ID ACON_YEAST STANDARD; PRT; 778 AA. AC P19414; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE ACONITATE HYDRATASE, MITOCHONDRIAL PRECURSOR (EC 4.2.1.3) (CITRATE DE HYDRO-LYASE) (ACONITASE). GN ACO1 OR GLU1 OR YLR304C OR L8003.22. 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. RC STRAIN=DBY747; RX MEDLINE=90287144; PubMed=1972545; RA Gangloff S.P., Marguet D., Lauquin G.J.-M.; RT "Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) RT and evidence of a synergistic regulation of expression by glucose RT plus glutamate."; RL Mol. Cell. Biol. 10:3551-3561(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., RA Favello A., Fulton L., Gattung S., Greco T., Kirsten J., RA Kucaba T., Hallsworth K., Hawkins J., Hillier L., Jier M., RA Johnson D., Johnston L., Langston Y., Latreille P., Le T., RA Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., RA Rifken L., Riles L., Taich A., Trevaskis E., Vignati D., RA Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR GROWTH ON NONFERMENTABLE CARBON SOURCES AND CC FOR BIOSYNTHESIS OF GLUTAMATE. CC -!- CATALYTIC ACTIVITY: CITRATE = CIS-ACONITATE + H(2)O. CC -!- COFACTOR: ACONITASE HAS AN ACTIVE (4FE-4S) AND AN INACTIVE (3FE- CC 4S) FORMS. THE ACTIVE (4FE-4S) CLUSTER IS PART OF THE CATALYTIC CC SITE THAT INTERCONVERTS CITRATE, CIS-ACONITASE, AND ISOCITRATE (BY CC SIMILARITY). CC -!- ENZYME REGULATION: SUBJECT TO CATABOLITE REGULATION. CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL AND EXTRAMITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE ACONITASE/IPM ISOMERASE 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; M33131; AAA34389.1; -. DR EMBL; U17243; AAB67348.1; -. DR PIR; A35668; A35668. DR HSSP; P16276; 6ACN. DR SGD; S0004295; ACO1. DR InterPro; IPR001030; Aconitase. DR InterPro; IPR000573; Aconitase_C. DR Pfam; PF00330; aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR ProDom; PD000511; -; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. KW Lyase; Tricarboxylic acid cycle; Iron-sulfur; Mitochondrion; KW Transit peptide; 4Fe-4S. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 778 ACONITATE HYDRATASE. FT METAL 382 382 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 445 445 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 448 448 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT CONFLICT 527 549 DGLPQRGYDAGENTYQAPPADRS -> RWFASKEVMMLVRT FT LTKLHLQTVA (IN REF. 1). SQ SEQUENCE 778 AA; 85368 MW; AA9EB9A24388090E CRC64; MLSARSAIKR PIVRGLATVS NLTRDSKVNQ NLLEDHSFIN YKQNVETLDI VRKRLNRPFT YAEKILYGHL DDPHGQDIQR GVSYLKLRPD RVACQDATAQ MAILQFMSAG LPQVAKPVTV HCDHLIQAQV GGEKDLKRAI DLNKEVYDFL ASATAKYNMG FWKPGSGIIH QIVLENYAFP GALIIGTDSH TPNAGGLGQL AIGVGGADAV DVMAGRPWEL KAPKILGVKL TGKMNGWTSP KDIILKLAGI TTVKGGTGKI VEYFGDGVDT FSATGMGTIC NMGAEIGATT SVFPFNKSMI EYLEATGRGK IADFAKLYHK DLLSADKDAE YDEVVEIDLN TLEPYINGPF TPDLATPVSK MKEVAVANNW PLDVRVGLIG SCTNSSYEDM SRSASIVKDA AAHGLKSKTI FTVTPGSEQI RATIERDGQL ETFKEFGGIV LANACGPCIG QWDRRDIKKG DKNTIVSSYN RNFTSRNDGN PQTHAFVASP ELVTAFAIAG DLRFNPLTDK LKDKDGNEFM LKPPHGDGLP QRGYDAGENT YQAPPADRST VEVKVSPTSD RLQLLKPFKP WDGKDAKDMP ILIKAVGKTT TDHISMAGPW LKYRGHLENI SNNYMIGAIN AENKKANCVK NVYTGEYKGV PDTARDYRDQ GIKWVVIGDE NFGEGSSREH AALEPRFLGG FAIITKSFAR IHETNLKKQG LLPLNFKNPA DYDKINPDDR IDILGLAELA PGKPVTMRVH PKNGKPWDAV LTHTFNDEQI EWFKYGSALN KIKADEKK //