|
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: 570.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAVQ 80
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 81 PSPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEK 160
Cdd:COG1209 81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 161 PEKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGFAWLDTGTHETLLEASTFIETI 240
Cdd:COG1209 161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1489982263 241 EKRQNLKVACLEEISFRMGYITREQLVALAEPLKKNQYGQYLLRLAAE 288
Cdd:COG1209 241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
|
|
| rmlA |
TIGR01207 |
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ... |
2-286 |
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: 559.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAVQP 81
Cdd:TIGR01207 1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 82 SPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEKP 161
Cdd:TIGR01207 81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 162 EKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGFAWLDTGTHETLLEASTFIETIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1489982263 242 KRQNLKVACLEEISFRMGYITREQLVALAEPLKKNQYGQYLLRLA 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
1-240 |
3.72e-180 |
|
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: 495.56 E-value: 3.72e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAVQ 80
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 81 PSPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEK 160
Cdd:cd02538 81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 161 PEKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGFAWLDTGTHETLLEASTFIETI 240
Cdd:cd02538 161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-285 |
1.11e-159 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 446.04 E-value: 1.11e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAVQP 81
Cdd:PRK15480 5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 82 SPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEKP 161
Cdd:PRK15480 85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 162 EKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGFAWLDTGTHETLLEASTFIETIE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1489982263 242 KRQNLKVACLEEISFRMGYITREQLVALAEPLKKNQYGQYLLRL 285
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-238 |
3.09e-101 |
|
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: 296.09 E-value: 3.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDK-PMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAVQ 80
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 81 PSPDGLAQAFIIGEKFIG-TDSVCLVLGDNIYYGGGLSKMLQRAAAKES--GATVFGYHVNDPERFGVVEFDDDMHALSI 157
Cdd:pfam00483 81 PEGKGTAPAVALAADFLGdEKSDVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 158 EEKPEKPK-SNYAVTGLYFYDNEVVE-IAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGFAWLDTGTHETLLEAST 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240
|
...
gi 1489982263 236 FIE 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 |
4.14e-74 |
|
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: 226.68 E-value: 4.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDtPRFQELFGDGKDLGLQIDYAVQ 80
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 81 PSPDGLAQAFIIGEKFIGTDSVCLVLGDNIyYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDmHALSIEEK 160
Cdd:cd04189 80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNL-IQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489982263 161 PEKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNK--LSVEVMGrgfAWLDTGTHETLLEASTFI 237
Cdd:cd04189 158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrvGYSIVTG---WWKDTGTPEDLLEANRLL 233
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-225 |
6.85e-66 |
|
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: 205.12 E-value: 6.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDtPRFQELFGDGKDLGLQIDYAVQPS 82
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 83 PDGLAQAFIIGEKFIGTDSVCLVLGDNIYYGGgLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEKPE 162
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489982263 163 KPKSNYAVTGLYFYDNEVVEIAKNIKPsaRGELEITDINKVYLEKNKLSVEVMgrGFAWLDTG 225
Cdd:cd04181 159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-243 |
2.06e-64 |
|
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: 205.71 E-value: 2.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAVQP 81
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 82 SPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYgGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEKP 161
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQ-DGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 162 EKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGFaWLDTGTHETLLEASTFI-ETI 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIlDEV 238
|
...
gi 1489982263 241 EKR 243
Cdd:TIGR01208 239 ERE 241
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-233 |
8.03e-48 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 159.55 E-value: 8.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEIlIISTPQDTPRFQELFGDGKDLGLQIDYAVQP 81
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 82 SP----DGLAQAfiigEKFIGTDSVCLVLGDnIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSI 157
Cdd:COG1208 80 EPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489982263 158 EEKPEKPKSNYAVTGLYFYDNEVVE-IAKNikpsarGELEITDINKVYLEKNKLSVEVMgRGFaWLDTGTHETLLEA 233
Cdd:COG1208 155 VEKPEEPPSNLINAGIYVLEPEIFDyIPEG------EPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-234 |
6.70e-47 |
|
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: 161.61 E-value: 6.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTpRFQELFGDGKDLGLQIDYAVQ 80
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKE-KVREYFGDGSRGGVPIEYVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 81 PSPDGLAQAFIIGEKFIgtDSVCLVL-GDNIYYGGGLSKMLqraaaKESGATVFGYHVNDPERFGVVEFDDDmHALSIEE 159
Cdd:TIGR03992 80 EEQLGTADALGSAKEYV--DDEFLVLnGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489982263 160 KPEKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGRGfaWLDTGTHETLLEAS 234
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-234 |
9.39e-35 |
|
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: 126.49 E-value: 9.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQ--------DTPRFQE--LFGDGKD 70
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfDRSYELEetLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 71 LGL----------QIDYAVQPSPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYG--GGLSKMLQraAAKESGATVFGYHVN 138
Cdd:cd02541 81 DLLeevriisdlaNIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSkePCLKQLIE--AYEKTGASVIAVEEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 139 DPE---RFGVV---EFDDDM-HALSIEEKP--EKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNK 209
Cdd:cd02541 159 PPEdvsKYGIVkgeKIDGDVfKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238
|
250 260
....*....|....*....|....*.
gi 1489982263 210 LSVEVM-GRgfaWLDTGTHETLLEAS 234
Cdd:cd02541 239 VYAYVFeGK---RYDCGNKLGYLKAT 261
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-233 |
8.03e-27 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 105.88 E-value: 8.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQ--------DT-PRF-QELFGDGKD- 70
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGkraiedhfDRsYELeATLEAKGKEe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 71 ---------LGLQIDYAVQPSPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYG--GGLSKMLQraAAKESGATVFGYHVND 139
Cdd:COG1210 85 lleevrsisPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSekPCLKQMIE--VYEETGGSVIAVQEVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 140 PE---RFGVV---EFDDDMHALS-IEEKP--EKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNK- 209
Cdd:COG1210 163 PEevsKYGIVdgeEIEGGVYRVTgLVEKPapEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEPv 242
|
250 260
....*....|....*....|....
gi 1489982263 210 LSVEVMGRgfaWLDTGTHETLLEA 233
Cdd:COG1210 243 YAYEFEGK---RYDCGDKLGYLKA 263
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-233 |
3.86e-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: 99.93 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEIL---------IIstpqdtprfqELFGDGKDLGLQ 74
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVlsvgylaeqIE----------EYFGDGYRGGIR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 75 IDYAVQPSPDGLAQAFIIGEKFIGTDSVCLVLGDNiYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHA 154
Cdd:cd06915 72 IYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 155 LSIEEKPEKPKSNYAVTGLYFYDNEVVEIAKNIKPSargeLEiTDINKVYLEKNKLsvevmgRGFA----WLDTGTHETL 230
Cdd:cd06915 151 IAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDY 219
|
...
gi 1489982263 231 LEA 233
Cdd:cd06915 220 ARA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-233 |
2.06e-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: 92.57 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEIlIISTPQDTPRFQELFGDGKDLGLQIDYAVQPSP 83
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 84 DGLAQAFIIGEKFIgTDSVCLVLGD---NIYYggglSKMLQRAAAKESGATVFG--YHVNDPerFGVVEFDDDmHALSIE 158
Cdd:cd06426 81 LGTAGALSLLPEKP-TDPFLVMNGDiltNLNY----EHLLDFHKENNADATVCVreYEVQVP--YGVVETEGG-RITSIE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489982263 159 EKPEKpksNYAV-TGLYFYDNEVVE-IAKNIKpsargeLEITD-INKVYLEKNKLSV-EVMGRgfaWLDTGTHETLLEA 233
Cdd:cd06426 153 EKPTH---SFLVnAGIYVLEPEVLDlIPKNEF------FDMPDlIEKLIKEGKKVGVfPIHEY---WLDIGRPEDYEKA 219
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-233 |
5.55e-21 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 88.81 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKE-ILIIS-TPQDTPRFQELFgdGKDLGLQIDYA 78
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEY--EKKLGIKITFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 79 VQPSPDGLAQAFIIGEKFIGTDSVC-LVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHAL-S 156
Cdd:cd06425 79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIeR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 157 IEEKPEKPKSNYAVTGLYFYDNEVVEiaknikpsaRGELEITDINK----VYLEKNKLSVEVMgRGFaWLDTGTHETLLE 232
Cdd:cd06425 159 FVEKPKVFVGNKINAGIYILNPSVLD---------RIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQPKDFLK 227
|
.
gi 1489982263 233 A 233
Cdd:cd06425 228 G 228
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
2-233 |
2.75e-16 |
|
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: 75.69 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEIlIIST---PQdtpRFQELFGDgKDLGLQIDYa 78
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlAD---QIEAHLGD-SRFGLRITI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 79 vQPSPD-------GLAQAfiigEKFIGTDSVCLVLGDnIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDD 151
Cdd:cd06422 75 -SDEPDelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 152 mHALSIEEKPEKPKSNYAVTGLYFYDNEVVEiakNIKPsarGELEITDINKVYLEKNKLSVEVMgRGFaWLDTGTHETLL 231
Cdd:cd06422 149 -ADGRLRRGGGGAVAPFTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLL 219
|
..
gi 1489982263 232 EA 233
Cdd:cd06422 220 AA 221
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-180 |
5.09e-16 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 77.04 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMPI---Y---DkpmiFyPMSTLMLAGIKEILIIsTPQdtpRFQELF---GDGK--DL 71
Cdd:COG0448 4 AIILAGGRGSRLGPLTKDRAKPAVPFggkYriiD----F-PLSNCVNSGIRRVGVL-TQY---KSHSLNdhiGSGKpwDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 72 -----GLQIDYAVQPSPD-----GLAQA------FIIGEKFigtDSVCLVLGDNIY---YggglSKMLQRAAAKESGATV 132
Cdd:COG0448 75 drkrgGVFILPPYQQREGedwyqGTADAvyqnldFIERSDP---DYVLILSGDHIYkmdY----RQMLDFHIESGADITV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1489982263 133 FGYHVNDPE--RFGVVEFDDDMHALSIEEKPEKPKSNYAVTGLYFYDNEV 180
Cdd:COG0448 148 ACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
1-141 |
7.54e-15 |
|
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: 71.54 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQ-ELFGDGKDLGLQIDYAV 79
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEIStYLRSFPLNLKQKLDEVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489982263 80 QPS--PDGLAQAFIIGEKFIGTDSvcLVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPE 141
Cdd:cd04198 81 IVLdeDMGTADSLRHIRKKIKKDF--LVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSS 142
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-215 |
2.78e-13 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 68.76 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQ--------DTPRFQE--------- 63
Cdd:PRK10122 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASknavenhfDTSYELEslleqrvkr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 64 -LFGDGKDL---GLQIDYAVQPSPDGLAQAFIIGEKFIGTDSVCLVLGDNIYYGGGLSKMLQRAAA-----KESG-ATVF 133
Cdd:PRK10122 84 qLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAmiarfNETGrSQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 134 GYHV-NDPERFGVVEFDDDMHA-------LSIEEKPEKPK---SNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDInK 202
Cdd:PRK10122 164 AKRMpGDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDA-I 242
|
250
....*....|...
gi 1489982263 203 VYLEKNKlSVEVM 215
Cdd:PRK10122 243 AELAKKQ-SVDAM 254
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-207 |
7.16e-13 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 67.62 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIIsTPQDTPRFQELFGDGKDLGLQIDYAV-- 79
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELEAMLEKRVkr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 80 --------------------QPSPDGLAQAFIIGEKFIGTDSVCLVLGDNIY--YGGGLSK-----MLQRaaAKESGAT- 131
Cdd:PRK13389 89 qlldevqsicpphvtimqvrQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQdnlaeMIRR--FDETGHSq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 132 VFGYHVNDPERFGVVEFD-------DDMHALSIEEKP--EKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINK 202
Cdd:PRK13389 167 IMVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAID 246
|
....*
gi 1489982263 203 VYLEK 207
Cdd:PRK13389 247 MLIEK 251
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-233 |
1.52e-12 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 65.72 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQdtprfQELFGDGKDLGLQIDYAVQPSP 83
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYK-----KEQIEELLKKYPNIKFVYNPDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 84 D--GLAQAFIIGEKFIGTDsvCLVL-GDNIYYGGGLSKMLqrAAAKESGATVFGYHVNDPERFGVVeFDDDMHALSIEEK 160
Cdd:cd02523 77 AetNNIYSLYLARDFLDED--FLLLeGDVVFDPSILERLL--SSPADNAILVDKKTKEWEDEYVKD-LDDAGVLLGIISK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489982263 161 PEKPKSNYAVT-GLYFYDNE----VVEIAKNIKPSARGELEITDINKVYLEKNKLSVEVMGrGFAWLDTGTHETLLEA 233
Cdd:cd02523 152 AKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-234 |
4.99e-12 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 65.27 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDK-PMIFYPMSTLMLAGIKEILIIStpQDTPRfqELFG----------DGK 69
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT--QYQPL--ELNNhigigspwdlDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 70 DLGLQIdyaVQPSPD--------GLAQAFIIGEKFIgtDSV----CLVL-GDNIY---YggglSKMLQRAAAKESGATVF 133
Cdd:PRK05293 80 NGGVTI---LPPYSEseggkwykGTAHAIYQNIDYI--DQYdpeyVLILsGDHIYkmdY----DKMLDYHKEKEADVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 134 GYHV--NDPERFGVVEFDDDMHALSIEEKPEKPKSNYAVTGLYFY---------------DNEVVEIAKNIKPSargele 196
Cdd:PRK05293 151 VIEVpwEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL------ 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1489982263 197 itdinkvYLEKNKLSVEVMGRGFaWLDTGTHETLLEAS 234
Cdd:PRK05293 225 -------YLEEGEKLYAYPFKGY-WKDVGTIESLWEAN 254
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-52 |
5.25e-12 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 63.81 E-value: 5.25e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1489982263 1 MKGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILII 52
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-200 |
5.64e-11 |
|
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: 60.99 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLYpltKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIIstpqdtprfqelFGDGKDL------GLQIDY 77
Cdd:cd02540 2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEQvkkalaNPNVEF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 78 AVQPSPDGLAQAFIIGEKFI-GTDSVCLVLgdniyYG-------GGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFD 149
Cdd:cd02540 67 VLQEEQLGTGHAVKQALPALkDFEGDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRD 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489982263 150 DDMHALSI-EEK---PEKPKSNYAVTGLYFYDNEVVEIA-KNIKPS-ARGELEITDI 200
Cdd:cd02540 142 GNGKVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
|
|
| 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 |
8.06e-10 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 58.03 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGG--SGTRLYPLTKATSKQLMPIYDKPMIFYPMSTL-MLAGIKEILIISTPQDTPRFQELFGDGKDLGLQIDYAV 79
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 80 QPSPDGLA---------------QAFIIgekfIGTDSVCLV----LGDNIYYGGGLSKMLQRAAAKESgATVFGYHVNDP 140
Cdd:cd06428 81 EYKPLGTAgglyhfrdqilagnpSAFFV----LNADVCCDFplqeLLEFHKKHGASGTILGTEASREQ-ASNYGCIVEDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489982263 141 ERFGVVEFdddmhalsiEEKPEKPKSNYAVTGLYFYDNEVVEIAKNIKPSARGELEITDINKVYLEKNKLSVE 213
Cdd:cd06428 156 STGEVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-232 |
4.22e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 56.70 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRL---YPltkatsKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRfqelfgdgKDLGLQIDY 77
Cdd:PRK14357 1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELVK--------KLLPEWVKI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 78 AVQPSPDGLAQAFIIGEKFIGTDSVCLVL-GDN--IYYgGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHA 154
Cdd:PRK14357 67 FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVplISE-NTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 155 LsIEEK--PEKPKSNYAV-TGLYFYDNE-VVEIAKNIKP-SARGELEITDI----NKVYLEKNKLSVEVMG----RGFAW 221
Cdd:PRK14357 146 I-VEDKdaPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAvnfaEKVRVVKTEDLLEITGvntrIQLAW 224
|
250
....*....|.
gi 1489982263 222 LDTGTHETLLE 232
Cdd:PRK14357 225 LEKQLRMRILE 235
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-230 |
7.63e-09 |
|
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: 55.28 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 1 MKGIILAGGSGTRLYPL-TKATSKQLMPIY-DKPMIfypMSTLM----LAGIKEILIISTPQDTPRFQELFGDGKDlglQ 74
Cdd:cd02509 1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLL---QQTLDrlkgLVPPDRILVVTNEEYRFLVREQLPEGLP---E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 75 IDYAVQPSPDGLAQAFIIGEKFI---GTDSVCLVL------GDNIYYGGGLSKMLQraAAKESGATVFGYHVNDPE-RFG 144
Cdd:cd02509 75 ENIILEPEGRNTAPAIALAALYLakrDPDAVLLVLpsdhliEDVEAFLKAVKKAVE--AAEEGYLVTFGIKPTRPEtGYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 145 VVEFDDD-----MHALSIEEKP--EKPKSnYAVTGLYF-------------------YDNEVVEIAKNIKPSARGELEIT 198
Cdd:cd02509 153 YIEAGEKlgggvYRVKRFVEKPdlETAKE-YLESGNYLwnsgiflfraktfleelkkHAPDIYEALEKALAAAGTDDFLR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1489982263 199 DINKVYLEKNKLSVE--VMGR---------GFAWLDTGTHETL 230
Cdd:cd02509 232 LLEEAFAKIPSISIDyaVMEKtkkvavvpaDFGWSDLGSWDAL 274
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
2-52 |
7.93e-09 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 54.86 E-value: 7.93e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1489982263 2 KGIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILII 52
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-216 |
1.67e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 55.13 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLyplTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQdTPRFQELFGDGKDlglqIDYAVQPSP 83
Cdd:PRK14355 7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ-AEKVREHFAGDGD----VSFALQEEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 84 --DGLAQAFIIGEKFIGTDSVCLVLGDN-IYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSI-EE 159
Cdd:PRK14355 79 lgTGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 160 K---PEKPKSNYAVTGLYFYDNEVVEIA-KNIK-PSARGELEITDINKVYLEKNKL--------SVEVMG 216
Cdd:PRK14355 159 KdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEGLRclafpvadPDEIMG 228
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-200 |
6.12e-08 |
|
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: 53.11 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLYpltKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIIstpqdtprfqelFGDGKDL------GLQIDY 77
Cdd:COG1207 6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEQvraalaDLDVEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 78 AVQPSPDGLAQAFIIGEKFIGTDS-VCLVLgdniyYG-------GGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFD 149
Cdd:COG1207 71 VLQEEQLGTGHAVQQALPALPGDDgTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489982263 150 DDMHALSI-EEK---PEKPKSNYAVTGLYFYDNEVVEIA-KNIKPS-ARGELEITDI 200
Cdd:COG1207 146 EDGRVLRIvEEKdatEEQRAIREINTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-209 |
8.30e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 52.91 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRlypLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIIstpqdtprfqelFGDGKD-----LGLQIDYA 78
Cdd:PRK14354 6 IILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGAEevkevLGDRSEFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 79 VQPSPDGLAQAFIIGEKFI-GTDSVCLVL-GDN-IYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHAL 155
Cdd:PRK14354 71 LQEEQLGTGHAVMQAEEFLaDKEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 156 SI-EEK---PEKPKSNYAVTGLYFYDNEV-VEIAKNIKP-SARGELEITDINKVYLEKNK 209
Cdd:PRK14354 151 KIvEQKdatEEEKQIKEINTGTYCFDNKAlFEALKKISNdNAQGEYYLTDVIEILKNEGE 210
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-204 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLyplTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELFGDGkdlglqIDYAVQPSP 83
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 84 DGLAQAFIIGEKFIGT-DSVCLVL-GDN-IYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFGVVEFDDDMHALSIEEK 160
Cdd:PRK14358 82 LGTGDAFLSGASALTEgDADILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1489982263 161 PEKPKSNYAV----TGLYFYDNEVVEIAKNI-KPSARGELEITDINKVY 204
Cdd:PRK14358 162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLY 210
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-132 |
3.35e-07 |
|
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: 49.85 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMPI---YDkpMIFYPMSTLMLAGIKEILIIStpQDTPR--FQELfGDGKDLGL-QID 76
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT--QYKSRslNDHL-GSGKEWDLdRKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489982263 77 YAVQPSPdglAQAFIIGEKFIGT----------------DSVCLVLGDNIY---YggglSKMLQRaaAKESGATV 132
Cdd:cd02508 76 GGLFILP---PQQRKGGDWYRGTadaiyqnldyiersdpEYVLILSGDHIYnmdY----REMLDF--HIESGADI 141
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-166 |
1.00e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 49.45 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRLYPLTKATSKQLMPIYDKPMIF-YPMSTLMLAGIKEILII------STPQDTPR----FQELFGDGKDLg 72
Cdd:PRK00725 19 LILAGGRGSRLKELTDKRAKPAVYFGGKFRIIdFALSNCINSGIRRIGVLtqykahSLIRHIQRgwsfFREELGEFVDL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 73 lqidyavQPspdglAQAFIIGEK-FIGT-DSVC--------------LVL-GDNIY---YggglSKMLQRAAakESGA-- 130
Cdd:PRK00725 98 -------LP-----AQQRVDEENwYRGTaDAVYqnldiirrydpkyvVILaGDHIYkmdY----SRMLADHV--ESGAdc 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1489982263 131 TVFGYHVNDPE--RFGVVEFDDDMHALSIEEKPEKPKS 166
Cdd:PRK00725 160 TVACLEVPREEasAFGVMAVDENDRITAFVEKPANPPA 197
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-67 |
1.62e-06 |
|
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: 47.82 E-value: 1.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489982263 4 IILAGGSGTRlypLTKATSKQLMPIYDKPMIFYPMSTLMLAG-IKEILIISTPQDTPRFQELFGD 67
Cdd:COG1211 1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-52 |
2.64e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 48.34 E-value: 2.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMPIYDK-PMIFYPMSTLMLAGIKEILII 52
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
3-52 |
3.54e-06 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 47.93 E-value: 3.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMPI---YDkpMIFYPMSTLMLAGIKEILII 52
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
4-64 |
4.49e-06 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 46.67 E-value: 4.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489982263 4 IILAGGSGTRLypltKA-TSKQLMPIYDKPMIFYPMSTLMLAG-IKEILIISTPQDTPRFQEL 64
Cdd:PRK00155 7 IIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAEL 65
|
|
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-52 |
4.55e-06 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 47.37 E-value: 4.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1489982263 1 MKGIILAGGSGTRLYPL-TKATSKQLMPIY-DKPMIfypMSTLM----LAGIKEILII 52
Cdd:COG0836 3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLL---QQTVErlagLVPPENILVV 57
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-166 |
5.44e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 47.13 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMP---IYDkpMIFYPMSTLMLAGIKEILI------------------ISTPQDT--- 58
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhisqtwrLSGLLGNyit 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 59 --PRFQELfgdGKD--LGlqidyavqpSPDGLAQA--FIIGEKfigTDSVCLVLGDNIYYgGGLSKMLQRAAAKESGATV 132
Cdd:PRK00844 86 pvPAQQRL---GKRwyLG---------SADAIYQSlnLIEDED---PDYVVVFGADHVYR-MDPRQMVDFHIESGAGVTV 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1489982263 133 FGYHV--NDPERFGVVEFDDDMHALSIEEKPEKPKS 166
Cdd:PRK00844 150 AAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-75 |
8.64e-06 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 45.59 E-value: 8.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489982263 4 IILAGGSGTRlypLTKATSKQLMPIYDKPMIFYPMSTLM-LAGIKEILIISTPQDTPRFQELFGDGKDLGLQI 75
Cdd:cd02516 4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
6-64 |
7.48e-05 |
|
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: 42.57 E-value: 7.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489982263 6 LAGGSGTRLypltKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPqDTPRFQEL 64
Cdd:COG2266 1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREY 54
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-135 |
4.77e-04 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 39.87 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLypltkATSKQLMPIYDKPMIFYPMSTLMLAGiKEILIISTPQDTPRFQELFGdgkdlglqIDYAVQPS 82
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489982263 83 PD-----GLAQAFiigEKFIGTDSVCLVLGDNIYYGGG-LSKMLQRAAAKESGATVFGY 135
Cdd:pfam12804 67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPElLRRLLAAAEESGADIVVPVY 122
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-160 |
2.49e-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: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 4 IILAGGSGTRlypLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQdtprFQELFGDGKDLGLQIDYAVQPSP 83
Cdd:PRK14353 9 IILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPG----AEAVAAAAAKIAPDAEIFVQKER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 84 DGLAQAFIIGEKFI--GTDSVCLVLGDNIYYGGGLSKMLQRAAAKESGATVFGYHVNDPERFG-VVEFDDDMHALsIEEK 160
Cdd:PRK14353 82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrLIVKGGRLVAI-VEEK 160
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
3-52 |
2.53e-03 |
|
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: 38.36 E-value: 2.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLYPLTKATSKQLMPIYDKPMIFYPMSTLMLAGIKEILII 52
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-108 |
3.24e-03 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 37.83 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489982263 3 GIILAGGSGTRLypltkATSKQLMPIYDKPMIFYPMSTLMLAGIKEILIISTPQDTPRFQELfgdgKDLGLQI----DYA 78
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAL----AGLGVRVvvnpDWE 76
|
90 100 110
....*....|....*....|....*....|..
gi 1489982263 79 vqpspDGLAQAFIIGEKFI--GTDSVCLVLGD 108
Cdd:COG2068 77 -----EGMSSSLRAGLAALpaDADAVLVLLGD 103
|
|
| |
