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 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE ACONITATE HYDRATASE PRECURSOR (EC 4.2.1.3) (CITRATE HYDRO-LYASE) DE (ACONITASE). GN ACO1 OR GLU1 OR L8003.22. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DBY747; RX MEDLINE; 90287144. RA GANGLOFF S.P., MARGUET D., LAUQUIN G.J.-M.; 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 EMBL/GENBANK/DDBJ DATA BANKS. 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 -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBUNIT: MONOMER. CC -!- ACONITASE HAS AN ACTIVE (4FE-4S) AND AN INACTIVE (3FE-4S) FORMS. CC THE ACTIVE (4FE-4S) CLUSTER IS PART OF THE CATALYTIC SITE THAT CC INTERCONVERTS CITRATE, CIS-ACONITASE, AND ISOCITRATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL AND EXTRAMITOCHONDRIAL. CC -!- ENZYME REGULATION: SUBJECT TO CATABOLITE REGULATION. CC -!- SIMILARITY: TO OTHER ACONITASES, TO IPM ISOMERASE, AND TO IRE- CC BINDING PROTEIN. 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; M33131. DR EMBL; U17243; U17243. DR PIR; A35668; A35668. DR HSSP; P20004; 1ACO. DR LISTA; SC00014; ACO1. DR SGD; L0000022; ACO1. DR PROSITE; PS00450; ACONITASE. KW LYASE; TRICARBOXYLIC ACID CYCLE; IRON-SULFUR; MITOCHONDRION; KW TRANSIT PEPTIDE; 4FE-4S. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 778 ACONITASE. 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; 3007596 CN; 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 //