|
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: 561.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAEQ 80
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 81 PSPDGLAQAFIIGEEFISDDSVALILGDNIYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEK 160
Cdd:COG1209 81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 161 PEQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEASQYIETV 240
Cdd:COG1209 161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1578096338 241 QRMQNVQVANLEEIAYRMGYISREDVLALAQPLKKNEYGQYLLRLIGE 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: 539.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAEQP 81
Cdd:TIGR01207 1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 82 SPDGLAQAFIIGEEFISDDSVALILGDNIYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEKP 161
Cdd:TIGR01207 81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 162 EQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEASQYIETVQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1578096338 242 RMQNVQVANLEEIAYRMGYISREDVLALAQPLKKNEYGQYLLRL 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 |
5.21e-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: 487.47 E-value: 5.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAEQ 80
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 81 PSPDGLAQAFIIGEEFISDDSVALILGDNIYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEK 160
Cdd:cd02538 81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 161 PEQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEASQYIETV 240
Cdd:cd02538 161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-286 |
1.04e-151 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 426.01 E-value: 1.04e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAEQP 81
Cdd:PRK15480 5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 82 SPDGLAQAFIIGEEFISDDSVALILGDNIYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEKP 161
Cdd:PRK15480 85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 162 EQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEASQYIETVQ 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1578096338 242 RMQNVQVANLEEIAYRMGYISREDVLALAQPLKKNEYGQYLLRLI 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-238 |
1.24e-104 |
|
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: 304.56 E-value: 1.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDK-PMIYYPLSTLMLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAEQ 80
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 81 PSPDGLAQAFIIGEEFISDDSV-ALILGDNIYHGSGLSKMLQKAASKES--GATVFGYHVKDPERFGVVEFDQDMKAISI 157
Cdd:pfam00483 81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 158 EEKPEQPR-SNYAVTGLYFYDNDVVE-IAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFAWLDTGTHESLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240
|
...
gi 1578096338 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 |
4.11e-76 |
|
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: 231.69 E-value: 4.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDlHRFQELLQDGSEFGLKLSYAEQ 80
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 81 PSPDGLAQAFIIGEEFISDDSVALILGDNIYHGsGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDmKAISIEEK 160
Cdd:cd04189 80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578096338 161 PEQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGD--LSVELMGrgfAWLDTGTHESLLEASQYI 237
Cdd:cd04189 158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrvGYSIVTG---WWKDTGTPEDLLEANRLL 233
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-225 |
1.62e-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: 203.97 E-value: 1.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDlHRFQELLQDGSEFGLKLSYAEQPS 82
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 83 PDGLAQAFIIGEEFISDDSVALILGDNIYHGSgLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEKPE 162
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578096338 163 QPRSNYAVTGLYFYDNDVVEIAKSIKpsPRGELEITDVNKAYLDRGDLSVELMgrGFAWLDTG 225
Cdd:cd04181 159 LPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-237 |
7.05e-63 |
|
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: 201.86 E-value: 7.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAEQP 81
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 82 SPDGLAQAFIIGEEFISDDSVALILGDNIYHGsGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEKP 161
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578096338 162 EQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGFaWLDTGTHESLLEASQYI 237
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-237 |
3.19e-50 |
|
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: 170.08 E-value: 3.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHrFQELLQDGSEFGLKLSYAEQ 80
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEK-VREYFGDGSRGGVPIEYVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 81 PSPDGLAQAFIIGEEFIsDDSVALILGDNIYHGSGLSKMLqkaasKESGATVFGYHVKDPERFGVVEFDQDmKAISIEEK 160
Cdd:TIGR03992 80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578096338 161 PEQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGRGfaWLDTGTHESLLEASQYI 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-238 |
9.62e-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: 159.16 E-value: 9.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIstpqdLH----RFQELLQDGSEFGLKLSY 77
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVIN-----VGylaeQIEEYFGDGSRFGVRITY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 78 AEQPSP----DGLAQAfiigEEFISDDSVALILGDNIYhGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMK 153
Cdd:COG1208 76 VDEGEPlgtgGALKRA----LPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 154 AISIEEKPEQPRSNYAVTGLYFYDNDVVEIAksikpsPRGE-LEITDVNKAYLDRGDLSVELMgRGFaWLDTGTHESLLE 232
Cdd:COG1208 151 VTRFVEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLE 222
|
....*.
gi 1578096338 233 ASQYIE 238
Cdd:COG1208 223 ANALLL 228
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-234 |
2.86e-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: 114.55 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DLHRFQE--LLQDGSE 70
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfDRSYELEetLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 71 FGLKL----------SYAEQPSPDGLAQAFIIGEEFISDDSVALILGDNIY--HGSGLSKMLQkaASKESGATVFGYHVK 138
Cdd:cd02541 81 DLLEEvriisdlaniHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIdsKEPCLKQLIE--AYEKTGASVIAVEEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 139 DPE---RFGVVEF----DQDMKAISIEEKP--EQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGD 209
Cdd:cd02541 159 PPEdvsKYGIVKGekidGDVFKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238
|
250 260
....*....|....*....|....*.
gi 1578096338 210 -LSVELMGRgfaWLDTGTHESLLEAS 234
Cdd:cd02541 239 vYAYVFEGK---RYDCGNKLGYLKAT 261
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-233 |
1.75e-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: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDIlIISTPQDLHRFQELLQDGSEFGLKLSYAEQPSP 83
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFISDDSVALILGDNIYHGSgLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEKPEQ 163
Cdd:cd06915 81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578096338 164 PRSNYAVTGLYFYDNDVVEIAKSIKPSprgeLEiTDVNKAYLDRGDLsvelmgRGFA----WLDTGTHESLLEA 233
Cdd:cd06915 160 AAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-233 |
2.03e-23 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 96.64 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTP------------QDLHRF------QE 63
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdrsYELEATleakgkEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 64 LL---QDGSEfGLKLSYAEQPSPDGLAQAFIIGEEFISDDSVALILGDNIYHGS--GLSKMLQkaASKESGATVFGyhVK 138
Cdd:COG1210 85 LLeevRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQMIE--VYEETGGSVIA--VQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 139 --DPE---RFGVVEFDQD----MKAISIEEKP--EQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDR 207
Cdd:COG1210 160 evPPEevsKYGIVDGEEIeggvYRVTGLVEKPapEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239
|
250 260
....*....|....*....|....*..
gi 1578096338 208 GD-LSVELMGRgfaWLDTGTHESLLEA 233
Cdd:COG1210 240 EPvYAYEFEGK---RYDCGDKLGYLKA 263
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-233 |
1.25e-22 |
|
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: 92.96 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDIlIISTPQDLHRFQELLQDGSEFGLKLSYAEQPSP 83
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFIsDDSVALILGDnIYHGSGLSKMLQKAASKESGATVFG--YHVKDPerFGVVEFDQDmKAISIEEKP 161
Cdd:cd06426 81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEGG-RITSIEEKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578096338 162 EQprsNYAV-TGLYFYDNDVVE-IAKSIKpsprgeLEITDVNKAYLDRGDLSVELMGRGFaWLDTGTHESLLEA 233
Cdd:cd06426 156 TH---SFLVnAGIYVLEPEVLDlIPKNEF------FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-180 |
2.96e-20 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 89.36 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLYPLT--RAaskqlmpvydKPMIYY---------PLSTLMLAGIRDILIIsT---PQDLHRFqelLQDG 68
Cdd:COG0448 4 AIILAGGRGSRLGPLTkdRA----------KPAVPFggkyriidfPLSNCVNSGIRRVGVL-TqykSHSLNDH---IGSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 69 SEFGL--KLSY-----AEQPSPD-----GLAQAFIIGEEFI--SDDSVALIL-GDNIYHGSgLSKMLQkaASKESGA--T 131
Cdd:COG0448 70 KPWDLdrKRGGvfilpPYQQREGedwyqGTADAVYQNLDFIerSDPDYVLILsGDHIYKMD-YRQMLD--FHIESGAdiT 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578096338 132 VFGYHV--KDPERFGVVEFDQDMKAISIEEKPEQPRSNYAVTGLYFYDNDV 180
Cdd:COG0448 147 VACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-208 |
3.64e-20 |
|
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: 86.88 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRD-ILIIS-TPQDLHRFQELLQDgsEFGLKLSYA 78
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 79 EQPSPDGLAQAFIIGEEFISDDSVA-LILGDNIYHGSGLSKMLQ--KAASKEsgATVFGYHVKDPERFGVVEFDQDMKAI 155
Cdd:cd06425 79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDfhKKHGAE--GTILVTKVEDPSKYGVVVHDENTGRI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578096338 156 -SIEEKPEQPRSNYAVTGLYFYDNDV--------VEIAKSIKP--SPRGELEITDVNKAYLDRG 208
Cdd:cd06425 157 eRFVEKPKVFVGNKINAGIYILNPSVldriplrpTSIEKEIFPkmASEGQLYAYELPGFWMDIG 220
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
1-141 |
1.52e-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: 76.54 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIsTPQDlhrFQELLQDGsefglkLSYAEQ 80
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVV-VPEE---EQAEISTY------LRSFPL 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578096338 81 PSPDGLAQAFIIGEE---------FISD--DSVALILGDNIYHGSGLSKMLQKAASKESGATVFGYHVKDPE 141
Cdd:cd04198 71 NLKQKLDEVTIVLDEdmgtadslrHIRKkiKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSS 142
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
2-233 |
1.07e-13 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 68.75 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIistpqDLHRFQELLQD---GSEFGLKLSYA 78
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV-----NTHHLADQIEAhlgDSRFGLRITIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 79 EQP-----SPDGLAQAfiigEEFISDDSVALILGDNIYHGsGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMK 153
Cdd:cd06422 76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 154 AIsIEEKPEQPRSNYAVTGLYFYDNDVVEIAksikpsPRGELEITDVNKAYLDRGDLSVELMgRGFaWLDTGTHESLLEA 233
Cdd:cd06422 151 GR-LRRGGGGAVAPFTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-233 |
9.98e-13 |
|
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: 66.10 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDlHRFQELLQDgsEFGLKLSYAEQPSP 83
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKK--YPNIKFVYNPDYAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFISDDSVaLILGDNIYHGSGLSKMLqkAASKESGATVFGYHVKDPERFGVVeFDQDMKAISIEEKPEQ 163
Cdd:cd02523 79 TNNIYSLYLARDFLDEDFL-LLEGDVVFDPSILERLL--SSPADNAILVDKKTKEWEDEYVKD-LDDAGVLLGIISKAKN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578096338 164 PRSNYAVT-GLYFYDND----VVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVELMGrGFAWLDTGTHESLLEA 233
Cdd:cd02523 155 LEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-234 |
9.98e-13 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 67.59 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDK-PMIYYPLSTLMLAGIRDILIIST--PQDLHRFqelLQDGSEFGLK--- 74
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQyqPLELNNH---IGIGSPWDLDrin 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 75 -----LS-YAEQPSPD---GLAQAFIIGEEFIS--DDSVALIL-GDNIYHgSGLSKMLQKAASKESGATVFGYHV--KDP 140
Cdd:PRK05293 81 ggvtiLPpYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIYK-MDYDKMLDYHKEKEADVTIAVIEVpwEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 141 ERFGVVEFDQDMKAISIEEKPEQPRSNYAVTGLYFY---------------DNDVVEIAKSIKPSprgeleitdvnkaYL 205
Cdd:PRK05293 160 SRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL-------------YL 226
|
250 260
....*....|....*....|....*....
gi 1578096338 206 DRGDLSVELMGRGFaWLDTGTHESLLEAS 234
Cdd:PRK05293 227 EEGEKLYAYPFKGY-WKDVGTIESLWEAN 254
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-199 |
1.08e-12 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 66.84 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIS------------TPQDLHRFQEL---- 64
Cdd:PRK10122 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLLEQrvkr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 65 -----LQDGSEFGLKLSYAEQPSPDGLAQAFIIGEEFISDDSVALILGDNIYHGS-------GLSKMLqkAASKESG-AT 131
Cdd:PRK10122 84 qllaeVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplryNLAAMI--ARFNETGrSQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578096338 132 VFGYHVK-DPERFGVVEFDQDMKA-------ISIEEKPEQPR---SNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITD 199
Cdd:PRK10122 162 VLAKRMPgDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-199 |
1.86e-12 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 66.47 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIS------------TPQDLHRFQE------ 63
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEAMLEkrvkrq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 64 LLQDGSEF---GLKLSYAEQPSPDGLAQAFIIGEEFISDDSVALILGDNIY--HGSGLSK-----MLQKAasKESGAT-V 132
Cdd:PRK13389 90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQdnlaeMIRRF--DETGHSqI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578096338 133 FGYHVKDPERFGVVEFD-------QDMKAISIEEKP--EQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITD 199
Cdd:PRK13389 168 MVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-200 |
9.88e-12 |
|
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: 63.30 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLYpltRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIsTPQDLHRFQELLQDgsefgLKLSYAEQPSP 83
Cdd:cd02540 2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNVEFVLQEEQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFISDDS-VALIL-GDN--IyHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISI-E 158
Cdd:cd02540 73 LGTGHAVKQALPALKDFEgDVLVLyGDVplI-TPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIvE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1578096338 159 EK---PEQPRSNYAVTGLYFYDNDVVEIA-KSIKPSP-RGELEITDV 200
Cdd:cd02540 152 EKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI 198
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-52 |
1.02e-11 |
|
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: 63.04 E-value: 1.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILII 52
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-164 |
6.29e-11 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 62.17 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLYPLT--RAaskqlmpvydKPMIYY---------PLSTLMLAGIRDILIIsTPQDLHRFQELLQDG---- 68
Cdd:PRK00725 19 LILAGGRGSRLKELTdkRA----------KPAVYFggkfriidfALSNCINSGIRRIGVL-TQYKAHSLIRHIQRGwsff 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 69 -SEFG--LKLSYAEQPSPD-----GLAQAF-----IIGEEfisDDSVALIL-GDNIYHgSGLSKMLqkAASKESGA--TV 132
Cdd:PRK00725 88 rEELGefVDLLPAQQRVDEenwyrGTADAVyqnldIIRRY---DPKYVVILaGDHIYK-MDYSRML--ADHVESGAdcTV 161
|
170 180 190
....*....|....*....|....*....|....
gi 1578096338 133 FGYHV--KDPERFGVVEFDQDMKAISIEEKPEQP 164
Cdd:PRK00725 162 ACLEVprEEASAFGVMAVDENDRITAFVEKPANP 195
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
2-237 |
1.46e-10 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 59.87 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 2 KGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDlHRFQELLQdgsEFGLKLSYAEQP 81
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKA-ELIEEALA---RPGPDVTFVYNP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 82 SPDG------LAQAFiigeEFISDDsVALILGDNIYHGSGLSKMLqkaASKESGATVFGYHVKDPERFGV-VEFDQDMKA 154
Cdd:COG1213 77 DYDEtnniysLWLAR----EALDED-FLLLNGDVVFDPAILKRLL---ASDGDIVLLVDRKWEKPLDEEVkVRVDEDGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 155 ISIEEKPEQPRSNYAVTGLYFYDND----VVEIAKSIKPSPRGELEITDVNKAYLDRG-DLSVELMGRGFaWLDTGTHES 229
Cdd:COG1213 149 VEIGKKLPPEEADGEYIGIFKFSAEgaaaLREALEALIDEGGPNLYYEDALQELIDEGgPVKAVDIGGLP-WVEIDTPED 227
|
....*...
gi 1578096338 230 LLEASQYI 237
Cdd:COG1213 228 LERAEELF 235
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-132 |
1.14e-09 |
|
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: 56.78 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLYPLTRAASKQLMPV---YDkpMIYYPLSTLMLAGIRDILIIsTPQDLHRFQELLQDGSEF-------G 72
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVL-TQYKSRSLNDHLGSGKEWdldrkngG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578096338 73 LKLSYAEQ-PSPD---GLAQAFIIGEEFI--SDDSVALIL-GDNIYHgSGLSKMLQKAasKESGATV 132
Cdd:cd02508 78 LFILPPQQrKGGDwyrGTADAIYQNLDYIerSDPEYVLILsGDHIYN-MDYREMLDFH--IESGADI 141
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-208 |
5.57e-09 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 56.53 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLyplTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIsTPQDLHRFQELLQdgsefGLKLSYAEQPSP 83
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEAALQ-----GSGVAFARQEQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFIS--DDSVALILGDN-IYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISIEEK 160
Cdd:PRK14358 82 LGTGDAFLSGASALTegDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578096338 161 PEQPRSNYAV----TGLYFYDNDVVEIAKSI-KPSPRGELEITDVNKAYLDRG 208
Cdd:PRK14358 162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-200 |
1.47e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 55.15 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 1 MKGIILAGGSGTRL---YPltraasKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDLHRfQELLQDGSEFglklsy 77
Cdd:PRK14357 1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELVK-KLLPEWVKIF------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 78 aEQPSPDGLAQAFIIGEEFISDDSVALIL-GDN--IYHGSgLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKA 154
Cdd:PRK14357 68 -LQEEQLGTAHAVMCARDFIEPGDDLLILyGDVplISENT-LKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578096338 155 IsIEEK--PEQPRSNYAV-TGLYFYDND-VVEIAKSIKP-SPRGELEITDV 200
Cdd:PRK14357 146 I-VEDKdaPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-180 |
2.46e-08 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 54.45 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLYPLTRAASKQLMP---VYDkpMIYYPLSTLMLAGIRDILII----STPQDLH-----RFQELLQdgse 70
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLtqykSHSLDRHisqtwRLSGLLG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 71 fglklSYAEqPSP----------DGLAQAFIIGEEFISD---DSVALILGDNIYHgSGLSKMLQKAASKESGATVFGYHV 137
Cdd:PRK00844 82 -----NYIT-PVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHVYR-MDPRQMVDFHIESGAGVTVAAIRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578096338 138 --KDPERFGVVEFDQDMKAISIEEKPEQPRS-------NYAVTGLYFYDNDV 180
Cdd:PRK00844 155 prEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDA 206
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-68 |
5.33e-08 |
|
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: 52.96 E-value: 5.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAAS-KQLMPVY-DKPMIYYPLSTLM-LAGIRDILIISTPQdlHRF--QELLQDG 68
Cdd:cd02509 1 IYPVILAGGSGTRLWPLSRESYpKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVVTNEE--YRFlvREQLPEG 71
|
|
| 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 |
6.83e-08 |
|
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: 52.26 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGG--SGTRLYPLTRAASKQLMPVYDKPMIYYPLSTL-MLAGIRDILIISTPQDLHRFQELLQDGSEFGLKLSYAE 79
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 80 QPSPDGLAQAF-----IIGEEfisDDSVALILGDNIYHGSGLSKMLQKAASKESGATVFGYHV--KDPERFG-VVEFDQD 151
Cdd:cd06428 81 EYKPLGTAGGLyhfrdQILAG---NPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGcIVEDPST 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578096338 152 MKAISIEEKPEQPRSNYAVTGLYFYDNDVVEIAKSIKPSPRGELEITDVNKAYLDRGDLSVE 213
Cdd:cd06428 158 GEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-161 |
1.17e-07 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 52.58 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLYPLTRAASKQLMPVYDK-PMIYYPLSTLMLAGIRDILIIStpQ----DLHR--------------FQE 63
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT--QfnsaSLNRhisqtynfdgfsggFVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 64 LLqdgsefglklsyAEQPSPD------GLAQA-----FIIGEEFISDdsvALIL-GDNIYHgSGLSKMLQKaaSKESGA- 130
Cdd:PRK02862 84 VL------------AAQQTPEnpswfqGTADAvrkylWHFQEWDVDE---YLILsGDQLYR-MDYRLFVQH--HRETGAd 145
|
170 180 190
....*....|....*....|....*....|....
gi 1578096338 131 -TVFGYHV--KDPERFGVVEFDQDMKAISIEEKP 161
Cdd:PRK02862 146 iTLAVLPVdeKDASGFGLMKTDDDGRITEFSEKP 179
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-67 |
2.09e-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: 50.51 E-value: 2.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578096338 4 IILAGGSGTRlypLTRAASKQLMPVYDKPMIYYPLSTLMLAG-IRDILIISTPQDLHRFQELLQD 67
Cdd:COG1211 1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
|
|
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-61 |
7.83e-07 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 49.68 E-value: 7.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578096338 1 MKGIILAGGSGTRLYPLTRAAS-KQLMPVY-DKPMIYyplSTLM----LAGIRDILIIsTPQDlHRF 61
Cdd:COG0836 3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ---QTVErlagLVPPENILVV-TNEE-HRF 64
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-200 |
1.04e-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: 49.64 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLY---PltraasKQLMPVYDKPMIYYPLSTLMLAGIRDILIIstpqdlHRFQ-----ELLQDgsefgLKL 75
Cdd:COG1207 6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------VGHGaeqvrAALAD-----LDV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 76 SYAEQPSPDGLAQAFIIGEEFISDDS-VALIL-GDN--IyHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQD 151
Cdd:COG1207 69 EFVLQEEQLGTGHAVQQALPALPGDDgTVLVLyGDVplI-RAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDED 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1578096338 152 MKAISI-EEK---PEQpRSNYAV-TGLYFYDNDVVEIA-KSIKPS-PRGELEITDV 200
Cdd:COG1207 148 GRVLRIvEEKdatEEQ-RAIREInTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-216 |
1.21e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 49.36 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRLyplTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQDlHRFQELLQDGSEfglkLSYAEQPSP 83
Cdd:PRK14355 7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQA-EKVREHFAGDGD----VSFALQEEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFIS--DDSVALILGDN-IYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAISI-EE 159
Cdd:PRK14355 79 LGTGHAVACAAPALDgfSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 160 K---PEQPRSNYAVTGLYFYDNDVVEIA-KSIK-PSPRGELEITDVNKAYLDRG--------DLSVELMG 216
Cdd:PRK14355 159 KdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEGlrclafpvADPDEIMG 228
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-209 |
3.00e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 48.29 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRL---YPltraasKQLMPVYDKPMIYYPLSTLMLAGIRDI-LIISTPQDLhrFQELLQDGSEFGLKlsyAE 79
Cdd:PRK14354 6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIvTVVGHGAEE--VKEVLGDRSEFALQ---EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 80 QPspdGLAQAFIIGEEFISDDS--VALILGDN-IYHGSGLSKMLQKAASKESGATVFGYHVKDPERFGVVEFDQDMKAIS 156
Cdd:PRK14354 75 QL---GTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578096338 157 I-EEK---PEQPRSNYAVTGLYFYDNDV-VEIAKSIKP-SPRGELEITDVNKAYLDRGD 209
Cdd:PRK14354 152 IvEQKdatEEEKQIKEINTGTYCFDNKAlFEALKKISNdNAQGEYYLTDVIEILKNEGE 210
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
4-67 |
6.20e-06 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 46.28 E-value: 6.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578096338 4 IILAGGSGTRLypltrAAS--KQLMPVYDKPMIYYPLSTLMLAG-IRDILIISTPQDLHRFQELLQD 67
Cdd:PRK00155 7 IIPAAGKGSRM-----GADrpKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELLLA 68
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-70 |
1.38e-05 |
|
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: 45.21 E-value: 1.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578096338 4 IILAGGSGTRL---YPltraasKQLMPVYDKPMIYYPLSTLM-LAGIRDILIISTPQDLHRFQELLQDGSE 70
Cdd:cd02516 4 IILAAGSGSRMgadIP------KQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
3-52 |
1.73e-05 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 45.62 E-value: 1.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1578096338 3 GIILAGGSGTRLYPLTRAASKQLMPV---YDkpMIYYPLSTLMLAGIRDILII 52
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-108 |
5.85e-04 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 40.14 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIsTPqdlHRFQELLQDGSEFGLKLSYAEQPS 82
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LG---ADAEEVAAALAGLGVRVVVNPDWE 76
|
90 100
....*....|....*....|....*...
gi 1578096338 83 pDGLAQAFIIGEEFISD--DSVALILGD 108
Cdd:COG2068 77 -EGMSSSLRAGLAALPAdaDAVLVLLGD 103
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-60 |
1.00e-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: 1.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578096338 3 GIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTlmLAGIRDILIISTPQDLHR 60
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLER--LRPAGDEVVVVANDEEVL 51
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-108 |
1.44e-03 |
|
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: 38.70 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 3 GIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIIsTPQDLHRFQELLQDGSEFGLKLSYAEQps 82
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVV-LGAEADAVRAALAGLPVVVVINPDWEE-- 74
|
90 100
....*....|....*....|....*...
gi 1578096338 83 pdGLAQAFIIGEEFISDDS--VALILGD 108
Cdd:cd04182 75 --GMSSSLAAGLEALPADAdaVLILLAD 100
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-160 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 4 IILAGGSGTRlypLTRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTPQdlhrFQELLQDGSEFGLKLSYAEQPSP 83
Cdd:PRK14353 9 IILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPG----AEAVAAAAAKIAPDAEIFVQKER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578096338 84 DGLAQAFIIGEEFISD--DSVALILGDN--IYHGSgLSKMLQKAASKeSGATVFGYHVKDPERFG-VVEFDQDMKAIsIE 158
Cdd:PRK14353 82 LGTAHAVLAAREALAGgyGDVLVLYGDTplITAET-LARLRERLADG-ADVVVLGFRAADPTGYGrLIVKGGRLVAI-VE 158
|
..
gi 1578096338 159 EK 160
Cdd:PRK14353 159 EK 160
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
1-64 |
2.83e-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: 37.94 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578096338 1 MKGIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTlmLAGIRDILIISTPQDLHRFQEL 64
Cdd:cd02503 1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLER--LKPLVDEVVISANRDQERYALL 57
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
6-55 |
3.18e-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: 37.95 E-value: 3.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1578096338 6 LAGGSGTRLypltRAASKQLMPVYDKPMIYYPLSTLMLAGIRDILIISTP 55
Cdd:COG2266 1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-64 |
3.54e-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: 37.48 E-value: 3.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578096338 1 MKGIILAGGSGTRLypltrAASKQLMPVYDKPMIYYPLSTlmLAGIRDILIISTPQDlHRFQEL 64
Cdd:COG0746 5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP-ERYAAL 60
|
|
| |
