ID   CILA_KLEPN              Reviewed;         508 AA.
AC   P45413;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Citrate lyase alpha chain;
DE            Short=Citrase alpha chain;
DE            EC=4.1.3.6;
DE   AltName: Full=Citrate (pro-3S)-lyase alpha chain;
DE   AltName: Full=Citrate CoA-transferase subunit;
DE            EC=2.8.3.10;
GN   Name=citF;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=7830578; DOI=10.1111/j.1365-2958.1994.tb01295.x;
RA   Bott M., Dimroth P.;
RT   "Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase:
RT   localization, sequencing, and expression.";
RL   Mol. Microbiol. 14:347-356(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10.
RX   PubMed=773936; DOI=10.1016/s0021-9258(17)33477-4;
RA   Singh M., Srere P.A., Klapper D.G., Capra J.D.;
RT   "Subunit and chemical composition of citrate lyase from Klebsiella
RT   pneumoniae.";
RL   J. Biol. Chem. 251:2911-2915(1976).
CC   -!- FUNCTION: Represents a citrate:acetyl-ACP transferase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + citrate = (3S)-citryl-CoA + acetate;
CC         Xref=Rhea:RHEA:19405, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57321; EC=2.8.3.10;
CC   -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR   EMBL; X79817; CAA56217.1; -; Genomic_DNA.
DR   PIR; S60776; S60776.
DR   RefSeq; WP_004222627.1; NZ_WXZN01000037.1.
DR   AlphaFoldDB; P45413; -.
DR   SMR; P45413; -.
DR   BioCyc; MetaCyc:MON-16998; -.
DR   GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:InterPro.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008814; F:citrate CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   InterPro; IPR006472; Citrate_lyase_asu.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR40596; PTHR40596; 1.
DR   Pfam; PF04223; CitF; 1.
DR   PIRSF; PIRSF009451; Citrt_lyas_alpha; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
DR   TIGRFAMs; TIGR01584; citF; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lyase; Transferase.
FT   CHAIN           1..508
FT                   /note="Citrate lyase alpha chain"
FT                   /id="PRO_0000089754"
SQ   SEQUENCE   508 AA;  54668 MW;  8E7442046F4A573A CRC64;
     MKETVAMLNQ QYVMPNGLTP YAGVTAKSPW LASESEKRQR KICDSLETAI RRSGLQNGMT
     ISFHHAFRGG DKVVNMVVAK LAEMGFRDLT LASSSLIDAH WPLIEHIKNG VIRQIYTSGL
     RGKLGEEISA GLMENPVQIH SHGGRVQLIQ SGELSIDVAF LGVPCCDEFG NANGFSGKSR
     CGSLGYARVD AEHAKCVVLL TEEWVDYPNY PASIAQDQVD LIVQVDEVGD PQKITAGAIR
     LTSNPRELLI ARQAAKVVEH SGYFKEGFSL QTGTGGASLA VTRFLEDKMR RNGITASFGL
     GGITGTMVDL HEKGLIKTLL DTQSFDGDAA RSLAQNPNHV EISTNQYASP GSKGASCERL
     NVVMLSALEI DIDFNVNVMT GSNGVLRGAS GGHSDTAAGA DLTIITAPLV RGRIPCVVEK
     VLTRVTPGAS VDVLVTDHGI AVNPARQDLI DNLRSAGIPL MTIEELQQRA ELLTGKPQPI
     EFTDRVVAVV RYRDGSVIDV IRQVKNSD