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CISY_CANTR
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   03-AUG-2022, entry version 93.
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}.
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DR   EMBL; AB001565; BAA19410.1; -; Genomic_DNA.
DR   AlphaFoldDB; P79024; -.
DR   SMR; P79024; -.
DR   PRIDE; 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:InterPro.
DR   GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
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; 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; 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
 
 
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