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 13-SEP-2023, entry version 55. 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}. 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; 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 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:SF29; CITRATE SYNTHASE; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; Citrate synthase; 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 //