ID   CISY_XIPGL              Reviewed;         469 AA.
AC   Q6S9V6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.1;
DE   AltName: Full=Citrate (Si)-synthase;
DE   Flags: Precursor;
GN   Name=cs;
OS   Xiphias gladius (Swordfish) (Tetrapterus imperator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Istiophoriformes; Xiphiidae; Xiphias.
OX   NCBI_TaxID=8245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Red muscle;
RX   PubMed=15374817; DOI=10.1152/ajpregu.00152.2004;
RA   Dalziel A.C., Moore S.E., Moyes C.D.;
RT   "Mitochondrial enzyme content in the muscles of high-performance fish:
RT   evolution and variation among fiber types.";
RL   Am. J. Physiol. 288:R163-R172(2005).
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; AY461851; AAR98861.1; -; mRNA.
DR   AlphaFoldDB; Q6S9V6; -.
DR   SMR; Q6S9V6; -.
DR   UniPathway; UPA00223; UER00717.
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   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..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..469
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000253908"
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;  52214 MW;  75483B471DAB74D4 CRC64;
     MSFLTVSRLA PKLLNSKNAT YFLVAARNAS ASSTNLKDVL ADLIPKEQTR IKNFKQQYGK
     TNIGQITVDM VYGGMRGMKG LVYETSVLDP EEGIRFRGYS IPECQELLPK APGGEEPLPE
     GLFWLLVTGQ VPTEEQVNWV SKEWAKRAAL PSHVVTMLDN FPTNLHPMSQ FSAAITALNS
     ESSFARAYSE GVHKTKYWEF IYEDSMDLIA KLPCIAAKIY RNLYREGSSI GAIDSNLDWS
     HNFTNMLGYS EPQFTELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL SFSAAMNGLA
     GPLHGLANQE VLVWLTALQK ELGGEVSDER MRDYIWNTLK SGRVVPGYGH AVLRKTDPRY
     TCQREFALKH LPNDPMFKLV AQLYKIVPNV LLEQGKAKNP WPNVDAHSGV LLQYYGMTEM
     NYYTVLFGVS RALGVLAQLV WSRALGFPLE RPKSMSTDGL MTLVGAKSG