ID   CISY3_YEAST             Reviewed;         486 AA.
AC   P43635; D6W412;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Citrate synthase 3, mitochondrial {ECO:0000303|PubMed:9140965};
DE            EC=2.3.3.1 {ECO:0000269|PubMed:17570335};
DE   Flags: Precursor;
GN   Name=CIT3 {ECO:0000303|PubMed:9140965}; OrderedLocusNames=YPR001W;
GN   ORFNames=YP9723.01;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CW04;
RA   Jia Y.K., Becam A.-M., Slonimski P.P., Herbert C.J.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9140965; DOI=10.1046/j.1365-2958.1997.3011669.x;
RA   Jia Y.K., Becam A.M., Herbert C.J.;
RT   "The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial
RT   isoform of citrate synthase.";
RL   Mol. Microbiol. 24:53-59(1997).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17570335; DOI=10.1016/j.abb.2007.04.039;
RA   Graybill E.R., Rouhier M.F., Kirby C.E., Hawes J.W.;
RT   "Functional comparison of citrate synthase isoforms from S. cerevisiae.";
RL   Arch. Biochem. Biophys. 465:26-37(2007).
CC   -!- FUNCTION: Dual specificity mitochondrial citrate and methylcitrate
CC       synthase with similar catalytic efficiency with both acetyl-CoA and
CC       propionyl-CoA. {ECO:0000269|PubMed:17570335,
CC       ECO:0000269|PubMed:9140965}.
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=2.3.3.1;
CC         Evidence={ECO:0000269|PubMed:17570335};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1200 uM for acetyl-CoA {ECO:0000269|PubMed:17570335};
CC         KM=520 uM for propionyl-CoA {ECO:0000269|PubMed:17570335};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9140965}.
CC   -!- DISRUPTION PHENOTYPE: Leads to an accumulation of acetate and of
CC       isobutanol. {ECO:0000269|PubMed:17570335}.
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC       oxidative metabolism. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; X88846; CAA61299.1; -; Genomic_DNA.
DR   EMBL; Z48951; CAA88779.1; -; Genomic_DNA.
DR   EMBL; Z71255; CAA95041.1; -; Genomic_DNA.
DR   EMBL; U31900; AAA97580.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11428.1; -; Genomic_DNA.
DR   PIR; S52814; S52814.
DR   RefSeq; NP_015325.1; NM_001184098.1.
DR   AlphaFoldDB; P43635; -.
DR   SMR; P43635; -.
DR   BioGRID; 36177; 82.
DR   DIP; DIP-3915N; -.
DR   STRING; 4932.YPR001W; -.
DR   PaxDb; 4932-YPR001W; -.
DR   PeptideAtlas; P43635; -.
DR   EnsemblFungi; YPR001W_mRNA; YPR001W; YPR001W.
DR   GeneID; 856107; -.
DR   KEGG; sce:YPR001W; -.
DR   AGR; SGD:S000006205; -.
DR   SGD; S000006205; CIT3.
DR   VEuPathDB; FungiDB:YPR001W; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   GeneTree; ENSGT00390000006813; -.
DR   HOGENOM; CLU_022049_2_1_1; -.
DR   InParanoid; P43635; -.
DR   OMA; IDHGFNA; -.
DR   OrthoDB; 3513214at2759; -.
DR   BioCyc; MetaCyc:YPR001W-MONOMER; -.
DR   BioCyc; YEAST:YPR001W-MONOMER; -.
DR   SABIO-RK; P43635; -.
DR   UniPathway; UPA00223; UER00717.
DR   BioGRID-ORCS; 856107; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P43635; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P43635; Protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:SGD.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:SGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IGI:SGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IDA:SGD.
DR   CDD; cd06106; ScCit3_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:SF15; CITRATE SYNTHASE 3, 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   1: Evidence at protein level;
KW   Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..486
FT                   /note="Citrate synthase 3, mitochondrial"
FT                   /id="PRO_0000169985"
FT   MOTIF           484..486
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   486 AA;  53811 MW;  F299CA258B772125 CRC64;
     MVQRLLPGAH ICRRSFNSSA IIKSSALTLK EALENVIPKK RDAVKKLKAC YGSTFVGPIT
     ISSVLGGMRG NQSMFWQGTS LDPEHGIKFQ GLTIEECQNR LPNTGIDGDN FLPESMLWLL
     MTGGVPTFQQ AASFRKELAI RGRKLPHYTE KVLSSLPKDM HPMTQLAIGL ASMNKGSLFA
     TNYQKGLIGK MEFWKDTLED SLNLIASLPL LTGRIYSNIT NEGHPLGQYS EEVDWCTNIC
     SLLGMTNGTN SSNTCNLTSQ QSLDFINLMR LYTGIHVDHE GGNVSAHTTH LVGSALSDPY
     LSYSSGIMGL AGPLHGLAAQ EVVRFLIEMN SNISSIAREQ EIKDYLWKIL NSNRVIPGYG
     HAVLRKPDPR FTAMLEFAQK RPIEFENDKN VLLMQKLAEI APKVLLEHGK SKNPFPNVDS
     ASGILFYHYG IRELLFFTVI FGCSRAMGPL TQLVWDRILG LPIERPKSLN LEGLEALTKA
     SNVNKL
//