CISY_IGUIG
ID CISY_IGUIG Reviewed; 469 AA.
AC Q0GNE0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 52.
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 Iguana iguana (Common iguana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Iguanidae; Iguaninae; Iguana.
OX NCBI_TaxID=8517;
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}.
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DR EMBL; DQ829808; ABI21882.1; -; mRNA.
DR AlphaFoldDB; Q0GNE0; -.
DR SMR; Q0GNE0; -.
DR BRENDA; 2.3.3.16; 9922.
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_0000253901"
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; 51957 MW; 40C89727DCADD889 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 DPQFIELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL AFAAAMNGLA
GPLHGLANQE VLVWLTNLQK ELGEDVSDQK LRDFIWNTLN SGRVVPGYGH AVLRKTDPRY
TCQREFALKH LPKDPLFKLV AQLYKIVPNV LLEQGKAKNP WPNVDAHSGV LLQYYGMKEM
NYYTVLFGVS RALGVLSQLI WSRALGFPLE RPKSMSTDGL MVLVGAKSG
