[Citrate [pro-3S]-lyase] ligase
Details
- Name
- [Citrate [pro-3S]-lyase] ligase
- Synonyms
- 6.2.1.22
- Acetate:SH-citrate lyase ligase
- Citrate lyase synthetase
- ybeO
- Gene Name
- citC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0001606|[Citrate [pro-3S]-lyase] ligase MFGNDIFTRVKRSENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIK CVAISESVRGEGLALTLATELINLAYERHSTHLFIYTKTEYEALFRQCGFSTLTSVPGVM VLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLV KEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEID LKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTISAPPIELVEIERLRYQ EMPISASRVRQLLAKNDLTAIAPLVPAVTLHYLQNLLEHSRQDAAARQKTPA
- Number of residues
- 352
- Molecular Weight
- 40076.805
- Theoretical pI
- 8.21
- GO Classification
- Functions[citrate (pro-3S)-lyase] ligase activity / ATP binding / N-acetyltransferase activityProcessesbiosynthetic process / cellular protein modification process
- General Function
- N-acetyltransferase activity
- Specific Function
- Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0010568|[Citrate [pro-3S]-lyase] ligase (citC) ATGTTCGGCAATGATATTTTCACCCGCGTAAAACGTTCAGAAAATAAAAAAATGGCGGAA ATCGCCCAATTCCTGCATGAAAATGATTTGAGCGTTGACACCACAGTCGAAGTATTTATT ACCGTAACCCGCGATGAAAAGCTTATCGCGTGCGGTGGAATTGCCGGAAATATTATTAAA TGCGTTGCTATCAGTGAATCCGTCCGCGGTGAAGGACTGGCGCTGACATTAGCCACTGAA TTGATAAACCTCGCCTATGAGCGGCACAGCACGCATCTGTTTATTTATACCAAAACCGAA TACGAGGCGCTGTTCCGCCAGTGCGGTTTTTCCACGCTGACCAGCGTACCCGGCGTGATG GTGCTGATGGAAAACAGCGCCACGCGACTGAAACGCTATGCCGAATCGCTGAAAAAATTT CGTCATCCAGGGAACAAGATTGGCTGCATTGTGATGAACGCCAATCCCTTTACGAATGGT CACCGTTATCTGATTCAACAGGCTGCGGCACAGTGCGACTGGTTGCATCTGTTTTTAGTC AAAGAAGATTCTTCACGCTTCCCCTATGAAGACCGGCTGGATTTGGTGTTAAAAGGCACC GCCGATATTCCACGCCTGACTGTGCATCGTGGCTCCGAATACATCATCTCCCGCGCTACG TTCCCTTGCTACTTCATTAAAGAACAGAGCGTCATTAACCATTGTTACACCGAAATTGAT CTGAAGATTTTCCGTCAGTACCTCGCTCCCGCGCTGGGTGTAACTCACCGCTTTGTCGGT ACTGAACCCTTTTGTCGCGTTACCGCCCAGTACAACCAGGATATGCGCTACTGGCTGGAA ACGCCGACTATCTCCGCACCGCCCATCGAACTGGTTGAAATTGAGCGGCTGCGTTACCAG GAGATGCCGATATCCGCTTCCCGGGTACGTCAACTGCTGGCGAAAAACGATCTCACGGCT ATCGCGCCGCTGGTCCCTGCAGTCACGCTGCATTATTTGCAGAACCTGCTTGAGCACTCC CGCCAGGACGCGGCAGCTCGTCAAAAGACCCCCGCATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P77390 UniProtKB Entry Name CITC_ECOLI GenBank Protein ID 1778535 GenBank Gene ID U82598 - General References
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Shimada T, Yamamoto K, Ishihama A: Involvement of the leucine response transcription factor LeuO in regulation of the genes for sulfa drug efflux. J Bacteriol. 2009 Jul;191(14):4562-71. doi: 10.1128/JB.00108-09. Epub 2009 May 8. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details