ID CISY_CITMA Reviewed; 471 AA. AC P49298; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-SEP-2023, entry version 95. DE RecName: Full=Citrate synthase, mitochondrial; DE EC=2.3.3.16; DE Flags: Precursor; GN Name=CIT; OS Citrus maxima (Pomelo) (Citrus grandis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus. OX NCBI_TaxID=37334; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Siamese Sweet 2240; RA Canel C.; RL Thesis (1994), University of California Riverside, United States. 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=2.3.3.16; 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. 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; U19481; AAA82743.1; -; mRNA. DR AlphaFoldDB; P49298; -. DR SMR; P49298; -. DR UniPathway; UPA00223; UER00717. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro. DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.580.10; 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; Transferase; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1..18 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 19..471 FT /note="Citrate synthase, mitochondrial" FT /id="PRO_0000005486" FT ACT_SITE 307 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 353 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 408 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" SQ SEQUENCE 471 AA; 52183 MW; 8EE1E23F7E154806 CRC64; MASLRSATAL SRLRSRAGQQ SNLSNSVRWL QMQSSADLDL HSQLKEMIPE QQERLKKVKS DLGKAQLGNI TIDVVIGGMR GMTGLLWETS LLDPDEGIRF RGLSIPECQK LLPAAKPDGE PLPEGLLWLL LTGKVPSKEQ VDGLSKELRD RATVPDYVYK AIDALPVSAH PMTQFASGVM ALQVQSEFQE AYEKGIHKSK SWEPTSEDSL NLIARVPVVA AYVYQRIYKD GKIIPKDDSL DYGGNFSHML GFDDPKMLEL MRLYVTIHSD HEGGNVSAHT GHLVASALSD PYLSFLAALN GLAGPLHGLA NQEVLLWIKS VVDECGENVT TEQLKDYVWK TLNSGKVVPG FGHGVLRKTD PRYTCQREFA LKHLPDDPLF QLVSKLYEVV PPILTKLGKV KNPWPNVDAH SGVLLNHFGL AEARYYTVLF GVSRSLGICS QLIWDRALGL PLERPKSVTL DWIEKNCKKA A //