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Conserved domains on  [gi|1926443793|gb|QOV08905|]
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Glucose-1-phosphate cytidylyltransferase [uncultured Actinomycetes bacterium]

Protein Classification

glucose-1-phosphate cytidylyltransferase( domain architecture ID 10118576)

glucose-1-phosphate cytidylyltransferase catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-254 3.38e-165

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: 457.03  E-value: 3.38e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFDMRTNS 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 MEIHDNKTEPWRVTLVDTGAETMTGGRLKRIAEYV-QDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAVQPLGRFG 161
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLgDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 162 ALEIDGSGTVTSFTEKPLGDGNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRDKNY 241
Cdd:cd02524   161 ELDLDDDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240

                         250
                  ....*....|...
gi 1926443793 242 LEKLWKENKAPWR 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-254 3.38e-165

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: 457.03  E-value: 3.38e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFDMRTNS 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 MEIHDNKTEPWRVTLVDTGAETMTGGRLKRIAEYV-QDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAVQPLGRFG 161
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLgDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 162 ALEIDGSGTVTSFTEKPLGDGNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRDKNY 241
Cdd:cd02524   161 ELDLDDDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240

                         250
                  ....*....|...
gi 1926443793 242 LEKLWKENKAPWR 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
 2-256 1.31e-160

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: 445.35  E-value: 1.31e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFDMRTN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  82 SMEIHDNKTEPWRVTLVDTGAETMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAVQPLGRFG 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 162 ALEIDGsGTVTSFTEKPLGDGNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRDKNY 241
Cdd:TIGR02623 161 ALDLEG-EQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239

                         250
                  ....*....|....*
gi 1926443793 242 LEKLWKENKAPWRVW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-256 3.91e-99

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: 288.97  E-value: 3.91e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSnyflhnsdvtfdmrtn 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFG---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  82 smeihDNKTEPWRVTLVDTGAETMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAV--QPLGR 159
Cdd:COG1208    65 -----DGSRFGVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 160 FGALEIDGSGTVTSFTEKPLGD-GNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRD 238
Cdd:COG1208   140 YGVVELDGDGRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPED 219

                         250
                  ....*....|....*...
gi 1926443793 239 KNYLEKLWKENKAPWRVW 256
Cdd:COG1208   220 LLEANALLLSGKAPVVIW 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-221 6.90e-19

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: 82.69  E-value: 6.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADK-PMLWHIMKIYSHYGYNDF-VICLGYKGYTIKEYFSNYFLHNSDVTFDMR 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIiVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  80 TNsmeiHDNktepwrvtlvdtgaetmTGGRLKRIAEYVQDE--TFFMTYGDGVADVNLQELLAAHQASGKEVTLT----A 153
Cdd:pfam00483  81 PE----GKG-----------------TAPAVALAADFLGDEksDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTfgivP 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926443793 154 VQPLGRFGALEIDGSGTVTSFTEKPLGD--GNWINGGFFVCEPSALNRIQGD-ETSWEAQP-----LESLAADHQL 221
Cdd:pfam00483 140 VEPPTGYGVVEFDDNGRVIRFVEKPKLPkaSNYASMGIYIFNSGVLDFLAKYlEELKRGEDeitdiLPKALEDGKL 215
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-76 3.33e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 50.76  E-value: 3.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926443793   3 VVILAGGLGTRLSEETalkPKPMAEIADKPMLWHIMKiySHYGYNDFV-ICLGYKGYTIKEYFSNYFlhnSDVTF 76
Cdd:PRK14359    5 IIILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYF---PGVIF 71
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-254 3.38e-165

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: 457.03  E-value: 3.38e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFDMRTNS 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 MEIHDNKTEPWRVTLVDTGAETMTGGRLKRIAEYV-QDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAVQPLGRFG 161
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLgDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 162 ALEIDGSGTVTSFTEKPLGDGNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRDKNY 241
Cdd:cd02524   161 ELDLDDDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240

                         250
                  ....*....|...
gi 1926443793 242 LEKLWKENKAPWR 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
 2-256 1.31e-160

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: 445.35  E-value: 1.31e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFDMRTN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  82 SMEIHDNKTEPWRVTLVDTGAETMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAVQPLGRFG 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 162 ALEIDGsGTVTSFTEKPLGDGNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRDKNY 241
Cdd:TIGR02623 161 ALDLEG-EQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239

                         250
                  ....*....|....*
gi 1926443793 242 LEKLWKENKAPWRVW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-256 3.91e-99

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: 288.97  E-value: 3.91e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSnyflhnsdvtfdmrtn 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFG---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  82 smeihDNKTEPWRVTLVDTGAETMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAV--QPLGR 159
Cdd:COG1208    65 -----DGSRFGVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 160 FGALEIDGSGTVTSFTEKPLGD-GNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWQPMDTLRD 238
Cdd:COG1208   140 YGVVELDGDGRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPED 219

                         250
                  ....*....|....*...
gi 1926443793 239 KNYLEKLWKENKAPWRVW 256
Cdd:COG1208   220 LLEANALLLSGKAPVVIW 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-234 1.37e-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: 175.08  E-value: 1.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFdmrtns 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEY------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 meIHDnkTEPWrvtlvdtgaetMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTA--VQPLGRF 160
Cdd:cd04181    75 --VVQ--EEPL-----------GTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVkeVEDPSRY 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926443793 161 GALEIDGSGTVTSFTEKP-LGDGNWINGGFFVCEPSALNRIQGDETSWEAQP---LESLAADHQLNAFQHHGFWQPMD 234
Cdd:cd04181   140 GVVELDDDGRVTRFVEKPtLPESNLANAGIYIFEPEILDYIPEILPRGEDELtdaIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-224 1.84e-47

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: 156.94  E-value: 1.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFsnyflhnsdvtfdmrtns 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 meiHDNKTEPWRVTLVDtGAETM-TGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTA--VQPLGR 159
Cdd:cd06915    63 ---GDGYRGGIRIYYVI-EPEPLgTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALrrVPDASR 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926443793 160 FGALEIDGSGTVTSFTEKPLGDG-NWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAF 224
Cdd:cd06915   139 YGNVTVDGDGRVIAFVEKGPGAApGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGF 204
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-243 6.66e-35

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: 125.02  E-value: 6.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLH-NSDVTFdmr 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKlGIKITF--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  80 tnSMEihdnkTEPwrvtlvdTGaetmTGGRLKRIAEYV--QDETFFMTYGDGVADVNLQELLAAHQASGKEVTL--TAVQ 155
Cdd:cd06425    78 --SIE-----TEP-------LG----TAGPLALARDLLgdDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTIlvTKVE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 156 PLGRFGALEID-GSGTVTSFTEKPLG-DGNWINGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQLNAFQHHGFWqpM 233
Cdd:cd06425   140 DPSKYGVVVHDeNTGRIERFVEKPKVfVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFW--M 217

                         250
                  ....*....|
gi 1926443793 234 DTLRDKNYLE 243
Cdd:cd06425   218 DIGQPKDFLK 227
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-230 9.20e-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: 121.46  E-value: 9.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYFLHNSDVTFdmrtns 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISY------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 meIHDNKTepwrvtlvdTGaetmTGGRLKRIAEYvQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTA----VQ-Pl 157
Cdd:cd06426    75 --VREDKP---------LG----TAGALSLLPEK-PTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQvP- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926443793 158 grFGALEIDGsGTVTSFTEKPlgDGNW-INGGFFVCEPSALNRIQGDETSWEAQPLESLAADHQ-LNAFQHHGFW 230
Cdd:cd06426   138 --YGVVETEG-GRITSIEEKP--THSFlVNAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKkVGVFPIHEYW 207
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-221 6.90e-19

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: 82.69  E-value: 6.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADK-PMLWHIMKIYSHYGYNDF-VICLGYKGYTIKEYFSNYFLHNSDVTFDMR 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIiVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  80 TNsmeiHDNktepwrvtlvdtgaetmTGGRLKRIAEYVQDE--TFFMTYGDGVADVNLQELLAAHQASGKEVTLT----A 153
Cdd:pfam00483  81 PE----GKG-----------------TAPAVALAADFLGDEksDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTfgivP 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926443793 154 VQPLGRFGALEIDGSGTVTSFTEKPLGD--GNWINGGFFVCEPSALNRIQGD-ETSWEAQP-----LESLAADHQL 221
Cdd:pfam00483 140 VEPPTGYGVVEFDDNGRVIRFVEKPKLPkaSNYASMGIYIFNSGVLDFLAKYlEELKRGEDeitdiLPKALEDGKL 215
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-247 1.04e-18

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 82.21  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNY-----FLHNSDvtF 76
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPgpdvtFVYNPD--Y 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  77 DmRTNSMeihdnktepwrVTLvdtgaetMTGgrlkriAEYVQDETFFMtYGDGVADVNLQELLAAHQAsgkEVTLtAVQP 156
Cdd:COG1213    79 D-ETNNI-----------YSL-------WLA------REALDEDFLLL-NGDVVFDPAILKRLLASDG---DIVL-LVDR 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 157 LGRFGA-----LEIDGSGTVTSFTEKPlgDGNWING---GFFVCEPSALNRI----------QGDETSWEAQPLESLAAD 218
Cdd:COG1213   129 KWEKPLdeevkVRVDEDGRIVEIGKKL--PPEEADGeyiGIFKFSAEGAAALrealealideGGPNLYYEDALQELIDEG 206

                         250       260       270
                  ....*....|....*....|....*....|
gi 1926443793 219 HQLNAFQ-HHGFWQPMDTLRDKNYLEKLWK 247
Cdd:COG1213   207 GPVKAVDiGGLPWVEIDTPEDLERAEELFA 236
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-83 9.86e-17

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 76.50  E-value: 9.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNY----FLHNSDvtFDm 78
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpnikFVYNPD--YA- 77


                  ....*
gi 1926443793  79 RTNSM 83
Cdd:cd02523    78 ETNNI 82
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-238 3.99e-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: 74.91  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPML-WHIMKIYsHYGYNDFVICLGYKGYTIKEYFSNYFlHNSDVTFdmrt 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIdHALDRLA-AAGIRRIVVNTHHLADQIEAHLGDSR-FGLRITI---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  81 nSMEihdnktepwRVTLVDTGaetmtGGrLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVTLTAvqPLGR- 159
Cdd:cd06422    75 -SDE---------PDELLETG-----GG-IKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLL--PLVRn 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 160 -----FGALEIDGSGTVTSFTEKplGDGNWINGGFFVCEPSALNRIQGDETS----WEAqplesLAADHQLNAFQHHGFW 230
Cdd:cd06422   137 pghngVGDFSLDADGRLRRGGGG--AVAPFTFTGIQILSPELFAGIPPGKFSlnplWDR-----AIAAGRLFGLVYDGLW 209


                  ....*...
gi 1926443793 231 QPMDTLRD 238
Cdd:cd06422   210 FDVGTPER 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-178 1.38e-13

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: 67.98  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFsnyflhNSDVTFDMrt 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL------GDGSRFGV-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  81 nsmeihdnktepwRVTLVDTGAETMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQASGKEVT--LTAVQPLG 158
Cdd:cd04189    73 -------------RITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASilLAEVEDPR 139

                         170       180
                  ....*....|....*....|
gi 1926443793 159 RFGALEIDGsGTVTSFTEKP 178
Cdd:cd04189   140 RFGVAVVDD-GRIVRLVEKP 158
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-178 1.92e-09

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 56.64  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLG-YKGYTIKEYFSNyflhNSDvtFDMr 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGD----GSQ--LGI- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  80 tnsmeihdnktepwRVTLVDTGAETMTGGRLKRIAEYVQDETFFMTYGDGV--ADvNLQELLAAHQASGKEVTLTA--VQ 155
Cdd:COG1209    74 --------------KISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIfyGD-GLSELLREAAARESGATIFGykVE 138

                         170       180
                  ....*....|....*....|...
gi 1926443793 156 PLGRFGALEIDGSGTVTSFTEKP 178
Cdd:COG1209   139 DPERYGVVEFDEDGRVVSLEEKP 161
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 1.69e-08

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 53.80  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGG--LGTR---LSEETalkPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYkgYTiKEYFSNYFlhnSDVTFD 77
Cdd:cd06428     1 AVILVGGpqKGTRfrpLSLDV---PKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGF--YP-ESVFSDFI---SDAQQE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  78 MRTNSMEIhdnkTEPwrvtlvdtgAETMTGGRLKriaeYVQD-------ETFFMTYGDGVADVNLQELLAAHQASGKEVT 150
Cdd:cd06428    72 FNVPIRYL----QEY---------KPLGTAGGLY----HFRDqilagnpSAFFVLNADVCCDFPLQELLEFHKKHGASGT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 151 LTAVQPL----GRFGALEID-GSGTVTSFTEKPLGD-GNWINGGFFVCEPSALNRI---------------------QGD 203
Cdd:cd06428   135 ILGTEASreqaSNYGCIVEDpSTGEVLHYVEKPETFvSDLINCGVYLFSPEIFDTIkkafqsrqqeaqlgddnnregRAE 214

                         250       260
                  ....*....|....*....|....*..
gi 1926443793 204 ETSWEAQPLESLAADHQLNAFQHHGFW 230
Cdd:cd06428   215 VIRLEQDVLTPLAGSGKLYVYKTDDFW 241
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-178 2.53e-08

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: 52.96  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVIClgykgyTIKEYFSNYF-LHNSDVTFDMR 79
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII------STPEDLPLFKeLLGDGSDLGIR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  80 TnSMEIHDnktEPwrvtlvDTGAETMTGGRlkriaEYVQDETFFMTYGDGV-ADVNLQELL--AAHQASGKEVTLTAVQP 156
Cdd:cd02538    75 I-TYAVQP---KP------GGLAQAFIIGE-----EFIGDDPVCLILGDNIfYGQGLSPILqrAAAQKEGATVFGYEVND 139

                         170       180
                  ....*....|....*....|..
gi 1926443793 157 LGRFGALEIDGSGTVTSFTEKP 178
Cdd:cd02538   140 PERYGVVEFDENGRVLSIEEKP 161
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-172 1.85e-07

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 51.18  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRL-SEetalKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYflhnsDVTFdmr 79
Cdd:COG1207     3 LAVVILAAGKGTRMkSK----LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL-----DVEF--- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  80 tnsmeihdnktepwrvtlVD------TGAETMTGgrLKRIAEYvqDETFFMTYGdgvaDV------NLQELLAAHQASGK 147
Cdd:COG1207    71 ------------------VLqeeqlgTGHAVQQA--LPALPGD--DGTVLVLYG----DVpliraeTLKALLAAHRAAGA 124

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1926443793 148 EVT-LTAVQP----LGRfgaleI--DGSGTVT 172
Cdd:COG1207   125 AATvLTAELDdptgYGR-----IvrDEDGRVL 151
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-154 2.47e-07

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: 49.96  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYND-FVICLGYKGYTIKEYFSNYFLhnsdvtfdmr 79
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDvIVVVPEEEQAEISTYLRSFPL---------- 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926443793  80 tNSMEIHDNKTEPwrvtlvdtGAETMTGGRLKRIAEYVQDETFFMTYGDGVADVNLQELLAAHQAsgKEVTLTAV 154
Cdd:cd04198    71 -NLKQKLDEVTIV--------LDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRS--HDASLTVL 134
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-76 3.33e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 50.76  E-value: 3.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926443793   3 VVILAGGLGTRLSEETalkPKPMAEIADKPMLWHIMKiySHYGYNDFV-ICLGYKGYTIKEYFSNYFlhnSDVTF 76
Cdd:PRK14359    5 IIILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYF---PGVIF 71
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-178 9.58e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 48.92  E-value: 9.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   4 VILAGGLGTRLSEETALKPKPMAEIADKpmlwhimkiyshygYN--DFVIclgykgytikeyfSNyfLHNSDvtfdMRT- 80
Cdd:COG0448     5 IILAGGRGSRLGPLTKDRAKPAVPFGGK--------------YRiiDFPL-------------SN--CVNSG----IRRv 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  81 ------NSMEIHD--NKTEPWR-------VTLVdTGAETMTGGRLKR-IAEYV-QDETFFMTY---------GDGVADVN 134
Cdd:COG0448    52 gvltqyKSHSLNDhiGSGKPWDldrkrggVFIL-PPYQQREGEDWYQgTADAVyQNLDFIERSdpdyvlilsGDHIYKMD 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1926443793 135 LQELLAAHQASGKEVTLtAVQPL-----GRFGALEIDGSGTVTSFTEKP 178
Cdd:COG0448   131 YRQMLDFHIESGADITV-ACIEVpreeaSRFGVMEVDEDGRITEFEEKP 178
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 127-214 1.09e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 49.11  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 127 GDGVADVNLQELLAAHQASGKEVTLtAVQPLGR-----FGALEIDGSGTVTSFTEKPLGDgnwinggffvcepsALNRIQ 201
Cdd:PRK02862  124 GDQLYRMDYRLFVQHHRETGADITL-AVLPVDEkdasgFGLMKTDDDGRITEFSEKPKGD--------------ELKAMA 188

                          90
                  ....*....|...
gi 1926443793 202 GDETSWEAQPLES 214
Cdd:PRK02862  189 VDTSRLGLSPEEA 201
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-178 1.68e-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: 47.91  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMK--IYShyGYNDFVICLGYKGYTIKEYF-SNYFLHNsdvtFD 77
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEeaVAA--GIEDIIIVTGRGKRAIEDHFdRSYELEE----TL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  78 MRTNSMEIHDNKTEpwRVTLVD----TGAETM-TGGRLKRIAEYVQDETFFMTYGDGV---ADVNLQELLAAHQASGKEV 149
Cdd:cd02541    75 EKKGKTDLLEEVRI--ISDLANihyvRQKEPLgLGHAVLCAKPFIGDEPFAVLLGDDLidsKEPCLKQLIEAYEKTGASV 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1926443793 150 tlTAVQP-----LGRFGALEI----DGSGTVTSFTEKP 178
Cdd:cd02541   153 --IAVEEvppedVSKYGIVKGekidGDVFKVKGLVEKP 188
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-141 3.68e-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: 46.48  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYND-FVICLGYKGyTIKEYFSNYFLHNSdvtfdmr 79
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEvFVVCCEHSQ-AIIEHLLKSKWSSL------- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926443793  80 tNSMEIHDNKTEPwrvtlvdtGAETM-TGGRLKRIAEYVQDEtFFMTYGDGVADVNLQELLAA 141
Cdd:cd02507    73 -SSKMIVDVITSD--------LCESAgDALRLRDIRGLIRSD-FLLLSCDLVSNIPLSELLEE 125
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-176 7.60e-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: 45.58  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRL-SEetalKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYflhnsDVTFdmrtn 81
Cdd:cd02540     1 AVILAAGKGTRMkSD----LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-----NVEF----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  82 smeIHdnKTEPwrvtlvdTGaetmTGGRLKRIAEYVQD--ETFFMTYGDG--VADVNLQELLAAHQASGKEVT-LTAV-- 154
Cdd:cd02540    67 ---VL--QEEQ-------LG----TGHAVKQALPALKDfeGDVLVLYGDVplITPETLQRLLEAHREAGADVTvLTAEle 130

                         170       180
                  ....*....|....*....|..
gi 1926443793 155 QPLGrFGALEIDGSGTVTSFTE 176
Cdd:cd02540   131 DPTG-YGRIIRDGNGKVLRIVE 151
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 127-181 1.90e-05

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 45.23  E-value: 1.90e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793 127 GDGVADVNLQELLAAHQASGKEVTLtAVQPLG-----RFGALEIDGSGTVTSFTEKPLGD 181
Cdd:PLN02241  130 GDHLYRMDYMDFVQKHRESGADITI-ACLPVDesrasDFGLMKIDDTGRIIEFSEKPKGD 188
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-51 5.63e-05

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: 42.90  E-value: 5.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1926443793   3 VVILAGGLGTRLSeetALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVI 51
Cdd:cd02516     3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIV 48
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-208 7.23e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.43  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLseETALkPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYfsnyfLHNSDVTFDMRT 80
Cdd:PRK14358    8 LDVVILAAGQGTRM--KSAL-PKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAA-----LQGSGVAFARQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  81 NSMeihdnktepwrvtlvDTGAETMTGGRlkriAEYVQDETFFMTYGDG--VADVNLQELLAAHQASGKEVT-LTAVQPL 157
Cdd:PRK14358   80 QQL---------------GTGDAFLSGAS----ALTEGDADILVLYGDTplLRPDTLRALVADHRAQGSAMTiLTGELPD 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926443793 158 GR-FGALEIDGSGTV--------TSFTEKPLGDgnwINGGFFVCE---PSALNRIQGDETSWE 208
Cdd:PRK14358  141 ATgYGRIVRGADGAVeriveqkdATDAEKAIGE---FNSGVYVFDaraPELARRIGNDNKAGE 200
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 136-178 1.46e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 42.51  E-value: 1.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1926443793 136 QELLAAHQASGKEVTLTAV-QPLGR---FGALEIDGSGTVTSFTEKP 178
Cdd:PRK00844  134 RQMVDFHIESGAGVTVAAIrVPREEasaFGVIEVDPDGRIRGFLEKP 180
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-73 1.76e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 41.30  E-value: 1.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926443793   3 VVILAGGLGTRLSEetalkPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNY---FLHNSD 73
Cdd:COG2068     6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLgvrVVVNPD 74
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-37 3.43e-04

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 39.87  E-value: 3.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1926443793   3 VVILAGGLGTRLSEetalkPKPMAEIADKPMLWHI 37
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERV 30
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-177 4.39e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.27  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   4 VILAGGLGTRLSEETalkPKPMAEIADKPML-WHIMKIYSHyGYNDFVICLGYKGYTIKEYFSNyflhNSDVTFDMRtns 82
Cdd:PRK14355    7 IILAAGKGTRMKSDL---VKVMHPLAGRPMVsWPVAAAREA-GAGRIVLVVGHQAEKVREHFAG----DGDVSFALQ--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793  83 meihdnktepwrvtlvdtgAETMTGGRLKRIAEYVQDE---TFFMTYGDG--VADVNLQELLAAHQASGKEVT-LTAV-- 154
Cdd:PRK14355   76 -------------------EEQLGTGHAVACAAPALDGfsgTVLILCGDVplLRAETLQGMLAAHRATGAAVTvLTARle 136

                         170       180
                  ....*....|....*....|...
gi 1926443793 155 QPLGrFGALEIDGSGTVTSFTEK 177
Cdd:PRK14355  137 NPFG-YGRIVRDADGRVLRIVEE 158
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 3-69 5.09e-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: 5.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926443793   3 VVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFV-ICLgykgytiKEYFSNYFL 69
Cdd:cd04183     1 IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIfICR-------DEHNTKFHL 61
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-37 8.47e-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: 39.10  E-value: 8.47e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1926443793   6 LAGGLGTRL-SEEtalkpKPMAEIADKPMLWHI 37
Cdd:COG2266     1 MAGGKGTRLgGGE-----KPLLEICGKPMIDRV 28
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-36 9.39e-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: 39.34  E-value: 9.39e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1926443793   4 VILAGGLGTRLSEETalkPKPMAEIADKPMLWH 36
Cdd:COG1211     1 IIPAAGSGSRMGAGI---PKQFLPLGGKPVLEH 30
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-65 1.11e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 39.71  E-value: 1.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926443793   4 VILAGGLGTRLSEEtalKPKPMAEIADKPMLWHIMK-IYSHYGYNDFVIcLGYKGYTIKEYFS 65
Cdd:PRK14356    9 LILAAGKGTRMHSD---KPKVLQTLLGEPMLRFVYRaLRPLFGDNVWTV-VGHRADMVRAAFP 67
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-38 1.32e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 38.63  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1926443793   1 MKVVILAGGLGTRLSEEtalkPKPMAEIADKPMLWHIM 38
Cdd:PRK00317    4 ITGVILAGGRSRRMGGV----DKGLQELNGKPLIQHVI 37
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-52 1.38e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 38.71  E-value: 1.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1926443793   1 MKVVILAGGLGTRLSEetalkPKPMAEIADKPMLWHIMKIYSHYGYNDFVIC 52
Cdd:cd02503     1 ITGVILAGGKSRRMGG-----DKALLELGGKPLLEHVLERLKPLVDEVVISA 47
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 127-178 1.39e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 39.44  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1926443793 127 GDGVADVNLQELLAAHQASGKEVTLTAVQ-PL---GRFGALEIDGSGTVTSFTEKP 178
Cdd:PRK00725  137 GDHIYKMDYSRMLADHVESGADCTVACLEvPReeaSAFGVMAVDENDRITAFVEKP 192
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-37 2.69e-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: 37.86  E-value: 2.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1926443793   1 MKVVILAGGLGTRLSEetalkPKPMAEIADKPMLWHI 37
Cdd:COG0746     5 ITGVILAGGRSRRMGQ-----DKALLPLGGRPLLERV 36
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-73 3.80e-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: 37.15  E-value: 3.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926443793   3 VVILAGGLGTRLSEetalkPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNY---FLHNSD 73
Cdd:cd04182     3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLpvvVVINPD 71
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-146 5.60e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 37.70  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   1 MKVVILAGGLGTRLSEETalkPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNyflhnsdvtfdmrt 80
Cdd:PRK09451    6 MSVVILAAGKGTRMYSDL---PKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLAD-------------- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926443793  81 nsmeihdnktEPwrVTLVDTGAETMTGGRLKRIAEYVQD-ETFFMTYGDG--VADVNLQELLAAHQASG 146
Cdd:PRK09451   69 ----------EP--LNWVLQAEQLGTGHAMQQAAPFFADdEDILMLYGDVplISVETLQRLRDAKPQGG 125
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-68 5.64e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 37.58  E-value: 5.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926443793   2 KVVILAGGLGTRLSEETALKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKEYFSNYF 68
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSF 76
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-62 7.15e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.50  E-value: 7.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926443793   3 VVILAGGLGTRLSEEtalKPKPMAEIADKPMLWHIMKIYSHYGYNDFVICLGYKGYTIKE 62
Cdd:PRK14354    5 AIILAAGKGTRMKSK---LPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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