|
Name |
Accession |
Description |
Interval |
E-value |
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-289 |
0e+00 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 562.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLLGDGSEFGIKLSYAEQ 80
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSPDGLAQAFIIGADFIGDDHVALILGDNIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAISIEEK 160
Cdd:COG1209 81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 161 PEQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEAAQYIETV 240
Cdd:COG1209 161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489115363 241 QRMQNVQVANLEEIAYRMGYITKEQVHDLAQSLKKNEYGHYLLRLIGEE 289
Cdd:COG1209 241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
|
|
| 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: 538.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLLGDGSEFGIKLSYAEQP 81
Cdd:TIGR01207 1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 82 SPDGLAQAFIIGADFIGDDHVALILGDNIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAISIEEKP 161
Cdd:TIGR01207 81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 162 EQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEAAQYIETVQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489115363 242 RMQNVQVANLEEIAYRMGYITKEQVHDLAQSLKKNEYGHYLLRL 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 |
9.74e-177 |
|
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: 487.08 E-value: 9.74e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLLGDGSEFGIKLSYAEQ 80
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSPDGLAQAFIIGADFIGDDHVALILGDNIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAISIEEK 160
Cdd:cd02538 81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 161 PEQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEAAQYIETV 240
Cdd:cd02538 161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-286 |
7.25e-149 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 418.69 E-value: 7.25e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLLGDGSEFGIKLSYAEQP 81
Cdd:PRK15480 5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 82 SPDGLAQAFIIGADFIGDDHVALILGDNIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAISIEEKP 161
Cdd:PRK15480 85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 162 EQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEAAQYIETVQ 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489115363 242 RMQNVQVANLEEIAYRMGYITKEQVHDLAQSLKKNEYGHYLLRLI 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-238 |
1.08e-105 |
|
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: 307.26 E-value: 1.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDK-PMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLLGDGSEFGIKLSYAEQ 80
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSPDGLAQAFIIGADFIGDDHV-ALILGDNIYHGPGLSKMLQKAASKE--KGATVFGYQVKDPERFGVVEFDDNMNAISI 157
Cdd:pfam00483 81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 158 EEKPEQPR-SNYAVTGLYFYDNDVVE-IAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEAAQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240
|
...
gi 489115363 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 |
2.61e-75 |
|
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: 229.76 E-value: 2.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDlPRFEDLLGDGSEFGIKLSYAEQ 80
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSPDGLAQAFIIGADFIGDDHVALILGDNIYHGpGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNmNAISIEEK 160
Cdd:cd04189 80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115363 161 PEQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGD--LSVELMGrgfAWLDTGTHESLLEAAQYI 237
Cdd:cd04189 158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrvGYSIVTG---WWKDTGTPEDLLEANRLL 233
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-237 |
2.22e-65 |
|
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: 208.41 E-value: 2.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLLGDGSEFGIKLSYAEQP 81
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 82 SPDGLAQAFIIGADFIGDDHVALILGDNIYHGpGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAISIEEKP 161
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115363 162 EQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFaWLDTGTHESLLEAAQYI 237
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-225 |
8.06e-65 |
|
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: 202.43 E-value: 8.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPtDLPRFEDLLGDGSEFGIKLSYAEQPS 82
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY-LGEQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 83 PDGLAQAFIIGADFIGDDHVALILGDNIYHgPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAISIEEKPE 162
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTD-LDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115363 163 QPRSNYAVTGLYFYDNDVVEIAKNIKpsPRGELEITDVNKAYLDRGDLSVELMgrGFAWLDTG 225
Cdd:cd04181 159 LPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-237 |
1.24e-51 |
|
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: 173.93 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDlPRFEDLLGDGSEFGIKLSYAEQ 80
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSPDGLAQAFIIGADFIgDDHVALILGDNIYHGPGLSKMLqkaasKEKGATVFGYQVKDPERFGVVEFDDNmNAISIEEK 160
Cdd:TIGR03992 80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115363 161 PEQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGRGfaWLDTGTHESLLEAAQYI 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-238 |
6.32e-48 |
|
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: 159.55 E-value: 6.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDIlIISTPtDLP-RFEDLLGDGSEFGIKLSYAEQ 80
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVG-YLAeQIEEYFGDGSRFGVRITYVDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSP----DGLAQAfiigADFIGDDHVALILGDNIYhGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAIS 156
Cdd:COG1208 79 GEPlgtgGALKRA----LPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 157 IEEKPEQPRSNYAVTGLYFYDNDVVEIAknikpsPRGE-LEITDVNKAYLDRGDLSVELMgRGFaWLDTGTHESLLEAAQ 235
Cdd:COG1208 154 FVEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANA 225
|
...
gi 489115363 236 YIE 238
Cdd:COG1208 226 LLL 228
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-233 |
5.09e-32 |
|
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: 119.17 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPT------------DLPRF------E 62
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfdrsyELEETlekkgkT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 63 DLLGDGSEF--GIKLSYAEQPSPDGLAQAFIIGADFIGDDHVALILGDNIY--HGPGLSKMLQkaASKEKGATVFGYQVK 138
Cdd:cd02541 81 DLLEEVRIIsdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIdsKEPCLKQLIE--AYEKTGASVIAVEEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 139 DPE---RFGVV---EFDDNMNAIS-IEEKP--EQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGD 209
Cdd:cd02541 159 PPEdvsKYGIVkgeKIDGDVFKVKgLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238
|
250 260
....*....|....*....|....*
gi 489115363 210 -LSVELMGRgfaWLDTGTHESLLEA 233
Cdd:cd02541 239 vYAYVFEGK---RYDCGNKLGYLKA 260
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-233 |
2.13e-26 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 104.73 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPT--------DL-PRFEDLL---GDGS 69
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGkraiedhfDRsYELEATLeakGKEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 70 EF--------GIKLSYAEQPSPDGLAQAFIIGADFIGDDHVALILGDNIYHG--PGLSKMLQkaASKEKGATVFGYQVKD 139
Cdd:COG1210 85 LLeevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSekPCLKQMIE--VYEETGGSVIAVQEVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 140 PE---RFGVV---EFDDNMNAIS-IEEKP--EQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGD- 209
Cdd:COG1210 163 PEevsKYGIVdgeEIEGGVYRVTgLVEKPapEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEPv 242
|
250 260
....*....|....*....|....
gi 489115363 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 |
1.84e-25 |
|
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: 100.71 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILI--------IstptdlprfEDLLGDGSEFGIKL 75
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLsvgylaeqI---------EEYFGDGYRGGIRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 76 SYAEQPSPDGLAQAFIIGADFIGDDHVALILGDNIYHGpGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAI 155
Cdd:cd06915 73 YYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 156 SIEEKPEQPRSNYAVTGLYFYDNDVVEIAKNIKPSprgeLEiTDVNKAYLDRGDLsvelmgRGFA----WLDTGTHESLL 231
Cdd:cd06915 152 AFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYA 220
|
..
gi 489115363 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 |
2.52e-21 |
|
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: 89.49 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDIlIISTPTDLPRFEDLLGDGSEFGIKLSYAEQPSP 83
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 84 DGLAQAFIIGADFIgDDHVALILGDnIYHGPGLSKMLQKAASKEKGATVFG--YQVKDPerFGVVEFDDNmNAISIEEKP 161
Cdd:cd06426 81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEGG-RITSIEEKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115363 162 EQprsNYAV-TGLYFYDNDVVE-IAKNIKpsprgeLEITDVNKAYLDRGDLSVELMGRGFaWLDTGTHESLLEA 233
Cdd:cd06426 156 TH---SFLVnAGIYVLEPEVLDlIPKNEF------FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-208 |
6.46e-21 |
|
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: 88.81 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKD-ILIIS-TPTDLPRFEDLLGDgsEFGIKLSYA 78
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 79 EQPSPDGLAQAFIIGADFIGDDHVALIL--GDNIYHGPgLSKMLQ--KAASKEkgATVFGYQVKDPERFGVVEFDDNMNA 154
Cdd:cd06425 79 IETEPLGTAGPLALARDLLGDDDEPFFVlnSDVICDFP-LAELLDfhKKHGAE--GTILVTKVEDPSKYGVVVHDENTGR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115363 155 I-SIEEKPEQPRSNYAVTGLYFYDNDV--------VEIAKNIKP--SPRGELEITDVNKAYLDRG 208
Cdd:cd06425 156 IeRFVEKPKVFVGNKINAGIYILNPSVldriplrpTSIEKEIFPkmASEGQLYAYELPGFWMDIG 220
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-180 |
2.86e-18 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 83.59 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLYPLT--RAaskqlmpvydKPMIYY---------PLSTLMLAGIKDILIistptdLPRFE-----DLLG 66
Cdd:COG0448 4 AIILAGGRGSRLGPLTkdRA----------KPAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKshslnDHIG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 67 DGSE--FGIKLSY-----AEQPSPD-----GLAQAFIIGADFIGD---DHVaLIL-GDNIYHGPgLSKMLQkaASKEKGA 130
Cdd:COG0448 68 SGKPwdLDRKRGGvfilpPYQQREGedwyqGTADAVYQNLDFIERsdpDYV-LILsGDHIYKMD-YRQMLD--FHIESGA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489115363 131 --TVFGYQV--KDPERFGVVEFDDNMNAISIEEKPEQPRSNYAVTGLYFYDNDV 180
Cdd:COG0448 144 diTVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
1-153 |
2.83e-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: 75.77 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRFEDLL-GDGSEFGIKLSYAE 79
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLrSFPLNLKQKLDEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 80 QPS--PDGLAQA------------FIIGADFIGDDHVALILGDNIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFgV 145
Cdd:cd04198 81 IVLdeDMGTADSlrhirkkikkdfLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERD-V 159
|
....*...
gi 489115363 146 VEFDDNMN 153
Cdd:cd04198 160 IGLDEKTQ 167
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
2-233 |
2.08e-14 |
|
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: 70.68 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDIlIISTpTDLP-RFEDLLGDgSEFGIKLSYAEQ 80
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNT-HHLAdQIEAHLGD-SRFGLRITISDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 P-----SPDGLAQAfiigADFIGDDHVALILGDnIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFD-DNMNA 154
Cdd:cd06422 78 PdelleTGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSlDADGR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115363 155 ISIEEKPEQPRsnYAVTGLYFYDNDVVEiakNIKPSPrgeLEITDVNKAYLDRGDLSVELMgRGFaWLDTGTHESLLEA 233
Cdd:cd06422 153 LRRGGGGAVAP--FTFTGIQILSPELFA---GIPPGK---FSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-233 |
5.09e-13 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 68.36 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDK-PMIYYPLSTLMLAGIKDILIIST--PTDLPRFedlLGDGSEFG----- 72
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQyqPLELNNH---IGIGSPWDldrin 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 73 ----IKLSYAEQPSPD---GLAQAFIIGADFIG--DDHVALIL-GDNIYHgPGLSKMLQKAASKEKGATVFGYQV--KDP 140
Cdd:PRK05293 81 ggvtILPPYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIYK-MDYDKMLDYHKEKEADVTIAVIEVpwEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 141 ERFGVVEFDDNMNAISIEEKPEQPRSNYAVTGLYFY---------------DNDVVEIAKNIKPSprgeleitdvnkaYL 205
Cdd:PRK05293 160 SRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL-------------YL 226
|
250 260
....*....|....*....|....*...
gi 489115363 206 DRGDLSVELMGRGFaWLDTGTHESLLEA 233
Cdd:PRK05293 227 EEGEKLYAYPFKGY-WKDVGTIESLWEA 253
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-160 |
1.49e-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: 65.35 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTdlprFEDLLgdgsEFGIKLSYAEQ 80
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEH----SQAII----EHLLKSKWSSL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 81 PSPDGLAQAFIIGADFIGD-----DHVALILGD----------NIYhgpgLSKMLQKAASKEKGA----TVFgyQVKDPE 141
Cdd:cd02507 73 SSKMIVDVITSDLCESAGDalrlrDIRGLIRSDflllscdlvsNIP----LSELLEERRKKDKNAiatlTVL--LASPPV 146
|
170
....*....|....*....
gi 489115363 142 RFGVVEFDDNMNAISIEEK 160
Cdd:cd02507 147 STEQSKKTEEEDVIAVDSK 165
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-199 |
1.88e-12 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 66.08 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIIsTPTDLPRFEDLLGDGSEF---------- 71
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELeamlekrvkr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 72 ------------GIKLSYAEQPSPDGLAQAFIIGADFIGDDHVALILGDNI-------YHGPGLSKMLQKAasKEKGAT- 131
Cdd:PRK13389 89 qlldevqsicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdLSQDNLAEMIRRF--DETGHSq 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115363 132 VFGYQVKDPERFGVVEFD-------DNMNAISIEEKP--EQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITD 199
Cdd:PRK13389 167 IMVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-199 |
3.46e-12 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 65.29 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIIS------------TPTDLPRF------E 62
Cdd:PRK10122 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 63 DLLGDGSEF---GIKLSYAEQPSPDGLAQAFIIGADFIGDDHVALILGDNIYHGP-------GLSKMLQKAASKEKGATV 132
Cdd:PRK10122 84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplryNLAAMIARFNETGRSQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115363 133 FGYQVKDPERFGVVEFDDNMNA-------ISIEEKPEQPR---SNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITD 199
Cdd:PRK10122 164 AKRMPGDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-233 |
2.86e-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: 61.86 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILII----STptdlpRFEDLLGDgsEFGIKLSYAE 79
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVtgykKE-----QIEELLKK--YPNIKFVYNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 80 QPSPDGLAQAFIIGADFIGDDhVALILGDNIYHgpglSKMLQKAASKEKGATVFGYQVKDPERFGVVE-FDDNMNAISIE 158
Cdd:cd02523 75 DYAETNNIYSLYLARDFLDED-FLLLEGDVVFD----PSILERLLSSPADNAILVDKKTKEWEDEYVKdLDDAGVLLGII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 159 EKPEQPRSNYAVT-GLYFYDND----VVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVELMGrGFAWLDTGTHESLLEA 233
Cdd:cd02523 150 SKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-200 |
2.05e-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: 59.45 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLYpltRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIIstptdlprfedlLGDGSEF------GIKLSY 77
Cdd:cd02540 2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEQvkkalaNPNVEF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 78 AEQPSPDGLAQAFIIGADFIGDDH-VALIL-GDNiyhgP-----GLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDD 150
Cdd:cd02540 67 VLQEEQLGTGHAVKQALPALKDFEgDVLVLyGDV----PlitpeTLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489115363 151 NMNAISI-EEK---PEQPRSNYAVTGLYFYDNDVVEIA-KNIKPSP-RGELEITDV 200
Cdd:cd02540 143 NGKVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI 198
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-132 |
3.24e-10 |
|
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: 58.32 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLYPLTRAASKQLMPV---YDkpMIYYPLSTLMLAGIKDILII------STPTDLPRFEDLLGDGSEFGI 73
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLtqyksrSLNDHLGSGKEWDLDRKNGGL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115363 74 KLSYAEQ-PSPD---GLAQAFIIGADFIGD---DHVALILGDNIYHGPgLSKMLQKAasKEKGATV 132
Cdd:cd02508 79 FILPPQQrKGGDwyrGTADAIYQNLDYIERsdpEYVLILSGDHIYNMD-YREMLDFH--IESGADI 141
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
3-213 |
6.18e-10 |
|
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: 58.42 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGG--SGTRLYPLTRAASKQLMPVYDKPMIYYPLSTL-MLAGIKDILIISTPTDLPrFEDLLGDGS-EFGIKLSYA 78
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQqEFNVPIRYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 79 EQPSPDGLAQA----------------FIIGADFIGDDHVALILGDNIYHGpGLSKMLQKAASKEKgATVFGYQVKDPER 142
Cdd:cd06428 80 QEYKPLGTAGGlyhfrdqilagnpsafFVLNADVCCDFPLQELLEFHKKHG-ASGTILGTEASREQ-ASNYGCIVEDPST 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115363 143 FGVVEFddnmnaisiEEKPEQPRSNYAVTGLYFYDNDVVEIAKNIKPSPRGELEITDVNKAYLDRGDLSVE 213
Cdd:cd06428 158 GEVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
2-52 |
1.98e-09 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 56.79 E-value: 1.98e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489115363 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILII 52
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-164 |
1.03e-08 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 55.62 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLYPLT--RAaskqlmpvydKPMIYY---------PLSTLMLAGIKDILIIST-----------------P 55
Cdd:PRK00725 19 LILAGGRGSRLKELTdkRA----------KPAVYFggkfriidfALSNCINSGIRRIGVLTQykahslirhiqrgwsffR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 56 TDLPRFEDLLGdgsefgiklsyAEQPSPD-----GLAQAFIIGADFIGD---DHVALILGDNIYHgPGLSKMLqkAASKE 127
Cdd:PRK00725 89 EELGEFVDLLP-----------AQQRVDEenwyrGTADAVYQNLDIIRRydpKYVVILAGDHIYK-MDYSRML--ADHVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489115363 128 KGA--TVFGYQV--KDPERFGVVEFDDNMNAISIEEKPEQP 164
Cdd:PRK00725 155 SGAdcTVACLEVprEEASAFGVMAVDENDRITAFVEKPANP 195
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-208 |
1.30e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 55.37 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLyplTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIIStptdlprfedllGDGSE------FGIKLSY 77
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEqveaalQGSGVAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 78 AEQPSPDGLAQAFIIGADFI--GDDHVALILGDNIYHGPGLSKMLQKAASKEKGA-TVFGYQVKDPERFGVVEFDDNMNA 154
Cdd:PRK14358 76 ARQEQQLGTGDAFLSGASALteGDADILVLYGDTPLLRPDTLRALVADHRAQGSAmTILTGELPDATGYGRIVRGADGAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489115363 155 ISIEEKPEQPRSNYAV----TGLYFYDNDVVEIAKNI-KPSPRGELEITDVNKAYLDRG 208
Cdd:PRK14358 156 ERIVEQKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-180 |
4.06e-08 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 53.68 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLYPLTRAASKQLMP---VYDkpMIYYPLSTLMLAGIKDILI------------ISTPTdlpRFEDLLGd 67
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhISQTW---RLSGLLG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 68 gsefgiklSYAEqPSP----------DGLAQAFIIGADFIGD---DHVALILGDNIYHgPGLSKMLQKAASKEKGATVFG 134
Cdd:PRK00844 82 --------NYIT-PVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHVYR-MDPRQMVDFHIESGAGVTVAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489115363 135 YQV--KDPERFGVVEFDDNMNAISIEEKPEQPRS-------NYAVTGLYFYDNDV 180
Cdd:PRK00844 152 IRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDA 206
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-209 |
8.61e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 52.91 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRL---YPltraasKQLMPVYDKPMIYYPLSTLMLAGIKDI-LIISTPTDLprFEDLLGDGSEFGIKlsyAE 79
Cdd:PRK14354 6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIvTVVGHGAEE--VKEVLGDRSEFALQ---EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 80 QPspdGLAQAFIIGADFIGDD--HVALILGDN-IYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNAIS 156
Cdd:PRK14354 75 QL---GTGHAVMQAEEFLADKegTTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489115363 157 I-EEK---PEQPRSNYAVTGLYFYDNDV-VEIAKNIKP-SPRGELEITDVNKAYLDRGD 209
Cdd:PRK14354 152 IvEQKdatEEEKQIKEINTGTYCFDNKAlFEALKKISNdNAQGEYYLTDVIEILKNEGE 210
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-52 |
2.06e-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: 51.04 E-value: 2.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489115363 1 MKGIILAGGSGTRLYPLTRAAS-KQLMPVY-DKPMIYYPLSTLM-LAGIKDILII 52
Cdd:cd02509 1 IYPVILAGGSGTRLWPLSRESYpKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVV 55
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-67 |
4.88e-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: 49.36 E-value: 4.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115363 4 IILAGGSGTRlypLTRAASKQLMPVYDKPMIYYPLSTLMLAG-IKDILIISTPTDLPRFEDLLGD 67
Cdd:COG1211 1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
|
|
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-52 |
1.36e-06 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 48.91 E-value: 1.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489115363 1 MKGIILAGGSGTRLYPLTRAAS-KQLMPVY-DKPMIYyplSTLM----LAGIKDILII 52
Cdd:COG0836 3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ---QTVErlagLVPPENILVV 57
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-200 |
2.63e-06 |
|
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: 48.10 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLY---PltraasKQLMPVYDKPMIYYPLSTLMLAGIKDILIIstptdlprfedlLGDGSE------FGIK 74
Cdd:COG1207 6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEqvraalADLD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 75 LSYAEQPSPDGLAQAFIIGADFIG--DDHVaLIL-GDNiyhgP-----GLSKMLQKAASKEKGATVFGYQVKDPERFGVV 146
Cdd:COG1207 68 VEFVLQEEQLGTGHAVQQALPALPgdDGTV-LVLyGDV----PliraeTLKALLAAHRAAGAAATVLTAELDDPTGYGRI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115363 147 EFDDNMNAISI-EEK---PEQpRSNYAV-TGLYFYDNDVVEIA-KNIKPS-PRGELEITDV 200
Cdd:COG1207 143 VRDEDGRVLRIvEEKdatEEQ-RAIREInTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-200 |
4.54e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 47.45 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 1 MKGIILAGGSGTRL---YPltraasKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDLPRfeDLLGDGSEFgiklsy 77
Cdd:PRK14357 1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELVK--KLLPEWVKI------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 78 AEQPSPDGLAQAFIIGADFIGDDHVALIL-GDN--IYHGPgLSKMLQKAASKEKGATVFGYQVKDPERFGVVEFDDNMNA 154
Cdd:PRK14357 67 FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVplISENT-LKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489115363 155 IsIEEK--PEQPRSNYAV-TGLYFYDND-VVEIAKNIKP-SPRGELEITDV 200
Cdd:PRK14357 146 I-VEDKdaPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-161 |
5.63e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 47.19 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLYPLTRAASKQLMPVYDK-PMIYYPLSTLMLAGIKDILI------------ISTPTDLPRFedllGDGs 69
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVltqfnsaslnrhISQTYNFDGF----SGG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 70 eFgIKLSYAEQP--SPD---GLAQA------FIIGADFigdDHVaLIL-GDNIYHgPGLSKMLQKaaSKEKGA--TVFGY 135
Cdd:PRK02862 81 -F-VEVLAAQQTpeNPSwfqGTADAvrkylwHFQEWDV---DEY-LILsGDQLYR-MDYRLFVQH--HRETGAdiTLAVL 151
|
170 180
....*....|....*....|....*...
gi 489115363 136 QV--KDPERFGVVEFDDNMNAISIEEKP 161
Cdd:PRK02862 152 PVdeKDASGFGLMKTDDDGRITEFSEKP 179
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-70 |
7.35e-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: 45.98 E-value: 7.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115363 4 IILAGGSGTRL---YPltraasKQLMPVYDKPMIYYPLSTLM-LAGIKDILIISTPTDLPRFEDLLGDGSE 70
Cdd:cd02516 4 IILAAGSGSRMgadIP------KQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
4-65 |
1.34e-05 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 45.12 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115363 4 IILAGGSGTRLypltrAAS--KQLMPVYDKPMIYYPLSTLMLAG-IKDILIISTPTDLPRFEDLL 65
Cdd:PRK00155 7 IIPAAGKGSRM-----GADrpKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
3-52 |
7.48e-05 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 43.69 E-value: 7.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489115363 3 GIILAGGSGTRLYPLTRAASKQLMPV---YDkpMIYYPLSTLMLAGIKDILII 52
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-136 |
9.56e-05 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 42.46 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIIsTPtdlPRFEDLLGDGSEFGIKLSYAEQPS 82
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LG---ADAEEVAAALAGLGVRVVVNPDWE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115363 83 pDGLAQAFIIGADFIGD--DHVALILGDNiyhgPGLS-----KMLQKAASKEKGATVFGYQ 136
Cdd:COG2068 77 -EGMSSSLRAGLAALPAdaDAVLVLLGDQ----PLVTaetlrRLLAAFRESPASIVAPTYD 132
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-216 |
1.71e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 42.81 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRLyplTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDI-LIISTPTDLPRfEDLLGDGsefGIKLSYAEQPS 82
Cdd:PRK14355 7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIvLVVGHQAEKVR-EHFAGDG---DVSFALQEEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 83 PDGLAQAFIIGADFIGDDHVALILGDN-IYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFG--VVEFDDNMNAIsIEE 159
Cdd:PRK14355 80 GTGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGriVRDADGRVLRI-VEE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 160 K---PEQPRSNYAVTGLYFYDNDVVEIA-KNIK-PSPRGELEITDVNKAYLDRG--------DLSVELMG 216
Cdd:PRK14355 159 KdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEGlrclafpvADPDEIMG 228
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-141 |
2.00e-04 |
|
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: 41.03 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTlmLAGIKDILIISTPtdlprFEDLLGDGSEFGIKlsYAEQPS 82
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLER--LRPAGDEVVVVAN-----DEEVLAALAGLGVP--VVPDPD 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115363 83 PD-GLAQAFIIGADFIGD-DHVALILGDNIYHGPG-LSKMLQKAASKEKGATVFGYQVKDPE 141
Cdd:pfam12804 67 PGqGPLAGLLAALRAAPGaDAVLVLACDMPFLTPElLRRLLAAAEESGADIVVPVYDGGRGH 128
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-108 |
6.41e-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: 39.85 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 3 GIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPTDlPRFEDLLGDGSEFGIKLSYAEQps 82
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEA-DAVRAALAGLPVVVVINPDWEE-- 74
|
90 100
....*....|....*....|....*...
gi 489115363 83 pdGLAQAFIIGADFIGD--DHVALILGD 108
Cdd:cd04182 75 --GMSSSLAAGLEALPAdaDAVLILLAD 100
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
1-64 |
2.04e-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: 38.33 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115363 1 MKGIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTlmLAGIKDILIISTPTDLPRFEDL 64
Cdd:cd02503 1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLER--LKPLVDEVVISANRDQERYALL 57
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-160 |
2.66e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 39.07 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 4 IILAGGSGTRlypLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPtDLPRFEDLLGDgseFGIKLSYAEQPSP 83
Cdd:PRK14353 9 IILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAAAK---IAPDAEIFVQKER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 84 DGLAQAFIIGADFI--GDDHVALILGDNIYHGPGLSKMLQKAASKEKGATVFGYQVKDPERFG-VVEFDDNMNAIsIEEK 160
Cdd:PRK14353 82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrLIVKGGRLVAI-VEEK 160
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
6-65 |
4.12e-03 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 37.56 E-value: 4.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115363 6 LAGGSGTRLypltRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPtDLPRFEDLL 65
Cdd:COG2266 1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREYL 55
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-64 |
5.91e-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: 37.09 E-value: 5.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115363 1 MKGIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTlmLAGIKDILIISTPTDlPRFEDL 64
Cdd:COG0746 5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP-ERYAAL 60
|
|
| |
