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InterPro: IPR006472 Citrate lyase, alpha subunit

Protein matchesHelp
UniProtKB
Matches:
352 proteins
AccessionHelp IPR006472 Citrate_lyase_asu
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Process GO:0006084 acetyl-CoA metabolic process
Function GO:0008814 citrate CoA-transferase activity
Component GO:0005737 cytoplasm
GO:0009346 citrate lyase complex
InterPro annotation
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AbstractHelp

These sequences, from both Gram-positive and Gram-negative bacteria, represent the alpha subunit of the holoenzyme citrate lyase composed of alpha (EC:2.8.3.10), beta, and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The alpha subunit catalyzes the reaction Acetyl-CoA + citrate = acetate + (3S)-citryl-CoA. The protein from Lactococcus lactis subsp. lactis (Streptococcus lactis) has been experimentally characterised [1].

Structural linksHelp
SCOP: c.124.1.2
Database linksHelp
PANDIT: PF04223
Blocks: IPB006472

Taxonomic coverageHelp

Example proteinsHelp
O53079 Citrate lyase alpha chain

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR006472 Citrate lyase, alpha subunit
SWISS-MODEL
ModBase

PublicationsHelp
1. Kummel A, Behrens G, Gottschalk G.
Citrate lyase from Streptococcus diacetilactis. Association with its acetylating enzyme.
Arch. Microbiol. 102 111-6 1975 [PubMed: 1115558]
http://dx.doi.org/10.1007/BF00428354

Additional ReadingHelp
Bott M, Dimroth P.
Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression.
Mol. Microbiol. 14 1994 347-56 [PubMed: 7830578]
http://dx.doi.org/10.1111/j.1365-2958.1994.tb01295.x
Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Divies C, Prevost H.
Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster.
J. Bacteriol. 180 1998 647-54 [PubMed: 9457870]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9457870&action=stream&blobtype=pdf
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InterPro 23.1