CISY3_YEAST
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 03-AUG-2022, entry version 175.
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; 79.
DR DIP; DIP-3915N; -.
DR STRING; 4932.YPR001W; -.
DR PaxDb; P43635; -.
DR PRIDE; P43635; -.
DR EnsemblFungi; YPR001W_mRNA; YPR001W; YPR001W.
DR GeneID; 856107; -.
DR KEGG; sce:YPR001W; -.
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; AEYWEPT; -.
DR BioCyc; MetaCyc:YPR001W-MON; -.
DR BioCyc; YEAST:YPR001W-MON; -.
DR SABIO-RK; P43635; -.
DR UniPathway; UPA00223; UER00717.
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 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 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
