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Conserved domains on  [gi|813185915|ref|XP_012207129|]
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hypothetical protein SPRG_12689 [Saprolegnia parasitica CBS 223.65]

Protein Classification

glycosyltransferase family 2 protein; glycosyltransferase family protein( domain architecture ID 10135960)

glycosyltransferase family 2 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-220 1.15e-64

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: 202.89  E-value: 1.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   4 YQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGK--ISVTVV 81
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLkqKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  82 AVEGEATETADALRAVADKIRSDFIVLAGDLITDCVLHNVADLHRINDATVTMLLKQEVAEVPTAKSKAASKEKPRRDEe 161
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDV- 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 813185915 162 midcIGMVDAENRVVFVSHSVYENDDLEVPRALLKRRPRINMHTDLYDAHVYIFSHWVL 220
Cdd:cd04198  160 ----IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-220 1.15e-64

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: 202.89  E-value: 1.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   4 YQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGK--ISVTVV 81
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLkqKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  82 AVEGEATETADALRAVADKIRSDFIVLAGDLITDCVLHNVADLHRINDATVTMLLKQEVAEVPTAKSKAASKEKPRRDEe 161
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDV- 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 813185915 162 midcIGMVDAENRVVFVSHSVYENDDLEVPRALLKRRPRINMHTDLYDAHVYIFSHWVL 220
Cdd:cd04198  160 ----IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 5-244 6.91e-36

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: 129.50  E-value: 6.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTA-KEmlDQVQSYVLGQYDGKISVTVVaV 83
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGyLA--EQIEEYFGDGSRFGVRITYV-D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  84 EGEATETADALRAVADKIRSD-FIVLAGDLITDCVLHNVADLHRINDATVTMLLKqevaEVPTAKSKaaskekprrdeem 162
Cdd:COG1208   78 EGEPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALV----PVPDPSRY------------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915 163 idciGMV--DAENRVVfvshsvyenDDLEVPRAllKRRPRINmhtdlydAHVYIFSHWVLDLLAEKKHIaSIkADLIPHL 240
Cdd:COG1208  141 ----GVVelDGDGRVT---------RFVEKPEE--PPSNLIN-------AGIYVLEPEIFDYIPEGEPF-DL-EDLLPRL 196


                 ....
gi 813185915 241 VRRQ 244
Cdd:COG1208  197 IAEG 200
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-133 5.39e-23

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: 95.40  E-value: 5.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915    6 AVILAGGSGVRLYPLTEETPKPLLLV-NGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGKISVTvVAVE 84
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVgGKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQIT-YALQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 813185915   85 GEATETADALRAVADKIR---SDFIVLAGDLITDCVLHNVADLHRINDATVT 133
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGdekSDVLVLGGDHIYRMDLEQAVKFHIEKAADAT 132
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 5-115 1.86e-22

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: 96.51  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915    5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTaKEMLDQVQSYVLGQYDGKISVTVVaVE 84
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVV-GYGKEKVREYFGDGSRGGVPIEYV-VQ 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 813185915   85 GEATETADALRAVADKIRSDFIVLAGDLITD 115
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDEFLVLNGDVLLD 110
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 1-59 2.47e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 57.38  E-value: 2.47e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 813185915   1 MAEYQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKE 59
Cdd:PRK15480   1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ 59
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-220 1.15e-64

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: 202.89  E-value: 1.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   4 YQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGK--ISVTVV 81
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLkqKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  82 AVEGEATETADALRAVADKIRSDFIVLAGDLITDCVLHNVADLHRINDATVTMLLKQEVAEVPTAKSKAASKEKPRRDEe 161
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDV- 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 813185915 162 midcIGMVDAENRVVFVSHSVYENDDLEVPRALLKRRPRINMHTDLYDAHVYIFSHWVL 220
Cdd:cd04198  160 ----IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 4-220 1.53e-47

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: 158.96  E-value: 1.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   4 YQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEmLDQVQSYVLG----QYDGKISVT 79
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEH-SQAIIEHLLKskwsSLSSKMIVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  80 VVAVEG-EATETADALRAVADKIRSDFIVLAGDLITDCVLHNV----ADLHRINDATVTMLLKqevaevptaksKAASKE 154
Cdd:cd02507   80 VITSDLcESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELleerRKKDKNAIATLTVLLA-----------SPPVST 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 813185915 155 KPRRDEEMIDCIGMVDAENRVVFVSHSVYENDDLEV--PRALLKRRPRINMHTDLYDAHVYIFSHWVL 220
Cdd:cd02507  149 EQSKKTEEEDVIAVDSKTQRLLLLHYEEDLDEDLELiiRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 5-244 6.91e-36

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: 129.50  E-value: 6.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTA-KEmlDQVQSYVLGQYDGKISVTVVaV 83
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGyLA--EQIEEYFGDGSRFGVRITYV-D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  84 EGEATETADALRAVADKIRSD-FIVLAGDLITDCVLHNVADLHRINDATVTMLLKqevaEVPTAKSKaaskekprrdeem 162
Cdd:COG1208   78 EGEPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALV----PVPDPSRY------------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915 163 idciGMV--DAENRVVfvshsvyenDDLEVPRAllKRRPRINmhtdlydAHVYIFSHWVLDLLAEKKHIaSIkADLIPHL 240
Cdd:COG1208  141 ----GVVelDGDGRVT---------RFVEKPEE--PPSNLIN-------AGIYVLEPEIFDYIPEGEPF-DL-EDLLPRL 196


                 ....
gi 813185915 241 VRRQ 244
Cdd:COG1208  197 IAEG 200
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-138 2.66e-34

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: 124.62  E-value: 2.66e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTaKEMLDQVQSYVLGQYDGKISVTVVaVEG 85
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVV-GYLGEQIEEYFGDGSKFGVNIEYV-VQE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 813185915  86 EATETADALRAVADKIRSD-FIVLAGDLITDCVLHNVADLHRINDATVTMLLKQ 138
Cdd:cd04181   79 EPLGTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAVKE 132
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 6-137 2.85e-23

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 95.31  E-value: 2.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAkEMLDQVQSYVLGQYDGKISVTVVaVEG 85
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVG-YLAEQIEEYFGDGYRGGIRIYYV-IEP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 813185915  86 EATETADALRAVADKIRSD-FIVLAGDLITDCVLHNVADLHRINDATVTMLLK 137
Cdd:cd06915   79 EPLGTGGAIKNALPKLPEDqFLVLNGDTYFDVDLLALLAALRASGADATMALR 131
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-133 5.39e-23

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: 95.40  E-value: 5.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915    6 AVILAGGSGVRLYPLTEETPKPLLLV-NGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGKISVTvVAVE 84
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVgGKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQIT-YALQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 813185915   85 GEATETADALRAVADKIR---SDFIVLAGDLITDCVLHNVADLHRINDATVT 133
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGdekSDVLVLGGDHIYRMDLEQAVKFHIEKAADAT 132
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 5-115 1.86e-22

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: 96.51  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915    5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTaKEMLDQVQSYVLGQYDGKISVTVVaVE 84
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVV-GYGKEKVREYFGDGSRGGVPIEYV-VQ 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 813185915   85 GEATETADALRAVADKIRSDFIVLAGDLITD 115
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDEFLVLNGDVLLD 110
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-156 5.09e-19

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: 83.72  E-value: 5.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLvTAKEMLDQVQSYvLGqyDG-KISVTVVAV- 83
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYI-SVNYLAEMIEDY-FG--DGsKFGVNISYVr 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 813185915  84 EGEATETADALRAVADKIRSDFIVLAGDLITDCVLHNVADLHRINDATVTMLLKQEVAEVP-----TAKSKAAS-KEKP 156
Cdd:cd06426   77 EDKPLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVPygvveTEGGRITSiEEKP 155
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 5-220 8.41e-18

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: 80.34  E-value: 8.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDV-LLVTAKEmlDQVQSYVLG--QYDGKIS-VTV 80
Cdd:cd04197    2 QAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVfVFCCSHS--DQIKEYIEKskWSKPKSSlMIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  81 VAVEGEATETA-DALRAVADK--IRSDFIVLAGDLITDCVLHNVADLHRIN-----DATVTMLLKQEVAEVPTAkskaas 152
Cdd:cd04197   80 IIIMSEDCRSLgDALRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLKEASPPHRTR------ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813185915 153 kekpRRDEEMIdcIGMVDAENRVVFvshsvYENDDL-------EVPRALLKRRPRINMHTDLYDAHVYIFSHWVL 220
Cdd:cd04197  154 ----RTGEEFV--IAVDPKTSRLLH-----YEELPGskyrsitDLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 6-244 1.73e-17

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: 79.95  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKE---MLDQVQsyvlgQYDGKISVTVV- 81
Cdd:cd06425    3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRpedMVPFLK-----EYEKKLGIKITf 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  82 AVEGEATETADALRAVADKIRSD---FIVLAGDLITDCVLHNVADLHRINDATVTMLlkqeVAEVptakskaaskEKPRR 158
Cdd:cd06425   78 SIETEPLGTAGPLALARDLLGDDdepFFVLNSDVICDFPLAELLDFHKKHGAEGTIL----VTKV----------EDPSK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915 159 ------DEEMidciGMVDA--ENRVVFVSHsvyenddlevprallkrrpRINmhtdlydAHVYIFSHWVLDLLAEKKhiA 230
Cdd:cd06425  144 ygvvvhDENT----GRIERfvEKPKVFVGN-------------------KIN-------AGIYILNPSVLDRIPLRP--T 191

                        250
                 ....*....|....
gi 813185915 231 SIKADLIPHLVRRQ 244
Cdd:cd06425  192 SIEKEIFPKMASEG 205
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-113 2.61e-17

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: 79.20  E-value: 2.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVT--AKEMLDqvqsYVLGQYDgKISvTVVAV 83
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgyKKEQIE----ELLKKYP-NIK-FVYNP 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 813185915  84 EGEATETADALRAVADKIRSDFIVLAGDLI 113
Cdd:cd02523   75 DYAETNNIYSLYLARDFLDEDFLLLEGDVV 104
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-136 3.09e-17

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: 78.77  E-value: 3.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVlLVTAKEMLDQVQSYVLGQYDGkISVTVVAVE 84
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHHLADQIEAHLGDSRFG-LRITISDEP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 813185915  85 GEATETADALRAVADKIRSD-FIVLAGDLITDCVLHNVADLHRINDATVTMLL 136
Cdd:cd06422   79 DELLETGGGIKKALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRMDALLLLL 131
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-113 2.06e-16

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 77.82  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSYvLGqyDGK---ISVTvVA 82
Cdd:COG1209    3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERL-LG--DGSqlgIKIS-YA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 813185915  83 VEGEATETADALRAVADKIRSDFIVLA-GDLI 113
Cdd:COG1209   79 VQPEPLGLAHAFIIAEDFIGGDPVALVlGDNI 110
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-182 8.93e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 75.28  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVT--AKEMLDQvqsyVLGQYDGKISvTVVA 82
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgyKAELIEE----ALARPGPDVT-FVYN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  83 VEGEATETADALRAVADKIRSDFIVLAGDlitdcVLHNVADLHRI--NDATVTMLLkqevaevptakskAASKEKPRRDE 160
Cdd:COG1213   76 PDYDETNNIYSLWLAREALDEDFLLLNGD-----VVFDPAILKRLlaSDGDIVLLV-------------DRKWEKPLDEE 137

                        170       180
                 ....*....|....*....|..
gi 813185915 161 EMIdcigMVDAENRVVFVSHSV 182
Cdd:COG1213  138 VKV----RVDEDGRIVEIGKKL 155
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-113 1.57e-15

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: 74.53  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMLDQVQSyVLGqyDGK---ISVTvVA 82
Cdd:cd02538    3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKE-LLG--DGSdlgIRIT-YA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 813185915  83 VEGEATETADALRAVADKIRSD-FIVLAGDLI 113
Cdd:cd02538   79 VQPKPGGLAQAFIIGEEFIGDDpVCLILGDNI 110
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-138 2.43e-15

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: 74.14  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAkEMLDQVQSYVLGQYDGKISVTVVaVEG 85
Cdd:cd04189    3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVG-PTGEEIKEALGDGSRFGVRITYI-LQE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 813185915  86 EATETADALRAVADKI-RSDFIVLAGDLITDCVLHNVADLHRINDATVTMLLKQ 138
Cdd:cd04189   81 EPLGLAHAVLAARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAE 134
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-135 3.48e-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: 62.15  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYpltEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMlDQVQSYVlgqydGKISVTVVaVEG 85
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA-EQVKKAL-----ANPNVEFV-LQE 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 813185915  86 EATETADALRAVADKIR---SDFIVLAGD--LITDCVLHNVADLHRINDATVTML 135
Cdd:cd02540   71 EQLGTGHAVKQALPALKdfeGDVLVLYGDvpLITPETLQRLLEAHREAGADVTVL 125
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 7-59 4.21e-11

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: 62.41  E-value: 4.21e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 813185915    7 VILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKE 59
Cdd:TIGR01207   3 IILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPE 55
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 1-59 2.47e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 57.38  E-value: 2.47e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 813185915   1 MAEYQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKE 59
Cdd:PRK15480   1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ 59
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-117 2.54e-09

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: 56.38  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLyplTEETPKPLLLVNGKPLIYYQL-ALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGKISVtvvaVE 84
Cdd:cd02516    3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLeAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI----VE 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 813185915  85 GEAT---ETADALRAVADKiRSDFIvlagdLITDCV 117
Cdd:cd02516   76 GGATrqdSVLNGLKALPDA-DPDIV-----LIHDAA 105
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 6-134 4.83e-09

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 55.24  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGK-PLIYYQLALLENSGFSDVLLVT---AKEMLDQVQS---YVLGQYDGkiSV 78
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVGVLTqykSRSLNDHLGSgkeWDLDRKNG--GL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813185915  79 TVVAVEGEATE-----TADALRAVADKI-RSD---FIVLAGDLITDCVLHNVADLHRINDATVTM 134
Cdd:cd02508   79 FILPPQQRKGGdwyrgTADAIYQNLDYIeRSDpeyVLILSGDHIYNMDYREMLDFHIESGADITV 143
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-108 1.03e-08

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: 54.75  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   7 VILAGGSGVRLyplTEETPKPLLLVNGKPLIYYQL-ALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDGKIsvtVVAVEG 85
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLeAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKP---VRVVAG 74

                         90       100
                 ....*....|....*....|....*.
gi 813185915  86 EAT--ET-ADALRAVADKIRsdfIVL 108
Cdd:COG1211   75 GATrqDSvRNGLEALPDDDD---WVL 97
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-132 1.44e-08

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 53.63  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   1 MAEYQAVILAGGSGVRLyplteETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVT---AKEMLDQVQSYvlgqydgkiS 77
Cdd:COG2068    1 MSKVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgadAEEVAAALAGL---------G 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  78 VTVVAVEGEATETADALRAVADKIRSD---FIVLAGD--LITDCVLHNVADLHRINDATV 132
Cdd:COG2068   67 VRVVVNPDWEEGMSSSLRAGLAALPADadaVLVLLGDqpLVTAETLRRLLAAFRESPASI 126
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 6-135 1.88e-08

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 54.18  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGG--SGVRLYPLTEETPKPLLLVNGKPLIYYQL-ALLENSGFSDVLLV---TAKEMLDQVQSyvlGQYDGKISVT 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIeACAKVPDLKEVLLIgfyPESVFSDFISD---AQQEFNVPIR 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  80 VVAvEGEATETADALRAVADKIR----SDFIVLAGDLITDCVLHNVADLHRINDATVTML 135
Cdd:cd06428   78 YLQ-EYKPLGTAGGLYHFRDQILagnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-115 1.72e-07

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 51.42  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPL-TEETPKPLL-LVNGKPLIyyQLALLENSGFS---DVLLVTAKEMLDQVQSYVLgqyDGKISVTV 80
Cdd:cd02509    3 PVILAGGSGTRLWPLsRESYPKQFLkLFGDKSLL--QQTLDRLKGLVppdRILVVTNEEYRFLVREQLP---EGLPEENI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 813185915  81 VaVEGEATETADALRAVADKIRSDF-----IVLAGD-LITD 115
Cdd:cd02509   78 I-LEPEGRNTAPAIALAALYLAKRDpdavlLVLPSDhLIED 117
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-108 2.69e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 50.52  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   1 MAEYQAVILAGGSGVRLyplTEETPKPLLLVNGKPLIYYQL-ALLENSGFSDVLLVTAKEMLDQVQSYVLGQYDgkisvT 79
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRM---GADRPKQYLPLGGKPILEHTLeAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDP-----K 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 813185915  80 VVAVEGEATEtAD----ALRAVADkirsDFIVL 108
Cdd:PRK00155  73 VTVVAGGAER-QDsvlnGLQALPD----DDWVL 100
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
6-65 3.88e-07

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 50.83  E-value: 3.88e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813185915   6 AVILAGGSGVRLYPL-TEETPKPLL-LVNGKPLIyyQLA---LLENSGFSDVLLVTAKEMLDQVQ 65
Cdd:COG0836    5 PVILAGGSGTRLWPLsRESYPKQFLpLLGEKSLL--QQTverLAGLVPPENILVVTNEEHRFLVA 67
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 6-135 4.22e-07

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: 51.18  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYpltEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEmLDQVQSYVlgqydGKISVTVVaveg 85
Cdd:COG1207    5 VVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHG-AEQVRAAL-----ADLDVEFV---- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 813185915  86 EATE---TADALRAVADKIRSD---FIVLAGD--LITDCVLHNVADLHRINDATVTML 135
Cdd:COG1207   72 LQEEqlgTGHAVQQALPALPGDdgtVLVLYGDvpLIRAETLKALLAAHRAAGAAATVL 129
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-135 1.38e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.36  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   1 MAEYQAVILAGGSGVRlypLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMlDQVQSYVLGQYDgkisvTV 80
Cdd:PRK14355   1 MNNLAAIILAAGKGTR---MKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQA-EKVREHFAGDGD-----VS 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 813185915  81 VAVEGEATETADALRAVADKIrSDF----IVLAGD--LITDCVLHNVADLHRINDATVTML 135
Cdd:PRK14355  72 FALQEEQLGTGHAVACAAPAL-DGFsgtvLILCGDvpLLRAETLQGMLAAHRATGAAVTVL 131
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 6-247 1.39e-06

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 49.30  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKpliyYQL---AL--LENSGFSDVllvtakemldqvqsYVLGQY-------- 72
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK----YRIidfPLsnCVNSGIRRV--------------GVLTQYkshslndh 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  73 ---------DGKIS-VTVVAVEGEATE------TADALRAVADKIRS---DFI-VLAGDLITDCVLHNVADLHRINDATV 132
Cdd:COG0448   66 igsgkpwdlDRKRGgVFILPPYQQREGedwyqgTADAVYQNLDFIERsdpDYVlILSGDHIYKMDYRQMLDFHIESGADI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915 133 TMllkqevaevptakskaASKEKPRrdEEMIDCIGM-VDAENRVVfvshSVYENDDlevprallkrrpriNMHTDLYDAH 211
Cdd:COG0448  146 TV----------------ACIEVPR--EEASRFGVMeVDEDGRIT----EFEEKPK--------------DPKSALASMG 189

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 813185915 212 VYIFS-HWVLDLL---AEKKHIASIKaDLIPHLVRR------QFRG 247
Cdd:COG0448  190 IYVFNkDVLIELLeedAPNSSHDFGK-DIIPRLLDRgkvyayEFDG 234
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 6-163 1.39e-06

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 48.72  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLL----------------------VTAKEMLDQ 63
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILclgykghvikeyflnyflhnsdVTIDLGTNR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  64 VQsyVLGQYDGKISVTVVAVeGEATETADALRAVADKIRSD--FIVLAGDLITDCVLHNVADLHRINDATVTMllkqeva 141
Cdd:cd02524   81 IE--LHNSDIEDWKVTLVDT-GLNTMTGGRLKRVRRYLGDDetFMLTYGDGVSDVNINALIEFHRSHGKLATV------- 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 813185915 142 evpTAKSKAAS---------------KEKPRRDEEMI 163
Cdd:cd02524  151 ---TAVHPPGRfgeldldddgqvtsfTEKPQGDGGWI 184
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 9-136 1.49e-06

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: 47.96  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   9 LAGGSGVRLypltEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMLDqVQSYVLgqydgKISVTVVAVEGEAT 88
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPK-TREYLK-----ERGVEVIETPGEGY 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 813185915  89 EtADaLRAVADKIRSDFIVLAGDL--ITDCVLHNVADLHRINDATVTMLL 136
Cdd:COG2266   71 V-ED-LNEALESISGPVLVVPADLplLTPEIIDDIIDAYLESGKPSLTVV 118
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-144 1.58e-06

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: 47.19  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915    6 AVILAGGSGVRLyplteETPKPLLLVNGKPLIYYQLALLEnSGFSDVLLVTAKemlDQVQSYVLGQydgkiSVTVVAVEG 85
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLR-PAGDEVVVVAND---EEVLAALAGL-----GVPVVPDPD 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813185915   86 EATETADALRAVADKIRSD--FIVLAGD--LITDCVLHNVADLHRINDATVTMLLKQEVAEVP 144
Cdd:pfam12804  67 PGQGPLAGLLAALRAAPGAdaVLVLACDmpFLTPELLRRLLAAAEESGADIVVPVYDGGRGHP 129
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 5-58 7.91e-06

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: 46.37  E-value: 7.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAK 58
Cdd:cd02541    2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGR 55
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-133 1.13e-05

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: 45.24  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLyplteETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVT-AKEmlDQVQSYVLGqydgkISVTVVAVE 84
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgAEA--DAVRAALAG-----LPVVVVINP 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 813185915  85 GEATETADALRAVADKIRSD---FIVLAGD--LITDCVLHNVADLHRINDATVT 133
Cdd:cd04182   71 DWEEGMSSSLAAGLEALPADadaVLILLADqpLVTAETLRALIDAFREDGAGIV 124
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 6-56 1.46e-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: 44.80  E-value: 1.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 813185915   6 AVILAGGSGVRLYplteeTPKPLLLVNGKPLIYYQLALLENSgFSDVLLVT 56
Cdd:COG0746    7 GVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVA 51
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-56 7.62e-05

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: 42.56  E-value: 7.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 813185915   6 AVILAGGSGVRLyplteETPKPLLLVNGKPLIYYQLALLENSgFSDVLLVT 56
Cdd:cd02503    3 GVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISA 47
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 6-160 1.49e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 43.30  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGK-PLIYYQLALLENSGFSDVLLVTakemldQVQSYVL------------GQY 72
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIGGNyRLIDIPMSNCINSGINKIYVLT------QFNSASLnrhlsraynfgnGGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  73 DGKISVTVVAVE---GEA---TETADALR-------AVADKIRSDFIVLAGD---------LITDcvlhnvadlHRINDA 130
Cdd:PLN02241  80 FGDGFVEVLAATqtpGEKgwfQGTADAVRqflwlfeDAKNKNVEEVLILSGDhlyrmdymdFVQK---------HRESGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 813185915 131 TVTmllkqeVAEVPTAKSKAAS---------------KEKPRRDE 160
Cdd:PLN02241 151 DIT------IACLPVDESRASDfglmkiddtgriiefSEKPKGDE 189
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 6-72 2.03e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 42.51  E-value: 2.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGK-PLIYYQLALLENSGFsdvllvtakemldqVQSYVLGQY 72
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNLVNSGY--------------LRIYVLTQY 61
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 6-130 6.10e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 40.99  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRlypLTEETPKPLLLVNGKPLIYYQL-ALLENSGFSDVLLVTAKEMLDQVQSYVlgqyDGKISVTVvaVE 84
Cdd:PRK09382   8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLeNLSSAPAFKEIVVVIHPDDIAYMKKAL----PEIKFVTL--VT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 813185915  85 GEATEtADALRAVADKIRSDFIvlagdLITD----CVLHNVadLHRINDA 130
Cdd:PRK09382  79 GGATR-QESVRNALEALDSEYV-----LIHDaarpFVPKEL--IDRLIEA 120
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 7-146 8.66e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.73  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   7 VILAGGSGVRLyplTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMlDQVQSYVLGqydgkiSVTVVAVEGE 86
Cdd:PRK14358  11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGA-EQVEAALQG------SGVAFARQEQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813185915  87 ATETADALRAVADKIR---SDFIVLAGD--LITDCVLHNVADLHRINDATVTMLlkqeVAEVPTA 146
Cdd:PRK14358  81 QLGTGDAFLSGASALTegdADILVLYGDtpLLRPDTLRALVADHRAQGSAMTIL----TGELPDA 141
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 6-34 9.22e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.64  E-value: 9.22e-04
                         10        20
                 ....*....|....*....|....*....
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGK 34
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGK 34
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-135 1.03e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.62  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLyplTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMlDQVQSYVlgqydGKISVTV-VAVE 84
Cdd:PRK14353   8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGA-EAVAAAA-----AKIAPDAeIFVQ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 813185915  85 GEATETADALRAVADKIRS---DFIVLAGD--LITDCVLHNVADLHRiNDATVTML 135
Cdd:PRK14353  79 KERLGTAHAVLAAREALAGgygDVLVLYGDtpLITAETLARLRERLA-DGADVVVL 133
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-145 1.53e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.81  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRlypLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVTAKEMlDQVQSYVLGQydgkisvTVVAVEG 85
Cdd:PRK14354   5 AIILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGA-EEVKEVLGDR-------SEFALQE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813185915  86 EATETADALRAVADKIRS---DFIVLAGD--LITDCVLHNVADLHRINDATVTMLlkQEVAEVPT 145
Cdd:PRK14354  74 EQLGTGHAVMQAEEFLADkegTTLVICGDtpLITAETLKNLIDFHEEHKAAATIL--TAIAENPT 136
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-56 2.81e-03

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 38.72  E-value: 2.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 813185915   1 MAEYQAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVT 56
Cdd:PRK10122   1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT 56
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-58 4.98e-03

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 38.09  E-value: 4.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLL-LVNgKPLIyyQLALLE--NSGFSDVLLVTAK 58
Cdd:COG1210    6 AVIPVAGLGTRFLPATKAIPKEMLpIVD-KPLI--QYVVEEavAAGIEEIIFVTGR 58
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 6-144 6.13e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.93  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGK-PLIYYQLALLENSGFSDVLLVTakemldQVQSYVLGQY---------DGK 75
Cdd:PRK05293   6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLELNNHigigspwdlDRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813185915  76 IS-VTV----VAVEGEA--TETADAL---RAVADKIRSDFI-VLAGDLITDCVLHNVADLHRINDATVTMllkqEVAEVP 144
Cdd:PRK05293  80 NGgVTIlppySESEGGKwyKGTAHAIyqnIDYIDQYDPEYVlILSGDHIYKMDYDKMLDYHKEKEADVTI----AVIEVP 155
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 6-56 6.63e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 37.90  E-value: 6.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 813185915   6 AVILAGGSGVRLYPLTEETPKPLLLVNGK-PLIYYQLALLENSGFSDVLLVT 56
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT 69
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 1-37 7.24e-03

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 37.81  E-value: 7.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 813185915   1 MAEYQAVILAGGSGVRLypltEETPKPLLLVNGKPLI 37
Cdd:PRK14489   3 ISQIAGVILAGGLSRRM----NGRDKALILLGGKPLI 35
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
5-56 7.52e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 37.58  E-value: 7.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 813185915   5 QAVILAGGSGVRLYPLTEETPKPLLLVNGKPLIYYQLALLENSGFSDVLLVT 56
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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