ID   CISY_DAUCA              Reviewed;         472 AA.
AC   O80433;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
GN   Name=CS;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. MS Yonsun;
RA   Takita E., Koyama H., Shirano Y., Shibata D., Hara T.;
RT   "cDNA encoding carrot mitochondrial citrate synthase.";
RL   Submitted (AUG-1998) 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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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}.
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DR   EMBL; AB017159; BAA32557.1; -; mRNA.
DR   AlphaFoldDB; O80433; -.
DR   SMR; O80433; -.
DR   PRIDE; O80433; -.
DR   BioCyc; MetaCyc:MON-15824; -.
DR   BRENDA; 2.3.3.16; 1841.
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   2: Evidence at transcript level;
KW   Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..472
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000005487"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   472 AA;  52657 MW;  A6C8CFCA17142120 CRC64;
     MVFFRSVSLL NKLRSRAVQQ SNLSNTVRWF QVQTSASDLD LRSQLKELIP EQQERIKKLK
     AEHGKVQLGN ITVDMVLGGM RGMTGLLWET SLLDPEEGIR FRGLSIPECQ KLLPGAKPGG
     EPLPEGLLWL LLTGKVPTKE QVDALSAELR SRAAVPEHVY KTIDALPVTA HPMTQFATGV
     MALQVQSEFQ KAYEKGIHKT KYWEPTYEDS ITLIAQLPVV AAYIYRRMYK NGQSISTDDS
     LDYGANFAHM LGYDSPSMQE LMRLYVTIHT DHEGGNVSAH TGHLVASALS DPYLSFAAAL
     NGLAGPLHGL ANQEVLLWIK SVVSECGENV TKEQLKDYIW KTLNSGKVVP GYGHGVLRNT
     DPRYICQREF ALKHLPDDPL FQLVSNLFEV VPPILTELGK VKNPWPNVDA HSGVLLNHYG
     LTEARYYTVL FGVSRAIGIC SQLVWDRALG LPLERPKSVT MEWLENHCKK SS