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Conserved domains on  [gi|1885885657|ref|WP_181834187|]
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glucose-1-phosphate cytidylyltransferase [Aquitalea aquatica]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
2-256 1.47e-169

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member TIGR02623:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 254  Bit Score: 468.08  E-value: 1.47e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSDVTIDFSNN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  82 QMEVHERHAEPWRVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAVQPPGRY 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYL-DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 162 GALLTDGAMVTGFREKPPGDGGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLREKSQ 241
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 1885885657 242 LDDLWRSGRAPWKVW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
 
Name Accession Description Interval E-value
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-256 1.47e-169

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 468.08  E-value: 1.47e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSDVTIDFSNN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  82 QMEVHERHAEPWRVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAVQPPGRY 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYL-DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 162 GALLTDGAMVTGFREKPPGDGGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLREKSQ 241
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 1885885657 242 LDDLWRSGRAPWKVW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-254 1.92e-167

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: 462.43  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSDVTIDFSNNQ 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  83 MEVHERHAEPWRVTLLDTGEDTMTGGRLKRVRNYLAAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAVQPPGRYG 162
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 163 AL-LTDGAMVTGFREKPPGDGGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLREKSQ 241
Cdd:cd02524   161 ELdLDDDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                         250
                  ....*....|...
gi 1885885657 242 LDDLWRSGRAPWK 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-256 7.79e-93

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: 273.18  E-value: 7.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANyflhmsdvtidfsnn 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD--------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  82 qmevheRHAEPWRVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAV--QPPG 159
Cdd:COG1208    66 ------GSRFGVRITYVDEGEPLGTGGALKRALPLL-GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 160 RYGALLTDGA-MVTGFREKPPGD-GGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLR 237
Cdd:COG1208   139 RYGVVELDGDgRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPE 218
                         250
                  ....*....|....*....
gi 1885885657 238 EKSQLDDLWRSGRAPWKVW 256
Cdd:COG1208   219 DLLEANALLLSGKAPVVIW 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-246 3.25e-18

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: 80.76  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGK-PILWHIMKIYSSHGINDFIICLGYkgyvikEYFANYFLHMSDvTIDFSN 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ------EHRFMLNELLGD-GSKFGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  81 NQMEVHERhaepwrvtlldtgEDTMTGGRLKRVRNYLAAGESFCF-TYGDGVADIDITAEVAFHRQHGKLATVA----AV 155
Cdd:pfam00483  74 QITYALQP-------------EGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRMDLEQAVKFHIEKAADATVTfgivPV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 156 QPPGRYGALLTDGA-MVTGFREKP--PGDGGWINGGFFVLQPEAIDF-VDNDGTSWEGEPM------AELARHQQLMAFE 225
Cdd:pfam00483 141 EPPTGYGVVEFDDNgRVIRFVEKPklPKASNYASMGIYIFNSGVLDFlAKYLEELKRGEDEitdilpKALEDGKLAYAFI 220
                         250       260
                  ....*....|....*....|..
gi 1885885657 226 HNGF-WqpMDTlrekSQLDDLW 246
Cdd:pfam00483 221 FKGYaW--LDV----GTWDSLW 236
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-80 8.49e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 46.14  E-value: 8.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885885657   4 VILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMKiySSHGINDFI-ICLGYKGYVIKEYFANYFLHMSDVTIDFSN 80
Cdd:PRK14359    6 IILAAGKGTRMKSS---LPKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYFPGVIFHTQDLEN 78
 
Name Accession Description Interval E-value
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-256 1.47e-169

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 468.08  E-value: 1.47e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSDVTIDFSNN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  82 QMEVHERHAEPWRVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAVQPPGRY 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYL-DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 162 GALLTDGAMVTGFREKPPGDGGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLREKSQ 241
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 1885885657 242 LDDLWRSGRAPWKVW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-254 1.92e-167

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: 462.43  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSDVTIDFSNNQ 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  83 MEVHERHAEPWRVTLLDTGEDTMTGGRLKRVRNYLAAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAVQPPGRYG 162
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 163 AL-LTDGAMVTGFREKPPGDGGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLREKSQ 241
Cdd:cd02524   161 ELdLDDDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                         250
                  ....*....|...
gi 1885885657 242 LDDLWRSGRAPWK 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-256 7.79e-93

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: 273.18  E-value: 7.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANyflhmsdvtidfsnn 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD--------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  82 qmevheRHAEPWRVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAV--QPPG 159
Cdd:COG1208    66 ------GSRFGVRITYVDEGEPLGTGGALKRALPLL-GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 160 RYGALLTDGA-MVTGFREKPPGD-GGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGFWQPMDTLR 237
Cdd:COG1208   139 RYGVVELDGDgRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPE 218
                         250
                  ....*....|....*....
gi 1885885657 238 EKSQLDDLWRSGRAPWKVW 256
Cdd:COG1208   219 DLLEANALLLSGKAPVVIW 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-234 1.94e-54

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: 174.69  E-value: 1.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHmsDVTIDFsnnq 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF--GVNIEY---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  83 meVHErhaepwrvtlldtGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAA--VQPPGR 160
Cdd:cd04181    75 --VVQ-------------EEPLGTAGAVRNAEDFL-GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVkeVEDPSR 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1885885657 161 YGALLTDGAM-VTGFREKP-PGDGGWINGGFFVLQPEAIDFVDND---GTSWEGEPMAELARHQQLMAFEHNGFWQPMD 234
Cdd:cd04181   139 YGVVELDDDGrVTRFVEKPtLPESNLANAGIYIFEPEILDYIPEIlprGEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-228 1.84e-45

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: 151.94  E-value: 1.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGGLGTRIseESHLK--PKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHmsDVTIDFSn 80
Cdd:cd06915     1 AVILAGGLGTRL--RSVVKdlPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRG--GIRIYYV- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  81 nqmevherhAEPwrvTLLdtGedtmTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAAVQPPG- 159
Cdd:cd06915    76 ---------IEP---EPL--G----TGGAIKNALPKL-PEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDa 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1885885657 160 -RYGALLTD-GAMVTGFREKPPGDG-GWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNG 228
Cdd:cd06915   137 sRYGNVTVDgDGRVIAFVEKGPGAApGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDG 208
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-230 2.93e-34

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: 122.62  E-value: 2.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANyfLHMSDVTIDFsnnq 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGD--GSKFGVNISY---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  83 meVHERhaEPwrvtlldTGedtmTGGRLKRVRNYLaaGESFCFTYGDGVADIDITAEVAFHRQHGKLATVAA----VQPP 158
Cdd:cd06426    75 --VRED--KP-------LG----TAGALSLLPEKP--TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQVP 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1885885657 159 grYGALLTDGAMVTGFREKPPGDgGWINGGFFVLQPEAIDFVDndgtswEGEP-------MAELARHQQLMAFEHNGFW 230
Cdd:cd06426   138 --YGVVETEGGRITSIEEKPTHS-FLVNAGIYVLEPEVLDLIP------KNEFfdmpdliEKLIKEGKKVGVFPIHEYW 207
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-237 5.30e-34

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: 122.70  E-value: 5.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   1 MKAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSdVTIDFSn 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLG-IKITFS- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  81 nqmevHERhaEPwrvtlldTGedtmTGGRLKRVRNYLAAGESFCFtygdgVADIDITAE------VAFHRQHGKLAT--V 152
Cdd:cd06425    79 -----IET--EP-------LG----TAGPLALARDLLGDDDEPFF-----VLNSDVICDfplaelLDFHKKHGAEGTilV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 153 AAVQPPGRYGALLTDGA--MVTGFREKPPG-DGGWINGGFFVLQPEAIDFVDNDGTSWEGEPMAELARHQQLMAFEHNGF 229
Cdd:cd06425   136 TKVEDPSKYGVVVHDENtgRIERFVEKPKVfVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGF 215
                         250
                  ....*....|..
gi 1885885657 230 W----QPMDTLR 237
Cdd:cd06425   216 WmdigQPKDFLK 227
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-67 2.42e-19

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: 83.82  E-value: 2.42e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1885885657   3 AVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANY 67
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKY 65
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-210 2.91e-19

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: 83.77  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   1 MKAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANyflhmsdvtidfsn 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGD-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  81 nqmevherhAEPW--RVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVAFHRQHGKLAT--VAAVQ 156
Cdd:cd04189    67 ---------GSRFgvRITYILQEEPLGLAHAVLAARDFL-GDEPFVVYLGDNLIQEGISPLVRDFLEEDADASilLAEVE 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1885885657 157 PPGRYGALLTDGAMVTGFREKP---PGDGGWIngGFFVLQPEAIDFVDNDGTSWEGE 210
Cdd:cd04189   137 DPRRFGVAVVDDGRIVRLVEKPkepPSNLALV--GVYAFTPAIFDAISRLKPSWRGE 191
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-129 4.97e-19

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 82.98  E-value: 4.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLHMSDVTIDF--- 78
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPDVTFVYNPDyde 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  79 SNN---------QME----------VHERH------AEPWRVTLL-------DTGEDTM----TGGRL----KRVRNYLA 118
Cdd:COG1213    81 TNNiyslwlareALDedflllngdvVFDPAilkrllASDGDIVLLvdrkwekPLDEEVKvrvdEDGRIveigKKLPPEEA 160
                         170
                  ....*....|....
gi 1885885657 119 AGES---FCFTYGD 129
Cdd:COG1213   161 DGEYigiFKFSAEG 174
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-246 3.25e-18

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: 80.76  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGK-PILWHIMKIYSSHGINDFIICLGYkgyvikEYFANYFLHMSDvTIDFSN 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ------EHRFMLNELLGD-GSKFGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  81 NQMEVHERhaepwrvtlldtgEDTMTGGRLKRVRNYLAAGESFCF-TYGDGVADIDITAEVAFHRQHGKLATVA----AV 155
Cdd:pfam00483  74 QITYALQP-------------EGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRMDLEQAVKFHIEKAADATVTfgivPV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 156 QPPGRYGALLTDGA-MVTGFREKP--PGDGGWINGGFFVLQPEAIDF-VDNDGTSWEGEPM------AELARHQQLMAFE 225
Cdd:pfam00483 141 EPPTGYGVVEFDDNgRVIRFVEKPklPKASNYASMGIYIFNSGVLDFlAKYLEELKRGEDEitdilpKALEDGKLAYAFI 220
                         250       260
                  ....*....|....*....|..
gi 1885885657 226 HNGF-WqpMDTlrekSQLDDLW 246
Cdd:pfam00483 221 FKGYaW--LDV----GTWDSLW 236
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-210 2.43e-13

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: 68.58  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKgyvikeyfanyflhmsdvtidfSNN 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPV----------------------TGE 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  82 QMEVHERHAEPW--RVTLLDTGEDTMTGGRLKRVRNYLaAGESFCFTYGDGVADIDITAEVA-FHRQH-GKLATVAAVQP 157
Cdd:TIGR01208  59 EIKEIVGEGERFgaKITYIVQGEPLGLAHAVYTARDFL-GDDDFVVYLGDNLIQDGISRFVKsFEEKDyDALILLTKVRD 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1885885657 158 PGRYG-ALLTDGAMVTGFREKP---PGDGGWIngGFFVLQPEAIDFVDNDGTSWEGE 210
Cdd:TIGR01208 138 PTAFGvAVLEDGKRILKLVEKPkepPSNLAVV--GLYMFRPLIFEAIKNIKPSWRGE 192
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-200 2.97e-13

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 66.83  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   2 KAVILAGGLGTRISEESHLKPKPMIDIGGKP-ILWHIMKIYSShGINDFIICLGYKGYVIKEYFANYFlhmSDVTIDFSn 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPlIDHALDRLAAA-GIRRIVVNTHHLADQIEAHLGDSR---FGLRITIS- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  81 nqmevHErhaepwRVTLLDTGedtmtGGrLKRVRNyLAAGESFcFTY-GDGVADIDITAEVAFH--RQHGKLATVAAVQP 157
Cdd:cd06422    76 -----DE------PDELLETG-----GG-IKKALP-LLGDEPF-LVVnGDILWDGDLAPLLLLHawRMDALLLLLPLVRN 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1885885657 158 PGRYG----ALLTDGAMvtgFREKPPGDGGWINGGFFVLQPEAIDFV 200
Cdd:cd06422   137 PGHNGvgdfSLDADGRL---RRGGGGAVAPFTFTGIQILSPELFAGI 180
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-230 1.47e-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: 59.96  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGG--LGTRISEESHLKPKPMIDIGGKPILWHIM----KIYSSHGIndFIIclgykGYVIKEYFANYFLHMSdvti 76
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIeacaKVPDLKEV--LLI-----GFYPESVFSDFISDAQ---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657  77 dfsnNQMEVHERHAEpwrvtlldtgEDTM--TGGRLKRVRNYLAAG--ESFCFTYGDGVADIDITAEVAFHRQHGKLATV 152
Cdd:cd06428    70 ----QEFNVPIRYLQ----------EYKPlgTAGGLYHFRDQILAGnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657 153 AAVQPP----GRYGALLTDGAM--VTGFREKPpgdGGW----INGGFFVLQPEAIDFVDN-------------------- 202
Cdd:cd06428   136 LGTEASreqaSNYGCIVEDPSTgeVLHYVEKP---ETFvsdlINCGVYLFSPEIFDTIKKafqsrqqeaqlgddnnregr 212
                         250       260
                  ....*....|....*....|....*....
gi 1885885657 203 -DGTSWEGEPMAELARHQQLMAFEHNGFW 230
Cdd:cd06428   213 aEVIRLEQDVLTPLAGSGKLYVYKTDDFW 241
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-64 8.33e-09

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 55.10  E-value: 8.33e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1885885657   1 MKAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLG-YKGYVIKEYF 64
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLL 65
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-52 7.30e-08

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: 51.51  E-value: 7.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1885885657   1 MKAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIIC 52
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVV 52
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-51 4.79e-07

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 49.06  E-value: 4.79e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1885885657   3 AVILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMKIYSSHGINDFII 51
Cdd:cd02516     3 AIILAAGSGSRMGAD---IPKQFLELGGKPVLEHTLEAFLAHPAIDEIV 48
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-80 1.00e-06

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: 48.02  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   1 MKAVILAGGLGTR---ISEEshlKPKPMIDIGGKPILWHIMKIYSSHGIND-FIICLGYKG----YVIKEYFANYFLHMS 72
Cdd:cd02507     1 FQAVVLADGFGSRflpLTSD---IPKALLPVANVPLIDYTLEWLEKAGVEEvFVVCCEHSQaiieHLLKSKWSSLSSKMI 77

                  ....*...
gi 1885885657  73 DVTIDFSN 80
Cdd:cd02507    78 VDVITSDL 85
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-70 1.81e-06

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: 47.51  E-value: 1.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885885657   3 AVILAGGLGTRIseESHLkPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANYFLH 70
Cdd:cd02540     1 AVILAAGKGTRM--KSDL-PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVE 65
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-69 3.73e-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: 46.76  E-value: 3.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   1 MKAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYF-ANYFL 69
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFdRSYEL 70
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-80 8.49e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 46.14  E-value: 8.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885885657   4 VILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMKiySSHGINDFI-ICLGYKGYVIKEYFANYFLHMSDVTIDFSN 80
Cdd:PRK14359    6 IILAAGKGTRMKSS---LPKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYFPGVIFHTQDLEN 78
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-67 1.14e-05

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: 45.79  E-value: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885885657   1 MKAVILAGGLGTRI-SEeshlKPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANY 67
Cdd:COG1207     3 LAVVILAAGKGTRMkSK----LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL 66
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-69 1.18e-05

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 45.32  E-value: 1.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1885885657   4 VILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFI-ICLgykgyviKEYFANYFL 69
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIfICR-------DEHNTKFHL 61
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-67 2.70e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.61  E-value: 2.70e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1885885657   3 AVILAGGLGTRISEeshlkPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANY 67
Cdd:COG2068     6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGL 65
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-67 4.39e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.58  E-value: 4.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885885657   3 AVILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMKIYSSHG-INDFIICL--GYKGYVIKEYFANY 67
Cdd:PRK00155    6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVppDDRPDFAELLLAKD 70
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-56 1.09e-04

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 41.41  E-value: 1.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1885885657   3 AVILAGGLGTRISEeshlkPKPMIDIGGKPILWHIMKIYSSHGiNDFIICLGYK 56
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPAG-DEVVVVANDE 48
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-52 1.34e-04

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: 41.41  E-value: 1.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1885885657   1 MKAVILAGGLGTRISEeshlkPKPMIDIGGKPILWHIMKIYSSHGINDFIIC 52
Cdd:cd02503     1 ITGVILAGGKSRRMGG-----DKALLELGGKPLLEHVLERLKPLVDEVVISA 47
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-51 1.66e-04

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: 41.65  E-value: 1.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1885885657   4 VILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMKIYSSHGINDFII 51
Cdd:COG1211     1 IIPAAGSGSRMGAG---IPKQFLPLGGKPVLEHTLEAFLAHPRIDEIV 45
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-38 2.42e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 40.94  E-value: 2.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1885885657   1 MKAVILAGGLGTRISEEshlkPKPMIDIGGKPILWHIM 38
Cdd:PRK00317    4 ITGVILAGGRSRRMGGV----DKGLQELNGKPLIQHVI 37
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-67 2.46e-04

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 41.01  E-value: 2.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1885885657   3 AVILAGGLGTRISEeshlkPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFANY 67
Cdd:cd04182     3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL 62
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-51 9.45e-04

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: 39.48  E-value: 9.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1885885657   1 MKAVILAGGLGTRISEESHLKPKPMIDIGGKPILWHIMKIYSSHGINDFII 51
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILI 51
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
3-39 1.06e-03

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 39.74  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1885885657   3 AVILAGGLGTRISEeshlKPKPMIDIGGKPILWHIMK 39
Cdd:PRK14489    8 GVILAGGLSRRMNG----RDKALILLGGKPLIERVVD 40
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-37 1.46e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 38.63  E-value: 1.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1885885657   1 MKAVILAGGLGTRISEeshlkPKPMIDIGGKPILWHI 37
Cdd:COG0746     5 ITGVILAGGRSRRMGQ-----DKALLPLGGRPLLERV 36
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-39 2.08e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.94  E-value: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1885885657   3 AVILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMK 39
Cdd:PRK14356    8 ALILAAGKGTRMHSD---KPKVLQTLLGEPMLRFVYR 41
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
3-51 4.14e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 37.43  E-value: 4.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1885885657   3 AVILAGGLGTRISEEshlKPKPMIDIGGKPILWHIMKIYSSHGINDFII 51
Cdd:pfam01128   1 AVIPAAGSGKRMGAG---VPKQFLQLLGQPLLEHTVDAFLASPVVDRIV 46
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-30 4.81e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 37.74  E-value: 4.81e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1885885657   1 MKAVILAGGLGTR---ISEESHlkPKPMIDIGG 30
Cdd:COG0836     3 IYPVILAGGSGTRlwpLSRESY--PKQFLPLLG 33
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-62 5.27e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.89  E-value: 5.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885885657   3 AVILAGGLGTRIseESHLkPKPMIDIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKE 62
Cdd:PRK14354    5 AIILAAGKGTRM--KSKL-PKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE 61
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-37 8.27e-03

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 36.40  E-value: 8.27e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1885885657   6 LAGGLGTRI-SEEshlkpKPMIDIGGKPILWHI 37
Cdd:COG2266     1 MAGGKGTRLgGGE-----KPLLEICGKPMIDRV 28
 
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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