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Conserved domains on  [gi|257228944|gb|ACV52992|]
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glucose-1-phosphate cytidylyltransferase [Yersinia pseudotuberculosis]

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 ...
6-260 2.05e-179

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: 493.12  E-value: 2.05e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944    6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFCMRDN 85
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   86 EMVVHQKRVEPWNVTLVDTGEDSMTGGRLRRVKDYVkDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATYPPGRF 165
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYL-DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  166 GALDIKDKQVRSFKEKPKGDGALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLRDKIY 245
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 257228944  246 LHELWEEGRAPWKIW 260
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 ...
6-260 2.05e-179

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: 493.12  E-value: 2.05e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944    6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFCMRDN 85
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   86 EMVVHQKRVEPWNVTLVDTGEDSMTGGRLRRVKDYVkDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATYPPGRF 165
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYL-DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  166 GALDIKDKQVRSFKEKPKGDGALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLRDKIY 245
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 257228944  246 LHELWEEGRAPWKIW 260
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
7-258 1.47e-170

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: 470.52  E-value: 1.47e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFCMRDNE 86
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  87 MVVHQKRVEPWNVTLVDTGEDSMTGGRLRRVKDYVKDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATYPPGRFG 166
Cdd:cd02524   81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 167 ALDIKDK-QVRSFKEKPKGDGALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLRDKIY 245
Cdd:cd02524  161 ELDLDDDgQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                        250
                 ....*....|...
gi 257228944 246 LHELWEEGRAPWK 258
Cdd:cd02524  241 LEELWNSGKAPWK 253
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
6-261 7.65e-98

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: 285.89  E-value: 7.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANyfmhMSDItfcmrdn 85
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD----GSRF------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  86 emvvhqkrvePWNVTLVDTGEDSMTGGRLRRVKDYVKDDEaFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATY--PPG 163
Cdd:COG1208   70 ----------GVRITYVDEGEPLGTGGALKRALPLLGDEP-FLVLNGDILTDLDLAALLAFHREKGADATLALVPvpDPS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 164 RFGALDIKDK-QVRSFKEKPKGD-GALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLR 241
Cdd:COG1208  139 RYGVVELDGDgRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPE 218
                        250       260
                 ....*....|....*....|
gi 257228944 242 DKIYLHELWEEGRAPWKIWE 261
Cdd:COG1208  219 DLLEANALLLSGKAPVVIWP 238
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
6-207 1.88e-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: 81.53  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944    6 KAVILAGGLGTRLSEETVVKPKPMVEIGGK-PILWHIMKLYSSYGINDFVICCGYkgyvikEYFANYFMHMSDITfcmrd 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ------EHRFMLNELLGDGS----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   85 nemvvhqkrvePWNVTLVDTGEDSM--TGGRLRRVKDYVKDDEAFCF-TYGDGVSDVNIAELIAFHKSHGKQATLT---- 157
Cdd:pfam00483  70 -----------KFGVQITYALQPEGkgTAPAVALAADFLGDEKSDVLvLGGDHIYRMDLEQAVKFHIEKAADATVTfgiv 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 257228944  158 ATYPPGRFGALDIKDK-QVRSFKEKPKGDGA--LINGGYFVLSPKVIDLIDGD 207
Cdd:pfam00483 139 PVEPPTGYGVVEFDDNgRVIRFVEKPKLPKAsnYASMGIYIFNSGVLDFLAKY 191
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-86 2.07e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 51.14  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   1 MEIQVkaVILAGGLGTRLSEETvvkPKPMVEIGGKPILWHIMKlySSYGINDFV-ICCGYKGYVIKEYFANYFmhmSDIT 79
Cdd:PRK14359   1 MKLSI--IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYF---PGVI 70

                 ....*..
gi 257228944  80 FCMRDNE 86
Cdd:PRK14359  71 FHTQDLE 77
 
Name Accession Description Interval E-value
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
6-260 2.05e-179

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: 493.12  E-value: 2.05e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944    6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFCMRDN 85
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   86 EMVVHQKRVEPWNVTLVDTGEDSMTGGRLRRVKDYVkDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATYPPGRF 165
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYL-DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  166 GALDIKDKQVRSFKEKPKGDGALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLRDKIY 245
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 257228944  246 LHELWEEGRAPWKIW 260
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
7-258 1.47e-170

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: 470.52  E-value: 1.47e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFCMRDNE 86
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  87 MVVHQKRVEPWNVTLVDTGEDSMTGGRLRRVKDYVKDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATYPPGRFG 166
Cdd:cd02524   81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 167 ALDIKDK-QVRSFKEKPKGDGALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLRDKIY 245
Cdd:cd02524  161 ELDLDDDgQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                        250
                 ....*....|...
gi 257228944 246 LHELWEEGRAPWK 258
Cdd:cd02524  241 LEELWNSGKAPWK 253
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
6-261 7.65e-98

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: 285.89  E-value: 7.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANyfmhMSDItfcmrdn 85
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD----GSRF------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  86 emvvhqkrvePWNVTLVDTGEDSMTGGRLRRVKDYVKDDEaFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATY--PPG 163
Cdd:COG1208   70 ----------GVRITYVDEGEPLGTGGALKRALPLLGDEP-FLVLNGDILTDLDLAALLAFHREKGADATLALVPvpDPS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 164 RFGALDIKDK-QVRSFKEKPKGD-GALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFWQPMDTLR 241
Cdd:COG1208  139 RYGVVELDGDgRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPE 218
                        250       260
                 ....*....|....*....|
gi 257228944 242 DKIYLHELWEEGRAPWKIWE 261
Cdd:COG1208  219 DLLEANALLLSGKAPVVIWP 238
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
7-238 6.26e-56

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: 178.54  E-value: 6.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFcmrdne 86
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEY------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  87 mvVHQKrvepwnvtlvdtgEDSMTGGRLRRVKDYVKDDEAFCFtYGDGVSDVNIAELIAFHKSHGKQATLTAT--YPPGR 164
Cdd:cd04181   75 --VVQE-------------EPLGTAGAVRNAEDFLGDDDFLVV-NGDVLTDLDLSELLRFHREKGADATIAVKevEDPSR 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257228944 165 FGALDIKDK-QVRSFKEKPK-GDGALINGGYFVLSPKVIDLIDGDKST---WEQEPLMTLAAQGELMAFEHAGFWQPMD 238
Cdd:cd04181  139 YGVVELDDDgRVTRFVEKPTlPESNLANAGIYIFEPEILDYIPEILPRgedELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
7-232 4.38e-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: 151.17  E-value: 4.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLseETVVK--PKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFcmrd 84
Cdd:cd06915    1 AVILAGGLGTRL--RSVVKdlPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYY---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  85 nemvvhqkRVEPwnvtlvdtgEDSMTGGRLRRVKDYVKDDEAFCFtYGDGVSDVNIAELIAFHKSHGKQATLTATYPPG- 163
Cdd:cd06915   75 --------VIEP---------EPLGTGGAIKNALPKLPEDQFLVL-NGDTYFDVDLLALLAALRASGADATMALRRVPDa 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257228944 164 -RFGALDI-KDKQVRSFKEKPKGDG-ALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAG 232
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 ...
7-204 3.55e-35

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: 125.32  E-value: 3.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMSDITFCMRDNE 86
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  87 MvvhqkrvepwnvtlvdtGedsmTGGRLRRVKDyvKDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATL-TATY----P 161
Cdd:cd06426   81 L-----------------G----TAGALSLLPE--KPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVcVREYevqvP 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 257228944 162 pgrFGALDIKDKQVRSFKEKPKGDgALINGGYFVLSPKVIDLI 204
Cdd:cd06426  138 ---YGVVETEGGRITSIEEKPTHS-FLVNAGIYVLEPEVLDLI 176
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
6-241 1.16e-33

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: 121.93  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMHMS-DITFCMRD 84
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGiKITFSIET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  85 nemvvhqkrvepwnvtlvdtgEDSMTGGRLRRVKDYV-KDDEAFCFTYGDGVSDVNIAELIAFHKSHGKQATLTATY--P 161
Cdd:cd06425   82 ---------------------EPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKveD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 162 PGRFGAL--DIKDKQVRSFKEKPKG-DGALINGGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQGELMAFEHAGFW---- 234
Cdd:cd06425  141 PSKYGVVvhDENTGRIERFVEKPKVfVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWmdig 220

                 ....*..
gi 257228944 235 QPMDTLR 241
Cdd:cd06425  221 QPKDFLK 227
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-80 2.56e-20

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 86.45  E-value: 2.56e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFMhmsDITF 80
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGP---DVTF 72
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
7-142 5.12e-20

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: 85.75  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYFmhmsDITFcmrdne 86
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYP----NIKF------ 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257228944  87 mvVHQKRVEPWNvtlvdtgedsmTGGRLRRVKDYVKDDeaFCFTYGDGVSDVNIAE 142
Cdd:cd02523   71 --VYNPDYAETN-----------NIYSLYLARDFLDED--FLLLEGDVVFDPSILE 111
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
5-242 1.70e-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: 84.54  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   5 VKAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFanyfmhmsditfcmRD 84
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL--------------GD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  85 NEMVvhqkrvePWNVTLVDTGEDSMTGGRLRRVKDYVKDDEaFCFTYGDGVSDVNIAELIAFHKSHGKQAT--LTATYPP 162
Cdd:cd04189   67 GSRF-------GVRITYILQEEPLGLAHAVLAARDFLGDEP-FVVYLGDNLIQEGISPLVRDFLEEDADASilLAEVEDP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 163 GRFGALDIKDKQVRSFKEKPK---GDGALInGGYFvLSPKVIDLIDGDKSTWEQEPLMTLAAQG------ELMAFEHAGF 233
Cdd:cd04189  139 RRFGVAVVDDGRIVRLVEKPKeppSNLALV-GVYA-FTPAIFDAISRLKPSWRGELEITDAIQWlidrgrRVGYSIVTGW 216

                 ....*....
gi 257228944 234 WQPMDTLRD 242
Cdd:cd04189  217 WKDTGTPED 225
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
6-207 1.88e-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: 81.53  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944    6 KAVILAGGLGTRLSEETVVKPKPMVEIGGK-PILWHIMKLYSSYGINDFVICCGYkgyvikEYFANYFMHMSDITfcmrd 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ------EHRFMLNELLGDGS----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   85 nemvvhqkrvePWNVTLVDTGEDSM--TGGRLRRVKDYVKDDEAFCF-TYGDGVSDVNIAELIAFHKSHGKQATLT---- 157
Cdd:pfam00483  70 -----------KFGVQITYALQPEGkgTAPAVALAADFLGDEKSDVLvLGGDHIYRMDLEQAVKFHIEKAADATVTfgiv 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 257228944  158 ATYPPGRFGALDIKDK-QVRSFKEKPKGDGA--LINGGYFVLSPKVIDLIDGD 207
Cdd:pfam00483 139 PVEPPTGYGVVEFDDNgRVIRFVEKPKLPKAsnYASMGIYIFNSGVLDFLAKY 191
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
6-223 2.51e-16

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: 77.44  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944    6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYK-GYVIKEYFANYFMHMSDITFcmrd 84
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEIVGEGERFGAKITY---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   85 nemvVHQKrvEPWNVtlvdtgedsmtGGRLRRVKDYVKDDEaFCFTYGDGVSDVNIAELIA-FHKSHGKQATLTATYP-P 162
Cdd:TIGR01208  77 ----IVQG--EPLGL-----------AHAVYTARDFLGDDD-FVVYLGDNLIQDGISRFVKsFEEKDYDALILLTKVRdP 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257228944  163 GRFGALDIKD-KQVRSFKEKPK---GDGALIngGYFVLSPKVIDLIDGDKSTWEQEPLMTLAAQG 223
Cdd:TIGR01208 139 TAFGVAVLEDgKRILKLVEKPKeppSNLAVV--GLYMFRPLIFEAIKNIKPSWRGELEITDAIQW 201
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
6-242 5.28e-16

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 74.53  E-value: 5.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKP-ILWHIMKLYsSYGINDFVICCGYKGYVIKEYFANYFMHMsDITFcmrd 84
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPlIDHALDRLA-AAGIRRIVVNTHHLADQIEAHLGDSRFGL-RITI---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  85 nemvvhqkRVEPwnVTLVDTGedsmtGGrLRRVKDYVKDDEAFCFTyGDGVSDVNIAELIAFH--KSHGKQATLTATYPP 162
Cdd:cd06422   75 --------SDEP--DELLETG-----GG-IKKALPLLGDEPFLVVN-GDILWDGDLAPLLLLHawRMDALLLLLPLVRNP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 163 GRFGALDIK-DKQVRSFKEKPKGDGALINGGYFVLSPKVIDLIDGDKST----WEQeplmtLAAQGELMAFEHAGFWQPM 237
Cdd:cd06422  138 GHNGVGDFSlDADGRLRRGGGGAVAPFTFTGIQILSPELFAGIPPGKFSlnplWDR-----AIAAGRLFGLVYDGLWFDV 212

                 ....*
gi 257228944 238 DTLRD 242
Cdd:cd06422  213 GTPER 217
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
7-234 1.53e-15

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: 73.83  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGG--LGTR---LSEETvvkPKPMVEIGGKPILWHIM-KLYSSYGINDFVICCGYKgyviKEYFANYFMHMSditf 80
Cdd:cd06428    1 AVILVGGpqKGTRfrpLSLDV---PKPLFPVAGKPMIHHHIeACAKVPDLKEVLLIGFYP----ESVFSDFISDAQ---- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  81 cmrdnemvvhqkrvEPWNVTLVDTGEDSM--TGGRLRRVKDYVKDD--EAFCFTYGDGVSDVNIAELIAFHKSHGKQATL 156
Cdd:cd06428   70 --------------QEFNVPIRYLQEYKPlgTAGGLYHFRDQILAGnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 157 TATYPPG----RFGAL--DIKDKQVRSFKEKPKGD-GALINGGYFVLSPKVIDLI---------------------DGDK 208
Cdd:cd06428  136 LGTEASReqasNYGCIveDPSTGEVLHYVEKPETFvSDLINCGVYLFSPEIFDTIkkafqsrqqeaqlgddnnregRAEV 215
                        250       260
                 ....*....|....*....|....*.
gi 257228944 209 STWEQEPLMTLAAQGELMAFEHAGFW 234
Cdd:cd06428  216 IRLEQDVLTPLAGSGKLYVYKTDDFW 241
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
5-160 3.03e-13

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: 66.89  E-value: 3.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   5 VKAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGIND-FVICCGYKGYVIKEYFAnyfmhmsdiTFCMR 83
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEvFVVCCEHSQAIIEHLLK---------SKWSS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  84 DNEMVVHQKRVEPwnvtlvdtGEDSM-TGGRLRRVKDYVKDDeaFCFTYGDGVSDVNIAELIA----FHKSHgkQATLTA 158
Cdd:cd02507   72 LSSKMIVDVITSD--------LCESAgDALRLRDIRGLIRSD--FLLLSCDLVSNIPLSELLEerrkKDKNA--IATLTV 139

                 ..
gi 257228944 159 TY 160
Cdd:cd02507  140 LL 141
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
6-182 1.04e-12

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: 65.37  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICC-----GYKGYVIKEYFANYFMHMSDITF 80
Cdd:cd04198    2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqAEISTYLRSFPLNLKQKLDEVTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  81 CmrdnemvvhqkrvepwnvtlvdtGEDSM-TGGRLRRVKDYVKDDeaFCFTYGDGVSDVNIAELIAFHKSHgkQATLTAT 159
Cdd:cd04198   82 V-----------------------LDEDMgTADSLRHIRKKIKKD--FLVLSCDLITDLPLIELVDLHRSH--DASLTVL 134
                        170       180
                 ....*....|....*....|...
gi 257228944 160 YPPGRFGALDIKDKQVRSFKEKP 182
Cdd:cd04198  135 LYPPPVSSEQKGGKGKSKKADER 157
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
6-232 3.41e-12

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: 64.48  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYF-ANYFMHMsditFCMRD 84
Cdd:cd02541    2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFdRSYELEE----TLEKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  85 NEMVVH---QKRVEPWNVTLVDTGEDSMTGGRLRRVKDYVkDDEAFCFTYGDgvsDV------NIAELIAFHKSHGKQAT 155
Cdd:cd02541   78 GKTDLLeevRIISDLANIHYVRQKEPLGLGHAVLCAKPFI-GDEPFAVLLGD---DLidskepCLKQLIEAYEKTGASVI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 156 LTATYPP---GRFGALDIKDKQVRSFK-----EKPKGDGALIN----GGYfVLSPKVIDLIDgdkstwEQEP-------- 215
Cdd:cd02541  154 AVEEVPPedvSKYGIVKGEKIDGDVFKvkglvEKPKPEEAPSNlaivGRY-VLTPDIFDILE------NTKPgkggeiql 226
                        250       260
                 ....*....|....*....|
gi 257228944 216 ---LMTLAAQGELMAFEHAG 232
Cdd:cd02541  227 tdaIAKLLEEEPVYAYVFEG 246
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-161 5.03e-10

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 59.27  E-value: 5.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   4 QVKAVILAGGLGTRL-SEetvvKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYfmhmsDITFcm 82
Cdd:COG1207    2 PLAVVILAAGKGTRMkSK----LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL-----DVEF-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  83 rdnemvVHQKrvEPWnvtlvdtGedsmTGGRLRRVKDYVKDDEAFCF-TYGDG--VSDVNIAELIAFHKSHGKQAT-LTA 158
Cdd:COG1207   71 ------VLQE--EQL-------G----TGHAVQQALPALPGDDGTVLvLYGDVplIRAETLKALLAAHRAAGAAATvLTA 131

                 ...
gi 257228944 159 TYP 161
Cdd:COG1207  132 ELD 134
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-205 1.69e-09

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 57.02  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCG-YKGYVIKEYFANyfmhMSD----ITF 80
Cdd:COG1209    2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGD----GSQlgikISY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  81 cmrdnemvVHQKrvEPwnvtlvD-TGEDSMTGgrlrrvKDYVKDDEaFCFTYGDgvsdvNI------AELIAFHKSHGKQ 153
Cdd:COG1209   78 --------AVQP--EP------LgLAHAFIIA------EDFIGGDP-VALVLGD-----NIfygdglSELLREAAARESG 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 154 ATLTAtYP---PGRFG--ALDiKDKQVRSFKEKP---KGDGALInGGYFvLSPKVIDLID 205
Cdd:COG1209  130 ATIFG-YKvedPERYGvvEFD-EDGRVVSLEEKPkepKSNLAVT-GLYF-YDNDVVEIAK 185
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
7-166 2.53e-09

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: 55.98  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRL-SEetvvKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYfmhmsDITFcmrdn 85
Cdd:cd02540    1 AVILAAGKGTRMkSD----LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-----NVEF----- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  86 emvVHQKrvepwnvtlvdtgEDSMTGGRLRRVKDYVKDDEAFCF-TYGDG--VSDVNIAELIAFHKSHGKQAT-LTATYP 161
Cdd:cd02540   67 ---VLQE-------------EQLGTGHAVKQALPALKDFEGDVLvLYGDVplITPETLQRLLEAHREAGADVTvLTAELE 130

                 ....*.
gi 257228944 162 -PGRFG 166
Cdd:cd02540  131 dPTGYG 136
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
7-260 4.64e-09

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 56.24  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKpilwhimklyssYGINDFVI--CcgykgyvikeyfANyfmhmSDItfcmrD 84
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK------------YRIIDFPLsnC------------VN-----SGI-----R 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  85 NEMVV----------HQKRVEPWN-------VTLV-----DTGEDSMTG---------GRLRRVK-DYVkddeafCFTYG 132
Cdd:COG0448   50 RVGVLtqykshslndHIGSGKPWDldrkrggVFILppyqqREGEDWYQGtadavyqnlDFIERSDpDYV------LILSG 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 133 DGVSDVNIAELIAFHKSHGKQATLtATYP-----PGRFGALDI-KDKQVRSFKEKPK-GDGALINGGYFVLSPKV-IDLI 204
Cdd:COG0448  124 DHIYKMDYRQMLDFHIESGADITV-ACIEvpreeASRFGVMEVdEDGRITEFEEKPKdPKSALASMGIYVFNKDVlIELL 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257228944 205 DGDKSTWE----QEPLMTLAAQGELMAFEHAGFWQP-----------MDTLRDKIYLhELWEEGrapWKIW 260
Cdd:COG0448  203 EEDAPNSShdfgKDIIPRLLDRGKVYAYEFDGYWRDvgtidsyyeanMDLLDPEPEF-NLYDPE---WPIY 269
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-86 2.07e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 51.14  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   1 MEIQVkaVILAGGLGTRLSEETvvkPKPMVEIGGKPILWHIMKlySSYGINDFV-ICCGYKGYVIKEYFANYFmhmSDIT 79
Cdd:PRK14359   1 MKLSI--IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYF---PGVI 70

                 ....*..
gi 257228944  80 FCMRDNE 86
Cdd:PRK14359  71 FHTQDLE 77
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
7-55 2.33e-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: 50.21  E-value: 2.33e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEETvvkPKPMVEIGGKPILWH-IMKLYSSYGINDFVI 55
Cdd:cd02516    3 AIILAAGSGSRMGADI---PKQFLELGGKPVLEHtLEAFLAHPAIDEIVV 49
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
8-57 2.39e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 47.05  E-value: 2.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 257228944   8 VILAGGLGTRLSEETvvkPKPMVEIGGKPILWH-IMKLYSSYGINDFVICC 57
Cdd:COG1211    1 IIPAAGSGSRMGAGI---PKQFLPLGGKPVLEHtLEAFLAHPRIDEIVVVV 48
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
7-60 2.67e-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: 46.03  E-value: 2.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 257228944    7 AVILAGGLGTRLSEetvvkPKPMVEIGGKPILWHIMKLYSSYGiNDFVICCGYK 60
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPAG-DEVVVVANDE 48
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
7-71 1.87e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 44.74  E-value: 1.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257228944   7 AVILAGGLGTRLSEEtvvKPKPMVEIGGKPILWH-IMKLYSSYGINDFVICC--GYKGYVIKEYFANY 71
Cdd:PRK00155   6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHtLEAFLAHPRIDEIIVVVppDDRPDFAELLLAKD 70
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
7-71 2.50e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 44.00  E-value: 2.50e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257228944   7 AVILAGGLGTRLSEetvvkPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANY 71
Cdd:COG2068    6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGL 65
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-41 2.69e-05

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 43.64  E-value: 2.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 257228944   1 MEIQVKAVILAGGLGTRLSEetvvkPKPMVEIGGKPILWHI 41
Cdd:COG0746    1 MTMPITGVILAGGRSRRMGQ-----DKALLPLGGRPLLERV 36
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
7-56 6.98e-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: 6.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEetvvkPKPMVEIGGKPILWHIMKLYSSYGINDFVIC 56
Cdd:cd02503    3 GVILAGGKSRRMGG-----DKALLELGGKPLLEHVLERLKPLVDEVVISA 47
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
6-55 9.49e-05

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: 42.56  E-value: 9.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKP-ILWHIMKLYSSyGINDFVI 55
Cdd:cd02538    2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPmIYYPLSTLMLA-GIREILI 51
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
3-42 1.05e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 42.10  E-value: 1.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 257228944   3 IQVKAVILAGGLGTRLSEEtvvkPKPMVEIGGKPILWHIM 42
Cdd:PRK00317   2 PPITGVILAGGRSRRMGGV----DKGLQELNGKPLIQHVI 37
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
5-148 1.57e-04

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: 41.82  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   5 VKAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGIND-FVICCGYKGYvIKEYFANyfmhmsditfcmr 83
Cdd:cd04197    1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEvFVFCCSHSDQ-IKEYIEK------------- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  84 dnemvvHQKRVEPWNVTLVD--TGEDSMT-GGRLRRVKDY--VKDDeaFCFTYGDGVSDVNIAELIAFHK 148
Cdd:cd04197   67 ------SKWSKPKSSLMIVIiiMSEDCRSlGDALRDLDAKglIRGD--FILVSGDVVSNIDLKEILEEHK 128
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
7-35 2.89e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 41.75  E-value: 2.89e-04
                         10        20
                 ....*....|....*....|....*....
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGK 35
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
10-41 3.06e-04

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 40.64  E-value: 3.06e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 257228944  10 LAGGLGTRL-SEEtvvkpKPMVEIGGKPILWHI 41
Cdd:COG2266    1 MAGGKGTRLgGGE-----KPLLEICGKPMIDRV 28
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
4-43 3.35e-04

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 41.28  E-value: 3.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 257228944   4 QVKAVILAGGLGTRLSEetvvKPKPMVEIGGKPILWHIMK 43
Cdd:PRK14489   5 QIAGVILAGGLSRRMNG----RDKALILLGGKPLIERVVD 40
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
7-202 4.13e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 41.25  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEEtvvKPKPMVEIGGKPILWHIMK-LYSSYGINDFVIcCGYKGYVIKEyfanyfmhmsdiTFCMRDN 85
Cdd:PRK14356   8 ALILAAGKGTRMHSD---KPKVLQTLLGEPMLRFVYRaLRPLFGDNVWTV-VGHRADMVRA------------AFPDEDA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  86 EMVVHQKRVEPWNVtlVDTGEDSMTGGRLRRVkdyvkddeafCFTYGDG--VSDVNIAELIAfhKSHGKQ-ATLTATYP- 161
Cdd:PRK14356  72 RFVLQEQQLGTGHA--LQCAWPSLTAAGLDRV----------LVVNGDTplVTTDTIDDFLK--EAAGADlAFMTLTLPd 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 257228944 162 PGRFGALDIKDKQVRSFKEKPKGDGAL-------INGGYFVLSPKVID 202
Cdd:PRK14356 138 PGAYGRVVRRNGHVAAIVEAKDYDEALhgpetgeVNAGIYYLRLDAVE 185
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
8-73 4.68e-04

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: 40.31  E-value: 4.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257228944   8 VILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFV-ICcgykgyvIKEYFANYFM 73
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIfIC-------RDEHNTKFHL 61
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
7-55 8.23e-04

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: 39.45  E-value: 8.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGKpilwhimklyssYGINDFVI 55
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR------------YRLIDFPL 37
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-232 8.24e-04

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 40.02  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMK-LYSSyGINDFVICCGYKGYVIKEYFANYF------------ 72
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEeAVAA-GIEEIIFVTGRGKRAIEDHFDRSYeleatleakgke 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  73 ---------MHMSDITFcmrdnemvVHQKrvEP-------WnvtlvdtgedsmtggrlrRVKDYVkDDEAFCFTYGDgvs 136
Cdd:COG1210   84 elleevrsiSPLANIHY--------VRQK--EPlglghavL------------------CARPFV-GDEPFAVLLGD--- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944 137 DV------NIAELIAFHKSHGKQATLTATYPP---GRFGALDIKDKQVRSFK-----EKPKGDGA---L-INGGYfVLSP 198
Cdd:COG1210  132 DLidsekpCLKQMIEVYEETGGSVIAVQEVPPeevSKYGIVDGEEIEGGVYRvtglvEKPAPEEApsnLaIVGRY-ILTP 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 257228944 199 KVIDLIDgdkstwEQEP-----------LMTLAAQGELMAFEHAG 232
Cdd:COG1210  211 EIFDILE------KTKPgaggeiqltdaIAALAKEEPVYAYEFEG 249
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
7-71 1.06e-03

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 39.08  E-value: 1.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257228944   7 AVILAGGLGTRLSEetvvkPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANY 71
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL 62
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
7-58 3.00e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 3.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 257228944   7 AVILAGGLGTRLSEETvvkPKPMVEIGGKPILWHIMKLYSSYGINDFVICCG 58
Cdd:PRK14353   8 AIILAAGEGTRMKSSL---PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVG 56
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
7-161 5.49e-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: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   7 AVILAGGLGTRLSEEtvvKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFAnyfmhmsditfcmrDNE 86
Cdd:PRK14354   5 AIILAAGKGTRMKSK---LPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLG--------------DRS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944  87 MVVHQKrvepwnvtlvdtgEDSMTGGRLRRVKDYVKDDEA----FCftyGDG--VSDVNIAELIAFHKSHGKQAT-LTAT 159
Cdd:PRK14354  68 EFALQE-------------EQLGTGHAVMQAEEFLADKEGttlvIC---GDTplITAETLKNLIDFHEEHKAAATiLTAI 131

                 ..
gi 257228944 160 YP 161
Cdd:PRK14354 132 AE 133
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
6-72 5.49e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 37.58  E-value: 5.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257228944   6 KAVILAGGLGTRLSEETVVKPKPMVEIGGKPILWHIMKLYSSYGINDFVICCGYKGYVIKEYFANYF 72
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSF 76
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
7-35 8.07e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.15  E-value: 8.07e-03
                         10        20
                 ....*....|....*....|....*....
gi 257228944   7 AVILAGGLGTRLSEETVVKPKPMVEIGGK 35
Cdd:PRK05293   6 AMILAGGQGTRLGKLTKNIAKPAVPFGGK 34
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-87 8.50e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.03  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257228944   5 VKAVILAGGLGTRLSEETVvkpKPMVEIGGKPIL-WHIMKLYSSyGINDFVICCGYKGYVIKEYFANyfmhMSDITFCMR 83
Cdd:PRK14355   4 LAAIILAAGKGTRMKSDLV---KVMHPLAGRPMVsWPVAAAREA-GAGRIVLVVGHQAEKVREHFAG----DGDVSFALQ 75

                 ....
gi 257228944  84 DNEM 87
Cdd:PRK14355  76 EEQL 79
 
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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