ID   CISY_TETTH              Reviewed;         462 AA.
AC   P24118;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.16;
DE   AltName: Full=14 nm filament-forming protein;
DE   AltName: Full=49 kDa protein;
DE   Flags: Precursor;
OS   Tetrahymena thermophila.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-40, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   PubMed=1993043; DOI=10.1016/0006-291x(91)91522-e;
RA   Numata O., Takemasa T., Takagi I., Hirono M., Hirano H., Chiba J.,
RA   Watanabe Y.;
RT   "Tetrahymena 14-nm filament-forming protein has citrate synthase
RT   activity.";
RL   Biochem. Biophys. Res. Commun. 174:1028-1034(1991).
CC   -!- FUNCTION: Structural protein involved in oral morphogenesis and in
CC       pronuclear behavior during conjugation. Respiratory enzyme.
CC       {ECO:0000269|PubMed:1993043}.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:1993043}. Cytoplasm {ECO:0000269|PubMed:1993043}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:1993043}.
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; D90117; BAA14145.1; -; mRNA.
DR   PIR; JC5625; JC5625.
DR   AlphaFoldDB; P24118; -.
DR   SMR; P24118; -.
DR   UniPathway; UPA00223; UER00717.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
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; 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   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Mitochondrion;
KW   Transferase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1993043"
FT   CHAIN           22..462
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000005474"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        346
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   462 AA;  52575 MW;  F4F4EFDAE62243A6 CRC64;
     MRSINQLLKQ ASLSQKSQYN FSQTNLKKVI AEIIPQKQAE LKEVKEKYGD KVVGQYTVKQ
     VIGGMRGMKG LMSDLSRCDP YQGIIFRGYT IPQLKEFLPK ADPKAADQAN QEPLPEGIFW
     LLMTGQLPTH AQVDALKHEW QNRGTVNQDC VNFILNLPKD LHSMTMLSMA LLYLQKDSKF
     AKLYDEGKIS KKDYWEPFYE DSMDLIAKIP RVAAIIYRHK YRDSKLIDSD SKLDWAGNYA
     HMMGFEQHVV KECIRGYLSI HCDHEGGNVS AHTTHLVGSA LSDPYLSYSA GVNGLAGPLH
     GLANQEVLKW LLQFIEEKGT KVSDKDIEDY VDHVISSGRV VPGYGHAVLR DTDPRFHHQV
     DFSKFHLKDD QMIKLLHQCA DVIPKKLLTY KKIANPYPNV DCHSGVLLYS LGLTEYQYYT
     VVFAVSRALG CMANLIWSRA FGLPIERPGS ADLKWFHDKY RE