ID CISY_CANTR Reviewed; 467 AA. AC P79024; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 13-SEP-2023, entry version 96. DE RecName: Full=Citrate synthase, mitochondrial; DE EC=2.3.3.16; DE Flags: Precursor; GN Name=CIT; OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5482; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 20336 / pK233 / NCYC 997; RA Ueda M., Sanuki S., Kawachi H., Shimizu K., Atomi H., Tanaka A.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix. 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}. CC -!- CAUTION: The conserved active site Asp residue in position 402 is CC replaced by a Gly. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB001565; BAA19410.1; -; Genomic_DNA. DR AlphaFoldDB; P79024; -. DR SMR; P79024; -. DR VEuPathDB; FungiDB:CTMYA2_039600; -. DR VEuPathDB; FungiDB:CTRG_00747; -. DR UniPathway; UPA00223; UER00717. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:EnsemblFungi. DR GO; GO:0006101; P:citrate metabolic process; IEA:EnsemblFungi. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 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; IPR010109; Citrate_synthase_euk. DR InterPro; IPR036969; Citrate_synthase_sf. DR NCBIfam; TIGR01793; cit_synth_euk; 1. DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1. DR PANTHER; PTHR11739:SF8; CITRATE SYNTHASE, 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 3: Inferred from homology; KW Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..467 FT /note="Citrate synthase, mitochondrial" FT /id="PRO_0000005476" FT ACT_SITE 301 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 347 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" SQ SEQUENCE 467 AA; 52004 MW; 4B194132C4198CA2 CRC64; MSALRSFQRS SNVAKSTLKN SVRTYATAEP TLKQRLEEIL PAKAEEVKQL KKDYGKTVIG EVLLEQAYGG MRGIKGLVWE GSVLDPIEGI RFRGRTIPDI QKELPKAPGG EEPLPEALFW LLLTGEVPTE AQTRALSEEF AARSALPKHV EELIDRSPSH LHPMAQFSIA VTALESESQF AKAYAKGVHK SEYWKYTYED SIELLAKLPT IAAKIYRNVF HDGKLPAQID SKLDYGANLA SLLGFGENKE FLELMRLYLT IHSDHEGGNV SAHTTHLVGS ALSSPFLSLA AGLNGLAGPL HGRANQEVLE WLFKLREELN GDYSKEAIEK YLWDTLNAGR VGPGYGHAVL RKTDPRYTAQ REFALKHMPD YELFKLVSNI YEVAPGVFDQ HGMTKNPWPN VGSHSGVLLQ YYGLTEESFY TVLFGVSRAF GVLPQLILDR GLGMPIERPK SFSTEKYIEL VKSIGKN //