|
Name |
Accession |
Description |
Interval |
E-value |
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-295 |
1.83e-163 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 455.70 E-value: 1.83e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAIQE 85
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 QANGIAESLLIAEDFLAGHGCALVLGDNLFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEKP 165
Cdd:COG1209 82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 166 KAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGVAWLDTGTPDALSEATQFVAAIE 245
Cdd:COG1209 162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2403397112 246 KRQGLKINCPEEVAFRQGWIDGSQLMKLAKPLLNSGYGEYLESLVRKQRR 295
Cdd:COG1209 242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRA 291
|
|
| rmlA |
TIGR01207 |
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ... |
6-291 |
9.63e-156 |
|
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: 436.05 E-value: 9.63e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAIQE 85
Cdd:TIGR01207 1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 QANGIAESLLIAEDFLAGHGCALVLGDNLFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEKP 165
Cdd:TIGR01207 81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 166 KAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGVAWLDTGTPDALSEATQFVAAIE 245
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2403397112 246 KRQGLKINCPEEVAFRQGWIDGSQLMKLAKPLLNSGYGEYLESLVR 291
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-244 |
2.03e-133 |
|
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: 377.69 E-value: 2.03e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 5 KKGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAIQ 84
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 85 EQANGIAESLLIAEDFLAGHGCALVLGDNLFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEK 164
Cdd:cd02538 81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 165 PKAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGVAWLDTGTPDALSEATQFVAAI 244
Cdd:cd02538 161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
4-291 |
3.31e-125 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 358.99 E-value: 3.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 4 TKKGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAI 83
Cdd:PRK15480 3 TRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 84 QEQANGIAESLLIAEDFLAGHGCALVLGDNLFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQE 163
Cdd:PRK15480 83 QPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 164 KPKAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGVAWLDTGTPDALSEATQFVAA 243
Cdd:PRK15480 163 KPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIAT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2403397112 244 IEKRQGLKINCPEEVAFRQGWIDGSQLMKLAKPLLNSGYGEYLESLVR 291
Cdd:PRK15480 243 IEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-242 |
4.97e-76 |
|
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: 232.14 E-value: 4.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDK-PMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAIQ 84
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 85 EQANGIAESLLIAEDFLAGHGC-ALVLGDNLFYGENLAQIwLDAASQH---VGAHVFAYHVANPQDYGVVSLNQQGVVIS 160
Cdd:pfam00483 81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQA-VKFHIEKaadATVTFGIVPVEPPTGYGVVEFDDNGRVIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 161 IQEKPKAPK-SQYAMPGLYFFDSQAVEY-AKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGVAWLDTGTPDALSEAT 238
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEAN 239
|
....
gi 2403397112 239 QFVA 242
Cdd:pfam00483 240 LFLL 243
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-241 |
6.15e-60 |
|
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: 190.86 E-value: 6.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 5 KKGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDlPLFQTLLGRGQQWGIHLEYAIQ 84
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 85 EQANGIAESLLIAEDFLAGHGCALVLGDNLFyGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLnQQGVVISIQEK 164
Cdd:cd04189 80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLI-QEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2403397112 165 PKAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGVaWLDTGTPDALSEATQFV 241
Cdd:cd04189 158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
7-229 |
5.44e-53 |
|
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: 172.38 E-value: 5.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICTARDLPLFQTLLGRGQQWGIHLEYAIQEQ 86
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEI-ILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 87 ANGIAESLLIAEDFLAGHGCALVLGDNLFYgENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEKPK 166
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTD-LDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2403397112 167 APKSQYAMPGLYFFDSQAVEYAKGIQPssRGELEIVDVITQYMNTNQLTVSTLgrGVAWLDTG 229
Cdd:cd04181 159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
6-252 |
1.25e-52 |
|
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: 175.67 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAIQE 85
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 QANGIAESLLIAEDFLAGHGCALVLGDNLFYgENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEKP 165
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQ-DGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 166 KAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVItQYMNTNQLTVSTLGRGVAWLDTGTPDALSEATQFV-AAI 244
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAI-QWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLIlDEV 238
|
....*....
gi 2403397112 245 EKR-QGLKI 252
Cdd:TIGR01208 239 EREvQGVDD 247
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-243 |
2.59e-43 |
|
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: 147.99 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICTARDLPLFQTLLGRGQQWGIHLEYAIQE 85
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 QANGIAESLLIAEDFLAGHGCALVLGDNLFyGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEKP 165
Cdd:COG1208 80 EPLGTGGALKRALPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2403397112 166 KAPKSQYAMPGLYFFDSQAVEYAKGiqpssRGELEIVDVITQYMNTNQLTVSTLgRGVaWLDTGTPDALSEATQFVAA 243
Cdd:COG1208 159 EEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALLLS 229
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
6-231 |
7.30e-43 |
|
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: 151.21 E-value: 7.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDlPLFQTLLGRGQQWGIHLEYAIQE 85
Cdd:TIGR03992 2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 QANGIAESLLIAEDFLagHGCALVL-GDNLFYGENLAQIwLDAASQHVGAHvfayHVANPQDYGVVSLNQqGVVISIQEK 164
Cdd:TIGR03992 81 EQLGTADALGSAKEYV--DDEFLVLnGDVLLDSDLLERL-IRAEAPAIAVV----EVDDPSDYGVVETDG-GRVTGIVEK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2403397112 165 PKAPKSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNTNQLTVSTLGRGvaWLDTGTP 231
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRP 217
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-242 |
1.64e-21 |
|
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: 91.44 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 5 KKGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIcTAR-----------DLPLFQTLLGRGQ 73
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIV-TGRgkraiedhfdrSYELEETLEKKGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 74 Q----------WGIHLEYAIQEQANGIAESLLIAEDFLAGHGCALVLGDNLFYGE--NLAQIwLDAASQHvGAHVFAYHV 141
Cdd:cd02541 80 TdlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQL-IEAYEKT-GASVIAVEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 142 ANPQD---YGVVSLNQQG----VVISIQEKPK---APkSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMNT 211
Cdd:cd02541 158 VPPEDvskYGIVKGEKIDgdvfKVKGLVEKPKpeeAP-SNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEE 236
|
250 260 270
....*....|....*....|....*....|..
gi 2403397112 212 NQ-LTVSTLGRgvaWLDTGTPDALSEATQFVA 242
Cdd:cd02541 237 EPvYAYVFEGK---RYDCGNKLGYLKATVEFA 265
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-101 |
1.16e-19 |
|
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: 85.02 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQW--GIHLEY-A 82
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNlkQKLDEVtI 81
|
90 100
....*....|....*....|....
gi 2403397112 83 IQEQANGIAESLL-----IAEDFL 101
Cdd:cd04198 82 VLDEDMGTADSLRhirkkIKKDFL 105
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
8-237 |
1.84e-18 |
|
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: 81.83 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICTARDLPLFQTLLGRGQQWGIHLEYAIQEQA 87
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 88 NGIAESLLIAEDFLAGHGCaLVL-GDNLFYGeNLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEKPK 166
Cdd:cd06915 81 LGTGGAIKNALPKLPEDQF-LVLnGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2403397112 167 APKSQYAMPGLYFFDSQAVEYAKGIQPSsrgeLEiVDVITQYMNTNQLtvstlgRGVA----WLDTGTPDALSEA 237
Cdd:cd06915 159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-231 |
5.22e-18 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 81.10 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAIQE 85
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 QANGIAESLLIAEDFLAGhgcalvlGDNLFYGEN--------LAQIwLDAASQHVG-AHVFAYHVANPQDYGVVSLNQQ- 155
Cdd:cd06425 82 EPLGTAGPLALARDLLGD-------DDEPFFVLNsdvicdfpLAEL-LDFHKKHGAeGTILVTKVEDPSKYGVVVHDENt 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2403397112 156 GVVISIQEKPKAPKSQYAMPGLYFFDSQAVEYAKgIQPSSRgELEIVDVITQYmntNQLTVSTLgRGVaWLDTGTP 231
Cdd:cd06425 154 GRIERFVEKPKVFVGNKINAGIYILNPSVLDRIP-LRPTSI-EKEIFPKMASE---GQLYAYEL-PGF-WMDIGQP 222
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
5-238 |
6.30e-17 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 78.92 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 5 KKGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIcTAR-----------DLPLFQTLLGRGQ 73
Cdd:COG1210 4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFV-TGRgkraiedhfdrSYELEATLEAKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 74 Q----------WGIHLEYAIQEQANGIAESLLIAEDFLAGHGCALVLGDNLFYGE--NLAQIwLDAASQHVGAHVFAYHV 141
Cdd:COG1210 83 EelleevrsisPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQM-IEVYEETGGSVIAVQEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 142 anPQD----YGVVSLNQQ--GV--VISIQEKPK---APkSQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVITQYMN 210
Cdd:COG1210 162 --PPEevskYGIVDGEEIegGVyrVTGLVEKPApeeAP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAK 238
|
250 260
....*....|....*....|....*....
gi 2403397112 211 TNQ-LTVSTLGRgvaWLDTGTPDALSEAT 238
Cdd:COG1210 239 EEPvYAYEFEGK---RYDCGDKLGYLKAT 264
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
8-237 |
1.36e-16 |
|
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: 76.78 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICTARDLPLFQTLLGRGQQWGIHLEYAIQEQA 87
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 88 NGIAESLLIAEDFLagHGCALVLGDNLFYGENLAQIwLDAASQH-----VGAHVFAYHVAnpqdYGVVSLNqQGVVISIQ 162
Cdd:cd06426 81 LGTAGALSLLPEKP--TDPFLVMNGDILTNLNYEHL-LDFHKENnadatVCVREYEVQVP----YGVVETE-GGRITSIE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2403397112 163 EKPKapKSQYAMPGLYFFDSQAVEYakgIQPSSRgeLEIVDVITQYMNTNQLTVSTLGRGvAWLDTGTPDALSEA 237
Cdd:cd06426 153 EKPT--HSFLVNAGIYVLEPEVLDL---IPKNEF--FDMPDLIEKLIKEGKKVGVFPIHE-YWLDIGRPEDYEKA 219
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-112 |
6.90e-16 |
|
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: 74.60 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWG-----IHLE 80
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLsskmiVDVI 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 2403397112 81 YAIQEQANGIAESLL-----IAEDFLaghgcaLVLGD 112
Cdd:cd02507 82 TSDLCESAGDALRLRdirglIRSDFL------LLSCD 112
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
8-259 |
6.74e-14 |
|
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: 69.57 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICT--ARDlpLFQTLLGRGQqwGIHL----EY 81
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDI-VIVTgyKKE--QIEELLKKYP--NIKFvynpDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 82 AIqeqaNGIAESLLIAEDFLaGHGCALVLGDnLFYGENLAQIWLDAAsqhvGAHVFAYHVANPQDYGVVS--LNQQGVVI 159
Cdd:cd02523 77 AE----TNNIYSLYLARDFL-DEDFLLLEGD-VVFDPSILERLLSSP----ADNAILVDKKTKEWEDEYVkdLDDAGVLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 160 SIQEKPKAPKS-QYAMPGLYFFDSQAVEyakgiqpssrgelEIVDVITQYMNTnqltvstlGRGVAWLDTGTPDALSEAT 238
Cdd:cd02523 147 GIISKAKNLEEiQGEYVGISKFSPEDAD-------------RLAEALEELIEA--------GRVNLYYEDALQRLISEEG 205
|
250 260
....*....|....*....|.
gi 2403397112 239 QFVAAIEKRQGLKINCPEEVA 259
Cdd:cd02523 206 VKVKDISDGFWYEIDDLEDLE 226
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-242 |
3.18e-13 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 67.57 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLpLFQTLLgrgQQWGIHLEYAIQ- 84
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAE-LIEEAL---ARPGPDVTFVYNp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 85 --EQANGIAeSLLIAEDFLAGhGCALVLGDNLFYGENLAQIwldAASQHVGAHVFAYHVANPQDYGV-VSLNQQGVVISI 161
Cdd:COG1213 77 dyDETNNIY-SLWLAREALDE-DFLLLNGDVVFDPAILKRL---LASDGDIVLLVDRKWEKPLDEEVkVRVDEDGRIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 162 QEKPKAPKSQYAMPGLYFFDSQA----VEYAKGIQPSSRGELEIVDVITQYMNTNQL--TVSTlgRGVAWLDTGTPDALS 235
Cdd:COG1213 152 GKKLPPEEADGEYIGIFKFSAEGaaalREALEALIDEGGPNLYYEDALQELIDEGGPvkAVDI--GGLPWVEIDTPEDLE 229
|
....*..
gi 2403397112 236 EATQFVA 242
Cdd:COG1213 230 RAEELFA 236
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-237 |
1.16e-12 |
|
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: 65.67 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICTARdLP--LFQTLlgRGQQWGIHLEY-- 81
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHH-LAdqIEAHL--GDSRFGLRITIsd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 82 ---AIQEQANGI--AESLLIAEDFLaghgcaLVLGDNLFYGENLAQIWLDAASQHvGAHVFAYHVANP--QDYGVVSLNQ 154
Cdd:cd06422 77 epdELLETGGGIkkALPLLGDEPFL------VVNGDILWDGDLAPLLLLHAWRMD-ALLLLLPLVRNPghNGVGDFSLDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 155 QGVVISIQEKPKAPksqYAMPGLYFFDSQAVEyakGIQPssrGELEIVDVITQYMNTNQLTVStLGRGVaWLDTGTPDAL 234
Cdd:cd06422 150 DGRLRRGGGGAVAP---FTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGL-VYDGL-WFDVGTPERL 218
|
...
gi 2403397112 235 SEA 237
Cdd:cd06422 219 LAA 221
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
8-205 |
3.51e-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: 64.46 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIcTARDLPLFQTLLGRGQqwgihLEYAIQEQA 87
Cdd:cd02540 2 VILAAGKGTR---MKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALANPN-----VEFVLQEEQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 88 NGIAESLLIAEDFLAGH-GCALVL-GDN-LFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEK 164
Cdd:cd02540 73 LGTGHAVKQALPALKDFeGDVLVLyGDVpLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVEE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2403397112 165 PKAPKSQYAM----PGLYFFDSQAV-EYAKGIQPS-SRGELEIVDVI 205
Cdd:cd02540 153 KDATEEEKAIrevnAGIYAFDAEFLfEALPKLTNNnAQGEYYLTDII 199
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-205 |
4.24e-11 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 62.93 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 4 TKKGIVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIctardlplfqtlLGRG-----QQWGIH 78
Cdd:PRK14354 2 NRYAIILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGaeevkEVLGDR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 79 LEYAIQEQANGIAESLLIAEDFLAGH-GCALVL-GDN-LFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQ 155
Cdd:PRK14354 67 SEFALQEEQLGTGHAVMQAEEFLADKeGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2403397112 156 GVVISIQEKPKAPKSQYAM----PGLYFFDSQAVEYA-KGIQP-SSRGELEIVDVI 205
Cdd:PRK14354 147 GEVEKIVEQKDATEEEKQIkeinTGTYCFDNKALFEAlKKISNdNAQGEYYLTDVI 202
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
7-181 |
2.39e-10 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 60.47 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSkqllpiydKPMIYY---------PLATLMQAGIQHILIIctARDLPlfQTL---LGRGQQ 74
Cdd:COG0448 4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVL--TQYKS--HSLndhIGSGKP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 75 W-------GIHLEYAIQEQ---------ANGIAESLliaeDFLAGHGCALVL---GDNLF---YGENLAqiwldaasQHV 132
Cdd:COG0448 72 WdldrkrgGVFILPPYQQRegedwyqgtADAVYQNL----DFIERSDPDYVLilsGDHIYkmdYRQMLD--------FHI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2403397112 133 --GAH--VFAYHVANPQ--DYGVVSLNQQGVVISIQEKPKAPKSQYAMPGLYFFD 181
Cdd:COG0448 140 esGADitVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
8-71 |
3.79e-10 |
|
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: 58.60 E-value: 3.79e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAG-IQHILIICTARDLPLFQTLLGR 71
Cdd:COG1211 1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
8-163 |
4.98e-10 |
|
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: 59.65 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIC-TARDLpLFQTLLGRGqqwgihLEYAIQEQ 86
Cdd:COG1207 6 VILAAGKGTR---MKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVgHGAEQ-VRAALADLD------VEFVLQEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 87 ANGIAESLLIAEDFLAGH-GCALVL-GDN-LFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQE 163
Cdd:COG1207 76 QLGTGHAVQQALPALPGDdGTVLVLyGDVpLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRIVE 155
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-207 |
1.87e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 58.22 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQqwgihLEYAIQEQA 87
Cdd:PRK14355 7 IILAAGKGTR---MKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 88 NGIAESLLIAEDFLAG-HGCALVL-GDN-LFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEK 164
Cdd:PRK14355 79 LGTGHAVACAAPALDGfSGTVLILcGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIVEE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2403397112 165 PKAPKSQYAM----PGLYFFDSQAVEYA-KGIQ-PSSRGELEIVDVITQ 207
Cdd:PRK14355 159 KDATPEERSIrevnSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAM 207
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
8-189 |
7.01e-09 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 54.95 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTA---RDLPLFQTLLGRGQQWGIHLeyaIQ 84
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDehnTKFHLDESLKLLAPNATVVE---LD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 85 EQANGIAESLLIAEDFLAGHGCALVL-GDNLFYGENLAQIWLDAASQHVGAHV--FAYHvanPQdYGVVSLNQQGVVISI 161
Cdd:cd04183 79 GETLGAACTVLLAADLIDNDDPLLIFnCDQIVESDLLAFLAAFRERDLDGGVLtfFSSH---PR-WSYVKLDENGRVIET 154
|
170 180 190
....*....|....*....|....*....|
gi 2403397112 162 QEkpKAPKSQYAMPGLYFFDS--QAVEYAK 189
Cdd:cd04183 155 AE--KEPISDLATAGLYYFKSgsLFVEAAK 182
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
7-112 |
2.02e-08 |
|
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: 52.95 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGGQGSRLypmtlNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYaiqeq 86
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDW----- 72
|
90 100
....*....|....*....|....*...
gi 2403397112 87 ANGIAESLLIAEDFLAGH--GCALVLGD 112
Cdd:cd04182 73 EEGMSSSLAAGLEALPADadAVLILLAD 100
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-69 |
7.04e-08 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 52.06 E-value: 7.04e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAG-IQHILIICTARDLPLFQTLL 69
Cdd:PRK00155 7 IIPAAGKGSR---MGADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-69 |
1.07e-07 |
|
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: 51.37 E-value: 1.07e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAG-IQHILIICTARDLPLFQTLL 69
Cdd:cd02516 4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPDDIDLAKELA 63
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
8-208 |
1.12e-07 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 52.67 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGqqwgihLEYAIQEQA 87
Cdd:PRK14358 11 VILAAGQGTR---MKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 88 NGIAESLLIAEDFLA-GHGCALVL-GDN-LFYGENLAQIWLDAASQHVGAHVFAYHVANPQDYGVVSLNQQGVVISIQEK 164
Cdd:PRK14358 82 LGTGDAFLSGASALTeGDADILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2403397112 165 PKAPKSQYAM----PGLYFFDSQAVEYAKGIQPSSR-GELEIVDVITQY 208
Cdd:PRK14358 162 KDATDAEKAIgefnSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLY 210
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
5-209 |
1.77e-07 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 51.45 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 5 KKGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTAR----------DLPLFQTLLGRGQQ 74
Cdd:PRK13389 9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSknsienhfdtSFELEAMLEKRVKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 75 WGIHLEYAI-----------QEQANGIAESLLIAEDFLAGHGCALVLGDNLF--YGENLAQIWLDAASQHVG----AHVF 137
Cdd:PRK13389 89 QLLDEVQSIcpphvtimqvrQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQDNLAEMIRRFDetghSQIM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 138 AYHVANPQDYGVVSLnqQGV---------VISIQEKPKAPK--SQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVIT 206
Cdd:PRK13389 169 VEPVADVTAYGVVDC--KGVelapgesvpMVGVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAID 246
|
...
gi 2403397112 207 QYM 209
Cdd:PRK13389 247 MLI 249
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
6-207 |
2.00e-07 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 51.43 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 6 KGIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTAR------------------DLPLFQT 67
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASknavenhfdtsyelesllEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 68 LLGRGQQW---GIHLEYAIQEQANGIAESLLIAEDFLAGHGCALVLGDNLFYGE-------NLAQiwLDAASQHVG-AHV 136
Cdd:PRK10122 85 LLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplryNLAA--MIARFNETGrSQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 137 FAYHV-ANPQDYGVVS----LNQQGVVISIQ---EKPKAPK---SQYAMPGLYFFDSQAVEYAKGIQPSSRGELEIVDVI 205
Cdd:PRK10122 163 LAKRMpGDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAI 242
|
..
gi 2403397112 206 TQ 207
Cdd:PRK10122 243 AE 244
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
7-112 |
4.12e-07 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 49.39 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGGQGSRLypmtlNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYaiqeq 86
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDW----- 75
|
90 100
....*....|....*....|....*...
gi 2403397112 87 ANGIAESLLIAEDFLAGH--GCALVLGD 112
Cdd:COG2068 76 EEGMSSSLRAGLAALPADadAVLVLLGD 103
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
7-237 |
5.43e-07 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 50.21 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSKQLLP---IYDkpMIYYPLATLMQAGIQHILIICTARDLPLFQ---------TLLGR--- 71
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTQYKSHSLDRhisqtwrlsGLLGNyit 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 72 --------GQQWgihleYaiQEQANGIAESLLIAEDFLAGHGCalVLGDNLFYGENLAQIwldaASQHV--GAHVfayHV 141
Cdd:PRK00844 86 pvpaqqrlGKRW-----Y--LGSADAIYQSLNLIEDEDPDYVV--VFGADHVYRMDPRQM----VDFHIesGAGV---TV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 142 A-NPQD------YGVVSLNQQGVVISIQEKPKAPKSqyaMP----------GLYFFDSQA-----VEYA----------K 189
Cdd:PRK00844 150 AaIRVPreeasaFGVIEVDPDGRIRGFLEKPADPPG---LPddpdealasmGNYVFTTDAlvdalRRDAadedsshdmgG 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2403397112 190 GIQPS--SRGELEIVDvitqyMNTNQLTVSTLGRGVAWLDTGTPDALSEA 237
Cdd:PRK00844 227 DIIPRlvERGRAYVYD-----FSTNEVPGATERDRGYWRDVGTIDAYYDA 271
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
7-131 |
7.49e-07 |
|
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: 47.96 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGGQGSRlypmtLNVSKQLLPIYDKPMIYYPLATLMQAGiQHILIICtaRDLPLFQTLLGRGQQWgIHLEYAIQeq 86
Cdd:pfam12804 1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVA--NDEEVLAALAGLGVPV-VPDPDPGQ-- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2403397112 87 anGIAESLLIAEDFLAGHGCALVL-GDNLFYGENLAQIWLDAASQH 131
Cdd:pfam12804 70 --GPLAGLLAALRAAPGADAVLVLaCDMPFLTPELLRRLLAAAEES 113
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
7-78 |
1.10e-06 |
|
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: 48.31 E-value: 1.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSKQLLPI---YDkpMIYYPLATLMQAGIQHILIICTARDLPLFQTlLGRGQQWGIH 78
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLTQYKSRSLNDH-LGSGKEWDLD 72
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
7-91 |
1.32e-06 |
|
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: 48.79 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 7 GIVLAGG--QGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQ-AGIQHILIICTARDLPLFQTLLGRGQQWGIHLEYAI 83
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
|
....*...
gi 2403397112 84 QEQANGIA 91
Cdd:cd06428 81 EYKPLGTA 88
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-163 |
1.54e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 49.09 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIcTARDLPLFQTLLGRGqqwGIHLEYAIQEQA 87
Cdd:PRK14353 9 IILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVV-VGPGAEAVAAAAAKI---APDAEIFVQKER 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2403397112 88 NGIAESLLIAEDFLA-GHGCALVL-GDN-LFYGENLAQIwLDAASQHVGAHVFAYHVANPQDYGVVsLNQQGVVISIQE 163
Cdd:PRK14353 82 LGTAHAVLAAREALAgGYGDVLVLyGDTpLITAETLARL-RERLADGADVVVLGFRAADPTGYGRL-IVKGGRLVAIVE 158
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-57 |
3.12e-05 |
|
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: 43.64 E-value: 3.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2403397112 1 MVVTKKGIVLAGGQGSRlypmtLNVSKQLLPIYDKPMIYYPLATLMQAgIQHILIIC 57
Cdd:COG0746 1 MTMPITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVA 51
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
7-59 |
4.69e-05 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 43.75 E-value: 4.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIICTA 59
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCS 55
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
10-69 |
3.99e-04 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 40.64 E-value: 3.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 10 LAGGQGSRLYpmtlNVSKQLLPIYDKPMIYYPLATLMQAGIQHIlIICTARDLPLFQTLL 69
Cdd:COG2266 1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKI-YVAVSPNTPKTREYL 55
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-205 |
6.53e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 41.08 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQAGIQHILIIctardlplfqtlLGRG-QQWGIHLE------ 80
Cdd:PRK14352 8 IVLAAGAGTR---MRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVV------------VGHDrERVAPAVAelapev 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 81 -YAIQEQANGIAESLLIAEDFLAG--HGCALVL-GDN-LFYGENLAQiwLDAASQHVG--AHVFAYHVANPQDYGVVSLN 153
Cdd:PRK14352 73 dIAVQDEQPGTGHAVQCALEALPAdfDGTVVVTaGDVpLLDGETLAD--LVATHTAEGnaVTVLTTTLDDPTGYGRILRD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2403397112 154 QQGVVISIQEKPKAPKSQYAM----PGLYFFDSQAVEYAKGIQPS--SRGELEIVDVI 205
Cdd:PRK14352 151 QDGEVTAIVEQKDATPSQRAIrevnSGVYAFDAAVLRSALARLSSdnAQGELYLTDVL 208
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-258 |
8.23e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 40.48 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMqagiqhiliictardlPLF----QTLLGRGQQW------GI 77
Cdd:PRK14356 9 LILAAGKGTR---MHSDKPKVLQTLLGEPMLRFVYRALR----------------PLFgdnvWTVVGHRADMvraafpDE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 78 HLEYAIQEQANGIAESLLIAEDFLAGHG---CALVLGDNLFYGENLAQIWLDAAsqhVGAHV-FA-YHVANPQDYGVVsL 152
Cdd:PRK14356 70 DARFVLQEQQLGTGHALQCAWPSLTAAGldrVLVVNGDTPLVTTDTIDDFLKEA---AGADLaFMtLTLPDPGAYGRV-V 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 153 NQQGVVISIQEKPKAPKSQYAMP------GLYFFDSQAVE--YAKGIQPSSRGELEIVDVItQYMNTNQLTVSTLGRGVA 224
Cdd:PRK14356 146 RRNGHVAAIVEAKDYDEALHGPEtgevnaGIYYLRLDAVEslLPRLTNANKSGEYYITDLV-GLAVAEGMNVLGVNCGED 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2403397112 225 W--LDTGTPDAL--SEATQFVAAIEK--RQGLKINCPEEV 258
Cdd:PRK14356 225 PnlLGVNTPAELvrSEELLRARIVEKhlESGVLIHAPESV 264
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
7-56 |
8.65e-04 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 40.64 E-value: 8.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSKQLLPIYDK-PMIYYPLATLMQAGIQHILII 56
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
8-176 |
1.06e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 40.21 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRLYPMTLNVSKQLLPIYDK-PMIYYPLATLMQAGIQHILIICTARDLPLFQTLLgRGqqWGiHLEYAIQE- 85
Cdd:PRK00725 19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQ-RG--WS-FFREELGEf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 86 -------Q-----------ANGIAESLLIAEDFLAGHgcALVL-GDNLF---YGENLAqiwldaasQHV--GAHVFAYHV 141
Cdd:PRK00725 95 vdllpaqQrvdeenwyrgtADAVYQNLDIIRRYDPKY--VVILaGDHIYkmdYSRMLA--------DHVesGADCTVACL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2403397112 142 ANPQD----YGVVSLNQQGVVISIQEKPKAPKsqyAMPG 176
Cdd:PRK00725 165 EVPREeasaFGVMAVDENDRITAFVEKPANPP---AMPG 200
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
8-138 |
1.39e-03 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 39.33 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRlypMTLNVSKQLLPIYDKPMIYYPLATLMQ-AGIQHILIICTARDLPLFQtllGRGQQWGIHLEYAI--- 83
Cdd:PLN02728 28 ILLAGGVGKR---MGANMPKQYLPLLGQPIALYSLYTFARmPEVKEIVVVCDPSYRDVFE---EAVENIDVPLKFALpgk 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 84 --QEQA-NGIAESLLIAEdFLAGHGCA--LVLgdnlfyGENLAQIWLDAASqhVGAHVFA 138
Cdd:PLN02728 102 erQDSVfNGLQEVDANSE-LVCIHDSArpLVT------SADIEKVLKDAAV--HGAAVLG 152
|
|
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
8-98 |
1.89e-03 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 39.28 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 8 IVLAGGQGSRLYPMtlnvS-----KQLLPIYDKpmiyyplATLMQA---------GIQHILIICtardlplfqtllgrgq 73
Cdd:COG0836 6 VILAGGSGTRLWPL----SresypKQFLPLLGE-------KSLLQQtverlaglvPPENILVVT---------------- 58
|
90 100
....*....|....*....|....*
gi 2403397112 74 qwGIHLEYAIQEQANGIAESLLIAE 98
Cdd:COG0836 59 --NEEHRFLVAEQLPELGPANILLE 81
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-171 |
2.62e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 39.24 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 1 MVVTKKGIV-LAGGQGSRLYPmtlNVSKQLLPIYDKPMIYYPLATLMQAGIQHI-LIICTARDLpLFQTLLGRGQQWGIH 78
Cdd:PRK09451 1 MLNSAMSVViLAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVhLVYGHGGDL-LKQTLADEPLNWVLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2403397112 79 LE-----YAIQEQANGIAESlliaEDFLAGHGCA-LVLGDNLfygENLaqiwLDAASQHvGAHVFAYHVANPQDYGVVsL 152
Cdd:PRK09451 77 AEqlgtgHAMQQAAPFFADD----EDILMLYGDVpLISVETL---QRL----RDAKPQG-GIGLLTVKLDNPTGYGRI-T 143
|
170
....*....|....*....
gi 2403397112 153 NQQGVVISIQEKPKAPKSQ 171
Cdd:PRK09451 144 RENGKVVGIVEQKDATDEQ 162
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
7-57 |
5.23e-03 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 37.17 E-value: 5.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2403397112 7 GIVLAGGQGSRlypMTLNvsKQLLPIYDKPMIYYPLATLMQAgIQHILIIC 57
Cdd:cd02503 3 GVILAGGKSRR---MGGD--KALLELGGKPLLEHVLERLKPL-VDEVVISA 47
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
7-37 |
9.03e-03 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 37.53 E-value: 9.03e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2403397112 7 GIVLAGGQGSRLYPMTLNVSKQLLPI---Y---DKPM 37
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYrliDIPM 42
|
|
| |
