Summary: Citrate lyase, alpha subunit (CitF)
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Citrate lyase, alpha subunit (CitF) Provide feedback
In citrate-utilising prokaryotes, citrate lyase EC:22.214.171.124 cleaves intracellular citrate into acetate and oxaloacetate, and is organised as a functional complex consisting of alpha, beta, and gamma subunits. The gamma subunit serves as an acyl carrier protein (ACP), and has a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group. The citrate lyase is active only if this prosthetic group is acetylated; this acetylation is catalysed by an acetate:SH-citrate lyase ligase. The alpha subunit substitutes citryl for the acetyl group to form citryl-S-ACP. The beta subunit completes the reaction by cleaving the citryl to yield oxaloacetate and (regenerated) acetyl-S-ACP. This family represents the alpha subunit EC:126.96.36.199.
Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Divies C, Prevost H; , J Bacteriol 1998;180:647-654.: Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster. PUBMED:9457870 EPMC:9457870
Internal database links
|Similarity to PfamA using HHSearch:||AcetylCoA_hyd_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR006472
These sequences, from both Gram-positive and Gram-negative bacteria, represent the alpha subunit of the holoenzyme citrate lyase composed of alpha (EC), 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 proteins from Lactococcus lactis subsp. lactis (Streptococcus lactis) [PUBMED:1115558] and Klebsiella pneumoniae has been experimentally characterised [PUBMED:7830578].
|Cellular component||citrate lyase complex (GO:0009346)|
|Molecular function||citrate CoA-transferase activity (GO:0008814)|
|Biological process||acetyl-CoA metabolic process (GO:0006084)|
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This superfamily contains a variety of enzymes and non-enzymatic ligand binding domains.
The clan contains the following 12 members:5-FTHF_cyc-lig AcetylCoA_hyd_C AcetylCoA_hydro CitF CoA_trans DeoRC DUF162 Glucosamine_iso IF-2B Mal_decarbox_Al Rib_5-P_isom_A Sugar-bind
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Curation and family details
|Number in seed:||5|
|Number in full:||5419|
|Average length of the domain:||455.10 aa|
|Average identity of full alignment:||71 %|
|Average coverage of the sequence by the domain:||91.56 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CitF domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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