ID   CISY_LEIBR              Reviewed;         470 AA.
AC   A4H9H8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Probable citrate synthase, mitochondrial;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
GN   ORFNames=LbrM18_V2.0760, LbrM_18_0760;
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904;
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; FR798992; CAM38050.1; -; Genomic_DNA.
DR   RefSeq; XP_001564000.1; XM_001563950.1.
DR   AlphaFoldDB; A4H9H8; -.
DR   SMR; A4H9H8; -.
DR   STRING; 5660.A4H9H8; -.
DR   GeneID; 5414535; -.
DR   KEGG; lbz:LBRM_18_0760; -.
DR   VEuPathDB; TriTrypDB:LbrM.18.0760; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_180012800; -.
DR   InParanoid; A4H9H8; -.
DR   OMA; TVGWCAQ; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000007258; 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   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 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; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 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_0000291604"
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;  51957 MW;  D1EFE121FC034466 CRC64;
     MRAARCSIIR GAAGLRMASS VMSEMKEQML KRSKVEKQTI SELRKKHGDV KLSDASIDAA
     YCGMRGITGL VYEPSLLDPV EGIRFRNRTI PECQEVLPKA PNGCETLPEA MFWLLMTGEV
     PTAEQARALN AELHRRADPV AIAAAQKAIA ALPASTHPMT AFSVGVLALQ TYSKFAAAYA
     TGKSNKTTYW EYALEDSLDM LARTPAVAAM IYNRVTKGRA EVAASSNSEL DWAANFSNML
     GFKDNEFWEC MRLYLSIHVD HEGGNVSAHT TTLVASALSD PYLAFSAGLN GLAGPLHGLA
     NQEVLKYLLS MQDRVKADGV NVCDEAALEV ALTKYTWELL NSGQVVPGYG HAVLRKVDPR
     YTCLRNFCLR HHFEDDLFKL INIIYKIMPG ILTEHGKTKN PYPNVDAHSG VLLQHYGLTE
     QDYYTVLFGL SRQMGVMAGV VWDRLQGRPL ERPKSITTEM LAKKYLCTPR