ID   CISY_SOLTU              Reviewed;         471 AA.
AC   Q43175;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree;
RX   PubMed=7580855; DOI=10.1007/bf01106771;
RA   Landschuetze V., Willmitzer L., Mueller-Roeber B.;
RT   "Mitochondrial citrate synthase from potato: predominant expression in
RT   mature leaves and young flower buds.";
RL   Planta 196:756-764(1995).
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   -!- TISSUE SPECIFICITY: Ubiquitous.
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; X75082; CAA52976.1; -; mRNA.
DR   PIR; S44316; S44316.
DR   RefSeq; NP_001305561.1; NM_001318632.1.
DR   AlphaFoldDB; Q43175; -.
DR   SMR; Q43175; -.
DR   STRING; 4113.PGSC0003DMT400074559; -.
DR   PRIDE; Q43175; -.
DR   GeneID; 102595372; -.
DR   KEGG; sot:102595372; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43175; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; Reference proteome; Transferase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..471
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000005489"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   471 AA;  52612 MW;  BC6B5673792564C6 CRC64;
     MVFYRSVSLL SKLRSRAVQQ SNVSNSVRWL QVQTSSGLDL RSELVQELIP EQQDRLKKIK
     SDMKGSIGNI TVDMVLGGMR GMTGLLWKPH YLDPDEGIRF RGLSIPECQK VLPAAKPGGE
     PLPEGLLWLL LTGKVPSKEQ VNSIVSGIAE SGIISLIIMY TTIDALPVTA HPMTQFATGV
     MALQVQSEFQ KAYEKGIHKS KYWEPTYEDS MNLIAQVPLV AAYVYRRMYK NGDTIPKDES
     LDYGANFAHM LGFSSSEMHE LLMRLYVTIH SDHEGGNVSA HTGHLVASAL SDPYLSFAAA
     LNGLAGPLHG LANQEVLLWI KSVVEECGEN ISKEQLKDYV WKTLNSGKVV PGFGHGVLRK
     TVPRYTCQRE FAMKHLPEDP LFQLVSKLYE VFLLFLQNLA KLKPWPNVDA HSGVLLNYYG
     LTEARYYTVL FGVSRALGIC SQLIWDRALG LPLERPKSVT MEWLENQCKK A