkdlprfeelLGDGSE------FGIS 74
Cdd:COG1207 6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEqvraalADLD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 75 LSYKEQPSPDGLAQAFIIGEEFI-GDDRVALILgdniyhgNG---------LTRMLQKAAAKEKGATVFGYQVKDPERFG 144
Cdd:COG1207 68 VEFVLQEEQLGTGHAVQQALPALpGDDGTVLVL-------YGdvpliraetLKALLAAHRAAGAAATVLTAELDDPTGYG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739728420 145 VVEFDDEMNAISI-EEKPAVPKSHfAV----TGLYFYDNDVVEIA-KSIKPS-ARGELEITDV 200
Cdd:COG1207 141 RIVRDEDGRVLRIvEEKDATEEQR-AIreinTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-200 |
1.84e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 42.79 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRLYpltRAASKQLMPIYDKPMIYYPLSTL---------MLAGIRDILIISTPKDLP-RF---EELLGDGSE 70
Cdd:PRK14356 9 LILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRALrplfgdnvwTVVGHRADMVRAAFPDEDaRFvlqEQQLGTGHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 71 FGISLsykeqpspDGLAQAfiigeefiGDDRVALILGDNIYHGNGLTRMLQKAAAKekgaTVFGY---QVKDPERFG-VV 146
Cdd:PRK14356 86 LQCAW--------PSLTAA--------GLDRVLVVNGDTPLVTTDTIDDFLKEAAG----ADLAFmtlTLPDPGAYGrVV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739728420 147 EFDDEMNAIsIEEKPAVPKSHFAVT-----GLYFYDNDVVE--IAKSIKPSARGELEITDV 200
Cdd:PRK14356 146 RRNGHVAAI-VEAKDYDEALHGPETgevnaGIYYLRLDAVEslLPRLTNANKSGEYYITDL 205
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-108 |
4.29e-04 |
|
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: 40.24 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGGSGTRLypltrAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDLPRFEELLGDGSEFGISLSYKEqps 82
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE--- 74
|
90 100
....*....|....*....|....*...
gi 739728420 83 pdGLAQAFIIGEEFIGD--DRVALILGD 108
Cdd:cd04182 75 --GMSSSLAAGLEALPAdaDAVLILLAD 100
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
6-65 |
5.29e-04 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 40.26 E-value: 5.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 6 LAGGSGTRLypltRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPKDlPRFEELL 65
Cdd:COG2266 1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNT-PKTREYL 55
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-201 |
8.53e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 40.62 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 4 IILAGGSGTRlypLTRAASKQLMPIYDKPMIYYPLSTLMLAGIRDILIISTPkDLPRFEELLGDGSEFGISLSYKEQPsp 83
Cdd:PRK14353 9 IILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAAAKIAPDAEIFVQKERL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739728420 84 dGLAQAFIIGEEFI--GDDRVALILGDN--IYHGNgLTRMLQKAAAKEkGATVFGYQVKDPERFG-VVEFDDEMNAIsIE 158
Cdd:PRK14353 83 -GTAHAVLAAREALagGYGDVLVLYGDTplITAET-LARLRERLADGA-DVVVLGFRAADPTGYGrLIVKGGRLVAI-VE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739728420 159 EKPAVPKSHfAVT----GLY----------------------FYDNDVVEIAKSIKPSAR----GELEITDVN 201
Cdd:PRK14353 159 EKDASDEER-AITlcnsGVMaadgadalalldrvgndnakgeYYLTDIVAIARAEGLRVAvveaPEDEVRGIN 230
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-66 |
1.31e-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: 38.71 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739728420 3 GIILAGGSGTRLypltrAASKQLMPIYDKPMIYYPLSTLMLAGiRDILIISTPKDLPRFEELLG 66
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG 58
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-64 |
2.22e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 38.25 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739728420 1 MKGIILAGGSGTRLypltrAASKQLMPIYDKPMIYYPLSTlmLAGIRDILIISTPKDlPRFEEL 64
Cdd:COG0746 5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP-ERYAAL 60
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-52 |
2.56e-03 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 38.22 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 739728420 3 GIILAGGSGTRLypltrAASKQLMPIYDKPMIYYPLSTLMLAGIRDILII 52
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
1-64 |
2.85e-03 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 37.86 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739728420 1 MKGIILAGGSGTRLypltRAASKQLMPIYDKPMIYYPLSTlmLAGIRDILIISTPKDLPRFEEL 64
Cdd:PRK00317 4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIER--LAPQVDEIVINANRNLARYAAF 61
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
1-64 |
5.15e-03 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 37.17 E-value: 5.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739728420 1 MKGIILAGGSGTRLypltrAASKQLMPIYDKPMIYYPLSTlmLAGIRDILIISTPKDLPRFEEL 64
Cdd:cd02503 1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLER--LKPLVDEVVISANRDQERYALL 57
|
|
| |
