ID   CISY_TETNG              Reviewed;         469 AA.
AC   Q4S5X1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.1;
DE   AltName: Full=Citrate (Si)-synthase;
DE   Flags: Precursor;
GN   Name=cs; ORFNames=GSTENG00023547001;
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
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=2.3.3.1; 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 {ECO:0000250}.
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; CAAE01014729; CAG03961.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4S5X1; -.
DR   SMR; Q4S5X1; -.
DR   STRING; 99883.ENSTNIP00000015491; -.
DR   Ensembl; ENSTNIT00000015697.1; ENSTNIP00000015491.1; ENSTNIG00000012522.1.
DR   KEGG; tng:GSTEN00023547G001; -.
DR   GeneTree; ENSGT00390000006813; -.
DR   HOGENOM; CLU_022049_2_1_1; -.
DR   InParanoid; Q4S5X1; -.
DR   OMA; VLEWLFK; -.
DR   TreeFam; TF300398; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd06105; ScCit1-2_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; IPR010109; Citrate_synthase_euk.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   NCBIfam; TIGR01793; cit_synth_euk; 1.
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   3: Inferred from homology;
KW   Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..469
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000253905"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   469 AA;  52012 MW;  980C3309C330B9FE CRC64;
     MSFLTVNRLA SKLLNSKNAT YFLVAARNAS ASTTNLKDVL ADLIPKEQNR IKNFKQQYGK
     TNIGQITVDM VYGGMRGMKG LVYETSVLDP DEGIRFRGYS IPECQKLLPK AAGGQEPLPE
     GLFWLLVTGQ VPTEEQVNWV SKEWAKRAAL PSHVVTMLDN FPTNLHPMSQ FSAAVTALNS
     ESSFARAYSE GVHKSKYWEF AYEDSMDLIA KLPCIAAKIY RNLYREGSSI GAIDSGLDWS
     HNFTNMLGYS DAQFTELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL AFSAAMNGLA
     GPLHGLANQE VLVWLTALQK ELGGEVSDEK MRDYIWNTLK SGRVVPGYGH AVLRKTDPRY
     SCQREFAMKH LPNDPMFKLV AQLYKIVPDV LLEQGKAKNP WPNVDAHSGV LLQYYGMTEM
     NYYTVLFGVS RALGVLSQLV WSRALGFPLE RPKSMSTDGL MSLVGAKSG
//