Citrate synthase (P0ABH7)

Identification
Name:Citrate synthase
Synonyms:Not Available
Gene Name:gltA
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Specific Function:Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Water + 1.0Oxalacetic acid ↔ 1.0Citric acid + 1.0Coenzyme A + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Citric acid + 1.0Coenzyme A ↔ 1.0Acetyl-CoA + 1.0Water + 1.0Oxalacetic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Oxalacetic acid + 1.0Water + 1.0Acetyl-CoA → 1.0Citric acid + 1.0Coenzyme A + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Water + 1.0Oxalacetic acid ↔ 1.0Citric acid + 1.0Coenzyme A + 1.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB00094Citric acidMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00223Oxalacetic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
catalytic activity
citrate (Si)-synthase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
carbohydrate metabolic process
cellular carbohydrate metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
primary metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b0720
Gene OrientationCounterclockwise
Centisome Percentage:16.22
Left Sequence End752408
Right Sequence End753691
Gene Sequence:
>1284 bp
GTGTCGAATAACGCTTTACAAACAATTATTAACGCCCGGTTACCAGGCGAAGAGGGGCTG
TGGCAGATTCATCTGCAGGACGGAAAAATCAGCGCCATTGATGCGCAATCCGGCGTGATG
CCCATAACTGAAAACAGCCTGGATGCCGAACAAGGTTTAGTTATACCGCCGTTTGTGGAG
CCACATATTCACCTGGACACCACGCAAACCGCCGGACAACCGAACTGGAATCAGTCCGGC
ACGCTGTTTGAAGGCATTGAACGCTGGGCCGAGCGCAAAGCGTTATTAACCCATGACGAT
GTGAAACAACGCGCATGGCAAACGCTGAAATGGCAGATTGCCAACGGCATTCAGCATGTG
CGTACCCATGTCGATGTTTCGGATGCAACGCTAACTGCGCTGAAAGCAATGCTGGAAGTG
AAGCAGGAAGTCGCGCCGTGGATTGATCTGCAAATCGTCGCCTTCCCTCAGGAAGGGATT
TTGTCGTATCCCAACGGTGAAGCGTTGCTGGAAGAGGCGTTACGCTTAGGGGCAGATGTA
GTGGGGGCGATTCCGCATTTTGAATTTACCCGTGAATACGGCGTGGAGTCGCTGCATAAA
ACCTTCGCCCTGGCGCAAAAATACGACCGTCTCATCGACGTTCACTGTGATGAGATCGAT
GACGAGCAGTCGCGCTTTGTCGAAACCGTTGCTGCCCTGGCGCACCATGAAGGCATGGGC
GCGCGAGTCACCGCCAGCCACACCACGGCAATGCACTCCTATAACGGGGCGTATACCTCA
CGCCTGTTCCGCTTGCTGAAAATGTCCGGTATTAACTTTGTCGCCAACCCGCTGGTCAAT
ATTCATCTGCAAGGACGTTTCGATACGTATCCAAAACGTCGCGGCATCACGCGCGTTAAA
GAGATGCTGGAGTCCGGCATTAACGTCTGCTTTGGTCACGATGATGTCTTCGATCCGTGG
TATCCGCTGGGAACGGCGAATATGCTGCAAGTGCTGCATATGGGGCTGCATGTTTGCCAG
TTGATGGGCTACGGGCAGATTAACGATGGCCTGAATTTAATCACCCACCACAGCGCAAGG
ACGTTGAATTTGCAGGATTACGGCATTGCCGCCGGAAACAGCGCCAACCTGATTATCCTG
CCGGCTGAAAATGGGTTTGATGCGCTGCGCCGTCAGGTTCCGGTACGTTATTCGGTACGT
GGCGGCAAGGTGATTGCCAGCACACAACCGGCACAAACCACCGTATATCTGGAGCAGCCA
GAAGCCATCGATTACAAACGTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:427
Protein Molecular Weight:48015
Protein Theoretical pI:7
PDB File:1K3P
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Citrate synthase
MADTKAKLTLNGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTASCESKITFI
DGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITR
LFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYS
IGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVR
TAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSFR
LMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDPYFIEKKLYP
NVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLYTGYEKRD
FKSDIKR
References
External Links:
ResourceLink
Uniprot ID:P0ABH7
Uniprot Name:CISY_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674479
PDB ID:1K3P
Ecogene ID:EG10402
Ecocyc:EG10402
ColiBase:b0720
Kegg Gene:b0720
EchoBASE ID:EB0397
CCDB:CISY_ECOLI
BacMap:16128695
General Reference:
  • Bhayana, V., Duckworth, H. W. (1984). "Amino acid sequence of Escherichia coli citrate synthase." Biochemistry 23:2900-2905. Pubmed: 6380576
  • 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
  • Donald, L. J., Crane, B. R., Anderson, D. H., Duckworth, H. W. (1991). "The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR." J Biol Chem 266:20709-20713. Pubmed: 1939121
  • 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
  • Helling, R. B. (1995). "icdB mutants of Escherichia coli." J Bacteriol 177:2592-2593. Pubmed: 7730298
  • Hull, E. P., Spencer, M. E., Wood, D., Guest, J. R. (1983). "Nucleotide sequence of the promoter region of the citrate synthase gene (gltA) of Escherichia coli." FEBS Lett 156:366-370. Pubmed: 6343122
  • Ner, S. S., Bloxham, D. P., Handford, P. A., Akhtar, M. (1986). "The synthesis and use of oligodeoxynucleotides in plasmid DNA sequencing." Int J Biochem 18:257-262. Pubmed: 3514304
  • 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
  • Wilde, R. J., Guest, J. R. (1986). "Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12." J Gen Microbiol 132:3239-3251. Pubmed: 3309132
  • Wood, D., Darlison, M. G., Wilde, R. J., Guest, J. R. (1984). "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli." Biochem J 222:519-534. Pubmed: 6383359
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842