ID   CISY_AMBCR              Reviewed;         469 AA.
AC   Q0GNE1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
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   Amblyrhynchus cristatus (Galapagos marine iguana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Iguanidae; Iguaninae; Amblyrhynchus.
OX   NCBI_TaxID=51208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fields P.A., Strothers C.M.;
RT   "Temperature adaptation in muscle-type lactate dehydrogenase and citrate
RT   synthase of Amblyrhynchus cristatus, the Galapagos marine iguana.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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; DQ829807; ABI21881.1; -; mRNA.
DR   AlphaFoldDB; Q0GNE1; -.
DR   SMR; Q0GNE1; -.
DR   BRENDA; 2.3.3.16; 9921.
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..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..469
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000253900"
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;  52003 MW;  8216158BB22D9A27 CRC64;
     MTLLTASSRA AARLLGAKNS SCIIFAARHA STSTNLKDVL ANMIPKEQAR IKSFRQQYGS
     TVIGQITVDM LYGGMRGMKG LIYETSVLDP DEGIRFRGYS IPECQKLLPK APGGAEPLPE
     GLFWLLVTGE IPSQEQVNWV SREWAKRAAL PSHVVTMLDN FPTNLHPMSQ LSAAVTALNS
     ESTFARAYSE GISRTKYWEF IYEDSMDLIA KLPCIAAKIY RNLYREGSSI GAIDPALDWS
     HNFTNMLGYT DTQFIELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL AFAAAMNGLA
     GPLHGLANQE VLVWLTNLQK ELGEDVSDQK LRDFIWNTLN SGRVVPGYGH AVLRKTDPRY
     TCQREFALKH LPKDPLFKLV AQLYKIVPNV LLEQGKAKNP WPNVDAHSGV LLQYYGMKEM
     NYYTVLFGVS RALGVLSQLI WSRALGFPLE RPKSMSTDGL MVLVGAKSV