ID CISY_XENLA Reviewed; 468 AA. AC Q7ZWZ5; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 90. 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 Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (FEB-2003) 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; BC046571; AAH46571.1; -; mRNA. DR RefSeq; NP_001080194.1; NM_001086725.1. DR AlphaFoldDB; Q7ZWZ5; -. DR SMR; Q7ZWZ5; -. DR DNASU; 379886; -. DR GeneID; 379886; -. DR KEGG; xla:379886; -. DR AGR; Xenbase:XB-GENE-943167; -. DR CTD; 379886; -. DR Xenbase; XB-GENE-943167; cs.L. DR OrthoDB; 3513214at2759; -. DR UniPathway; UPA00223; UER00717. DR Proteomes; UP000186698; Chromosome 2L. DR Bgee; 379886; Expressed in muscle tissue and 19 other cell types or tissues. 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:SF8; CITRATE SYNTHASE, MITOCHONDRIAL; 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; Reference proteome; Transferase; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1..30 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 31..468 FT /note="Citrate synthase, mitochondrial" FT /id="PRO_0000253909" FT ACT_SITE 303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 349 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 404 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" SQ SEQUENCE 468 AA; 51747 MW; 233F8FAF3D4BE6DE CRC64; MSLISAGRVC ARILGAKNSP CALIAARQAS SSTNLKDVLS DLIPKEQTRI KNFKQQHGKT VIGQVTVDMV YGGMRGMKGL VYETSVLDPD EGIRFRGYSI PECQKLLPKA PGGEEPLPEG LFWLLVTGEV PNQDQVNWIS KEWAKRAALP SHVVTMLDNF PTNLHPMSQL SAAITALNSE SNFARAYAEG VNKAKYWELV YEDSMDLIAK LPCVAAKIYR NLYREGSSIG AIDSNLDWSD NFTNMLGYTD QQFTELMRLY LTIHSDHEGG NVSAHTSHLV GSALSDPYLS FSAAMNGLAG PLHGLANQEV LVWLTSLQKD LGGEVSDEKL RDYIWNTLNS GRVVPGYGHA VLRKTDPRYT CQREFALKHL PDDPMFKLVA QLYKIVPNIL LEQGKAKNPW PNVDAHSGVL LQYYGMTEMN YYTVLFGVSR ALGVLSQLIW SRALGFPLER PKSMSTDGLM QLVGSKSG //