CTP synthase (P0A7E5)

Identification
Name:CTP synthase
Synonyms:
  • CTP synthetase
  • UTP--ammonia ligase
Gene Name:pyrG
Enzyme Class:
Biological Properties
General Function:Involved in CTP synthase activity
Specific Function:Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Uridine triphosphate → 1.0ADP + 1.0Cytidine triphosphate + 1.0L-Glutamate + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine triphosphate + 1.0Ammonia ↔ 1.0ADP + 1.0Phosphate + 1.0Cytidine triphosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine triphosphate + 1.0L-Glutamine + 1.0Water ↔ 1.0ADP + 1.0Phosphate + 1.0Cytidine triphosphate + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Ammonia ↔ 1.0ADP + 1.0Phosphate + 1.0Cytidine triphosphate + 1.0L-Glutamate
ReactionCard
SMPDB Reactions:
1.0Uridine triphosphate+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0L-Glutamic acid+1.0Thumb+1.0Thumb+1.0Thumb
1.0Uridine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Adenosine triphosphate + 1.0Uridine triphosphate → 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0Phosphate + 1.0L-Glutamic acid + 1.0Cytidine triphosphate + 1.0ADP + 1.0L-Glutamate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Uridine triphosphate → 1.0ADP + 1.0Cytidine triphosphate + 1.0L-Glutamate + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine triphosphate + 1.0Ammonia → 1.0ADP + 1.0Inorganic phosphate + 1.0Cytidine triphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00285Uridine triphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
CTP synthase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
Process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
pyrimidine nucleotide biosynthetic process
pyrimidine nucleotide metabolic process
Gene Properties
Blattner:b2780
Gene OrientationCounterclockwise
Centisome Percentage:62.63
Left Sequence End2906051
Right Sequence End2907688
Gene Sequence:
>1638 bp
ATGACAACGAACTATATTTTTGTGACCGGCGGGGTCGTATCCTCTCTGGGTAAAGGCATT
GCCGCAGCCTCCCTCGCAGCCATTCTTGAAGCCCGTGGCCTCAATGTGACCATCATGAAA
CTGGATCCGTACATCAACGTCGATCCAGGTACTATGAGCCCAATCCAACACGGGGAAGTG
TTCGTTACTGAAGACGGCGCTGAAACCGACCTGGACCTGGGGCACTACGAGCGTTTCATT
CGTACCAAAATGAGCCGCCGCAACAACTTCACCACGGGTCGTATCTACTCTGACGTTCTG
CGTAAAGAACGCCGCGGTGACTACCTCGGCGCAACCGTGCAGGTTATTCCGCACATCACT
AACGCAATCAAAGAGCGCGTGCTGGAAGGTGGCGAAGGTCATGACGTAGTACTGGTAGAA
ATCGGCGGTACAGTAGGTGATATCGAATCCTTGCCGTTCCTCGAAGCGATTCGCCAGATG
GCTGTTGAAATTGGCCGTGAGCACACTCTGTTTATGCACCTGACGCTGGTGCCGTACATG
GCAGCGTCTGGTGAAGTCAAAACCAAACCGACTCAGCACTCTGTAAAAGAGCTGCTCTCC
ATCGGTATCCAGCCTGACATCCTGATTTGTCGTTCAGATCGCGCTGTTCCGGCGAACGAA
CGTGCGAAGATTGCATTGTTCTGTAATGTTCCGGAAAAAGCGGTTATTTCTCTGAAAGAC
GTCGATTCCATCTATAAAATTCCGGGCCTGTTGAAATCTCAGGGGCTGGACGATTATATT
TGTAAACGATTCAGCTTAAACTGCCCGGAAGCGAATCTGTCCGAATGGGAACAGGTTATC
TTCGAAGAAGCGAACCCGGTAAGTGAAGTCACCATCGGTATGGTCGGCAAGTACATTGAA
CTGCCGGATGCTTATAAATCAGTGATCGAAGCACTGAAACACGGTGGGCTGAAGAATCGT
GTCAGCGTCAACATCAAACTGATCGATTCACAAGATGTTGAAACGCGCGGCGTTGAAATC
CTTAAAGGTCTGGACGCAATCCTCGTACCTGGCGGTTTCGGCTATCGTGGCGTAGAAGGC
ATGATTACGACCGCGCGTTTTGCGCGTGAGAACAATATTCCTTATCTGGGCATTTGCCTG
GGTATGCAGGTGGCGTTAATTGATTACGCTCGCCATGTTGCCAACATGGAGAACGCCAAC
TCTACGGAATTTGTGCCAGACTGTAAGTACCCGGTTGTGGCGCTGATTACCGAGTGGCGC
GATGAAAACGGCAACGTTGAAGTTCGTAGCGAGAAGAGCGATCTCGGCGGTACCATGCGT
CTCGGCGCACAGCAGTGCCAGTTGGTTGACGATAGCCTGGTTCGCCAGCTGTACAATGCG
CCGACAATTGTTGAGCGTCATCGTCACCGTTACGAAGTCAACAACATGCTGTTGAAACAG
ATTGAAGATGCAGGTCTGCGCGTTGCGGGCCGTTCCGGGGATGATCAGTTGGTCGAGATC
ATCGAAGTTCCGAATCACCCGTGGTTCGTGGCTTGCCAGTTCCATCCGGAGTTTACTTCT
ACTCCACGTGATGGTCACCCGCTGTTTGCAGGCTTTGTGAAAGCCGCCAGCGAGTTCCAG
AAACGTCAGGCGAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:545
Protein Molecular Weight:60374
Protein Theoretical pI:6
PDB File:1S1M
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>CTP synthase
MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEV
FVTEDGAETDLDLGHYERFIRTKMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHIT
NAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAVEIGREHTLFMHLTLVPYM
AASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD
VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIE
LPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVETRGVEILKGLDAILVPGGFGYRGVEG
MITTARFARENNIPYLGICLGMQVALIDYARHVANMENANSTEFVPDCKYPVVALITEWR
DENGNVEVRSEKSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQ
IEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQ
KRQAK
References
External Links:
ResourceLink
Uniprot ID:P0A7E5
Uniprot Name:PYRG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675599
PDB ID:1S1M
Ecogene ID:EG10810
Ecocyc:EG10810
ColiBase:b2780
Kegg Gene:b2780
EchoBASE ID:EB0803
CCDB:PYRG_ECOLI
BacMap:16130687
General Reference:
  • Bearne, S. L., Hekmat, O., Macdonnell, J. E. (2001). "Inhibition of Escherichia coli CTP synthase by glutamate gamma-semialdehyde and the role of the allosteric effector GTP in glutamine hydrolysis." Biochem J 356:223-232. Pubmed: 11336655
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Robertson, J. G., Villafranca, J. J. (1993). "Characterization of metal ion activation and inhibition of CTP synthetase." Biochemistry 32:3769-3777. Pubmed: 8385490
  • Weng, M. L., Zalkin, H. (1987). "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain." J Bacteriol 169:3023-3028. Pubmed: 3298209
  • Weng, M., Makaroff, C. A., Zalkin, H. (1986). "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase." J Biol Chem 261:5568-5574. Pubmed: 3514618