2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase (P77231)

Identification
Name:2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase
Synonyms:
  • 2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase
Gene Name:citG
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'- dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Dephospho-CoA ↔ 1.02'-(5-Triphosphoribosyl)-3'-dephospho-CoA + 1.0Adenine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Dephospho-CoA → 1.02'-(5-Triphosphoribosyl)-3'-dephospho-CoA + 1.0Adenine
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0Dephospho-CoA + 1.0Adenosine triphosphate → 1.02'-(5-Triphosphoribosyl)-3'-dephospho-CoA + 1.0Adenine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB202232'-(5-Triphosphoribosyl)-3'-dephospho-CoAMetaboCard
ECMDB00034AdenineMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01373Dephospho-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular metabolic process
metabolic process
phosphate metabolic process
phosphorus metabolic process
phosphorylation
Gene Properties
Blattner:b0613
Gene OrientationCounterclockwise
Centisome Percentage:13.92
Left Sequence End645854
Right Sequence End646732
Gene Sequence:
>879 bp
ATGGCTGAAGCGCAAAATGATCCCCTGCTGCCGGGATACTCGTTTAACGCCCATCTGGTG
GCGGGTTTAACGCCGATTGAGGCCAACGGTTATCTCGATTTTTTTATCGACCGACCGCTG
GGAATGAAAGGTTATATTCTCAATCTCACCATTCGCGGTCAGGGGGTGGTGAAAAATCAG
GGACGAGAATTTGTCTGCCGACCGGGTGATATTTTGCTGTTCCCGCCAGGAGAGATTCAT
CACTACGGTCGTCATCCGGAGGCTCGCGAATGGTATCACCAGTGGGTTTACTTTCGTCCG
CGCGCCTACTGGCATGAATGGCTTAACTGGCCGTCAATATTTGCCAATACGGGTTTCTTT
CGCCCGGATGAAGCGCACCAGCCGCATTTCAGCGACCTGTTTGGGCAAATCATTAACGCC
GGGCAAGGGGAAGGGCGCTATTCGGAGCTGCTGGCGATAAATCTGCTTGAGCAATTGTTA
CTGCGGCGCATGGAAGCGATTAACGAGTCGCTCCATCCACCGATGGATAATCGGGTACGC
GAGGCTTGTCAGTACATCAGCGATCACCTGGCAGACAGCAATTTTGATATCGCCAGCGTC
GCACAGCATGTTTGCTTGTCGCCGTCGCGTCTGTCACATCTTTTCCGCCAGCAGTTAGGG
ATTAGCGTCTTAAGCTGGCGCGAGGACCAACGCATTAGTCAGGCGAAGCTGCTTTTGAGC
ACTACCCGGATGCCTATCGCCACCGTCGGTCGCAATGTTGGTTTTGACGATCAACTCTAT
TTCTCGCGAGTATTTAAAAAATGCACCGGGGCCAGCCCGAGCGAGTTTCGTGCCGGTTGT
GAAGAAAAAGTGAATGATGTAGCCGTCAAGTTGTCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:292
Protein Molecular Weight:31644
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase
MSMPATSTKTTKLATSLIDEYALLGWRAMLTEVNLSPKPGLVDRINCGAHKDMALEDFHR
SALAIQGWLPRFIEFGACSAEMAPEAVLHGLRPIGMACEGDMFRATAGVNTHKGSIFSLG
LLCAAIGRLLQLNQPVTPTTVCSTAASFCRGLTDRELRTNNSQLTAGQRLYQQLGLTGAR
GEAEAGYPLVINHALPHYLTLLDQGLDPELALLDTLLLLMAINGDTNVASRGGEGGLRWL
QREAQTLLQKGGIRTPADLDYLRQFDRECIERNLSPGGSADLLILTWFLAQI
References
External Links:
ResourceLink
Uniprot ID:P77231
Uniprot Name:CITG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321946
Ecogene ID:EG13539
Ecocyc:EG13539
ColiBase:b0613
Kegg Gene:b0613
EchoBASE ID:EB3309
CCDB:CITG_ECOLI
BacMap:16128596
General Reference:
  • 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
  • Schneider, K., Dimroth, P., Bott, M. (2000). "Biosynthesis of the prosthetic group of citrate lyase." Biochemistry 39:9438-9450. Pubmed: 10924139
  • Schneider, K., Dimroth, P., Bott, M. (2000). "Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group." FEBS Lett 483:165-168. Pubmed: 11042274