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