CISY_THUOB
ID CISY_THUOB Reviewed; 469 AA.
AC Q6S9V8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
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 Thunnus obesus (Bigeye tuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX NCBI_TaxID=8241;
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; AY461849; AAR98859.1; -; mRNA.
DR AlphaFoldDB; Q6S9V8; -.
DR SMR; Q6S9V8; -.
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_0000253907"
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; 52191 MW; BC5E52A73D3CA1A2 CRC64;
MSFLSVSRLA PKLLNSKNAT YFLVAARNAS ASTTNLKDVL ADLIPKEQSR IKNFKQQYGK
TNIGQITVDM VYGGMRGMKG LVYETSVLDP EEGIRFRGYS IPECQKLLPK APGGEEPLPE
GLFWLLVTGQ VPTEEQVNWV SKEWAKRAAL PSHVVTMLDN FPTNLHPMSQ FSAAITALNS
ESSFARAYSE GVHKTKYWEF VYEDSMDLIA KLPCIAAKIY RNLYREGSSI GAIDSNLDWS
HNFTNMLGYS EAQFTELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL SFSAAMNGLA
GPLHGLANQE VLVWLTALQK EMGGEVSDER MRDYIWNTLK SGRVVPGYGH AVLRKTDPRY
TCQREFALKH LPNDPMFKLV AQLYKIVPNV LLEQGKAKNP WPNVDAHSGV LLQYYGMTEM
NYYTVLFGVS RALGVLAQLV WSRALGFPLE RPKSMSTEGL MTLVGAKSG