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 22-FEB-2023, entry version 113. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd06103; ScCS-like; 1. DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1. DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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; CITRATE SYNTHASE; 1. DR PANTHER; PTHR11739:SF8; CITRATE SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; Citrate synthase; 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 //