CISY_LEIIN
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 03-AUG-2022, entry version 77.
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.XP_001464885.1; -.
DR GeneID; 5068291; -.
DR KEGG; lif:LINJ_18_0690; -.
DR VEuPathDB; TriTrypDB:LINF_180012100; -.
DR eggNOG; KOG2617; Eukaryota.
DR InParanoid; A4HXU4; -.
DR OMA; TVGWCAQ; -.
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 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_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