ID   CISY_LEIMA              Reviewed;         470 AA.
AC   Q4QDX3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable citrate synthase, mitochondrial;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
GN   ORFNames=LmjF18.0680, LmjF_18_0680;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B.G., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
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; FR796414; CAJ03695.1; -; Genomic_DNA.
DR   RefSeq; XP_001682475.1; XM_001682423.1.
DR   AlphaFoldDB; Q4QDX3; -.
DR   SMR; Q4QDX3; -.
DR   STRING; 5664.LmjF.18.0680; -.
DR   EnsemblProtists; CAJ03695; CAJ03695; LMJF_18_0680.
DR   GeneID; 5650994; -.
DR   KEGG; lma:LMJF_18_0680; -.
DR   VEuPathDB; TriTrypDB:LmjF.18.0680; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_180012400; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_180012300; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   InParanoid; Q4QDX3; -.
DR   OMA; TVGWCAQ; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000000542; Chromosome 18.
DR   GO; GO:0020023; C:kinetoplast; ISO:GeneDB.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:GeneDB.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; IPR010109; Citrate_synthase_euk.
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   TIGRFAMs; TIGR01793; cit_synth_euk; 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_0000291606"
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;  52329 MW;  5257C02EC31A2E0A CRC64;
     MRAVRCSLIR GVAGLRMASS ALDEMKEQML RRWKEDQKKI DDLRKKHGHE KLCDATIDAV
     YGGMRGITGL VYEPSLLDPA EGIRFRGLTI LECQEMLPKA PGGKEPLPEA MFWLLMTGEV
     PTEEQVRGLN AELHRRADPE AIAAAQKAIA ALPRNAHPMT AFSVGVLALQ SYSKFAAAYA
     AGKSNKKTYW EYALEDSLDM LARTPTVAAM IYNRETKGQV ELAAPSNSDL DWAANFAKMM
     GYQDEEFWEC MRLYLSVHAD HEGGNVSAHT TTLVASALSD PYLAFSAGLN GLAGPLHGLA
     NQEVLNYLLS MQERVKADGV NMHDEAALEK ALSNYTWELL NSGQVVPGYG HAVLRKVDPR
     YTCQRNFCLR HKFDDDLFKL VNTIYSIMPG ILKEHGKTKN PYPNVDAHSG VLLQHYGLTE
     QNYYTVLFGL SRQMGVLAGV VWDRLQGRPL ERPKSITTEM LAKKYLCNSL