ID CISZ_YEAST STANDARD; PRT; 460 AA. AC P08679; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Citrate synthase, peroxisomal (EC 2.3.3.1). GN CIT2 OR YCR005C OR YCR5C OR YCR043. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92254505; PubMed=1580102; RA Biteau N., Fremaux C., Hebrard S., Menara A., Aigle M., Crouzet M.; RT "The complete sequence of a 10.8kb fragment to the right of the RT chromosome III centromere of Saccharomyces cerevisiae."; RL Yeast 8:61-70(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87089811; PubMed=3540614; RA Rosenkrantz M., Alam T., Kim K.-S., Clark B.J., Srere P.A., RA Guarente L.P.; RT "Mitochondrial and nonmitochondrial citrate synthases in RT Saccharomyces cerevisiae are encoded by distinct homologous genes."; RL Mol. Cell. Biol. 6:4509-4515(1986). RN [3] RP SEQUENCE OF 1-24 FROM N.A. RX MEDLINE=91094853; PubMed=1986232; RA Liao X., Small W.C., Srere P.A., Butow R.A.; RT "Intramitochondrial functions regulate nonmitochondrial citrate RT synthase (CIT2) expression in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 11:38-46(1991). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate + CC CoA. CC -!- PATHWAY: Tricarboxylic acid cycle. CC -!- SUBCELLULAR LOCATION: Peroxisomal. CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells CC capable of oxidative metabolism. CC -!- SIMILARITY: Belongs to the citrate synthase family. 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; Z11113; CAA77442.1; -. DR EMBL; M14686; AAA34497.1; -. DR EMBL; M54982; AAA34498.1; -. DR EMBL; X59720; CAA42342.1; -. DR PIR; A25393; YKBYC. DR HSSP; P23007; 2CSC. DR GermOnline; 138910; -. DR SGD; S0000598; CIT2. DR GO; GO:0005777; C:peroxisome; IDA. DR InterPro; IPR002020; Citrate_synth. DR Pfam; PF00285; Citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR TIGRFAMs; TIGR01793; cit_synth_euk; 1. DR TIGRFAMs; TIGR01798; cit_synth_I; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. KW Transferase; Tricarboxylic acid cycle; Peroxisome; Multigene family. FT ACT_SITE 293 293 By similarity. FT ACT_SITE 339 339 By similarity. FT ACT_SITE 394 394 By similarity. FT SITE 458 460 Microbody targeting signal (Potential). SQ SEQUENCE 460 AA; 51413 MW; AB2F66AD9A9399EF CRC64; MTVPYLNSNR NVASYLQSNS SQEKTLKERF SEIYPIHAQD VRQFVKEHGK TKISDVLLEQ VYGGMRGIPG SVWEGSVLDP EDGIRFRGRT IADIQKDLPK AKGSSQPLPE ALFWLLLTGE VPTQAQVENL SADLMSRSEL PSHVVQLLDN LPKDLHPMAQ FSIAVTALES ESKFAKAYAQ GISKQDYWSY TFEDSLDLLG KLPVIAAKIY RNVFKDGKMG EVDPNADYAK NLVNLIGSKD EDFVDLMRLY LTIHSDHEGG NVSAHTSHLV GSALSSPYLS LASGLNGLAG PLHGRANQEV LEWLFALKEE VNDDYSKDTI EKYLWDTLNS GRVIPGYGHA VLRKTDPRYM AQRKFAMDHF PDYELFKLVS SIYEVAPGVL TEHGKTKNPW PNVDAHSGVL LQYYGLKESS FYTVLFGVSR AFGILAQLIT DRAIGASIER PKSYSTEKYK ELVKNIESKL //