ID   CISY_LEIIN              Reviewed;         470 AA.
AC   A4HXU4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Probable citrate synthase, mitochondrial;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
GN   ORFNames=LinJ18.0690, LinJ_18_0690;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5;
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC         Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10117};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC       oxidative metabolism.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; FR796450; CAM67122.1; -; Genomic_DNA.
DR   RefSeq; XP_001464885.1; XM_001464848.1.
DR   AlphaFoldDB; A4HXU4; -.
DR   SMR; A4HXU4; -.
DR   STRING; 5671.A4HXU4; -.
DR   GeneID; 5068291; -.
DR   KEGG; lif:LINJ_18_0690; -.
DR   VEuPathDB; TriTrypDB:LINF_180012100; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   InParanoid; A4HXU4; -.
DR   OMA; VLEWLFK; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000008153; Chromosome 18.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd06103; ScCS-like; 1.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR11739:SF8; CITRATE SYNTHASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..470
FT                   /note="Probable citrate synthase, mitochondrial"
FT                   /id="PRO_0000291605"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   470 AA;  52192 MW;  D38F325BC1A97824 CRC64;
     MRALRCSIIR GVAGLRMASS VLDEMKEQML RRSKEDHKKI GDLRKKHGHE KLCDATIDAV
     YGGMRGITGL VYEPSLLDSA EGIRFRGLTI LECQEMLPKA PGGKEPLPEA MFWLLMTGEV
     PTEEQARGLN AELHRRVDPE AIAAAQKAIA ALPKNAHPMT AFSVGVLALQ TYSKFAAAYA
     AGKSNKKTYW EYALEDSLDM LARTPAVAAM IYNRETKGQV ELAAPSNSDL DWAANFAKML
     GFQDEEFREC MRLYLSVHAD HEGGNVSAHT TTLVASALSD PYLAFSAGLN GLAGPLHGLA
     NQEVLKYLFS MQERVKADGV NVHDEAALEK ALTKYTWELL NSGQVVPGYG HAVLRKVDPR
     YTCQRNFCLR HNFQDDLFKL VNTIYMIMPG ILKEHGKTKN PYPNVDAHSG VLLQHYGLTE
     QNYYTVLFGL SRQMGVLAGV VWDRLQGRPL ERPKSITTEM LAKKYLCNSL
//