ID ACON_YEAST Reviewed; 778 AA. AC P19414; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 15-JAN-2008, entry version 80. DE Aconitate hydratase, mitochondrial precursor (EC 4.2.1.3) (Citrate DE hydro-lyase) (Aconitase). GN Name=ACO1; Synonyms=GLU1; OrderedLocusNames=YLR304C; GN ORFNames=L8003.22; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 44774 / 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 plus RT glutamate."; RL Mol. Cell. Biol. 10:3551-3561(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313267; PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [3] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, AND MASS RP SPECTROMETRY. RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409, AND MASS RP SPECTROMETRY. RX PubMed=17761666; DOI=10.1074/mcp.M700098-MCP200; RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; RT "Profiling phosphoproteins of yeast mitochondria reveals a role of RT phosphorylation in assembly of the ATP synthase."; RL Mol. Cell. Proteomics 6:1896-1906(2007). CC -!- FUNCTION: Required for growth on nonfermentable carbon sources and CC for biosynthesis of glutamate. CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- ENZYME REGULATION: Subject to catabolite regulation. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. CC -!- SUBUNIT: Monomer. CC -!- INTERACTION: CC P40555:NAS2; NbExp=1; IntAct=EBI-2104, EBI-14024; CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm. Note=Mitochondrial CC and extramitochondrial. CC -!- MISCELLANEOUS: Present with 96700 molecules/cell in log phase SD CC medium. 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; -; Genomic_DNA. DR EMBL; U17243; AAB67348.1; -; Genomic_DNA. DR PIR; S50387; S50387. DR RefSeq; NP_013407.1; -. DR HSSP; P20004; 1AMJ. DR DIP; DIP:4679N; -. DR IntAct; P19414; -. DR PeptideAtlas; P19414; -. DR Ensembl; YLR304C; Saccharomyces cerevisiae. DR GeneID; 851013; -. DR GenomeReviews; Y13138_GR; YLR304C. DR KEGG; sce:YLR304C; -. DR CYGD; YLR304c; -. DR SGD; S000004295; ACO1. DR LinkHub; P19414; -. DR GermOnline; YLR304C; Saccharomyces cerevisiae. DR GO; GO:0005829; C:cytosol; TAS:SGD. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD. DR GO; GO:0003994; F:aconitate hydratase activity; TAS:SGD. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD. DR GO; GO:0006101; P:citrate metabolic process; TAS:SGD. DR GO; GO:0006537; P:glutamate biosynthetic process; TAS:SGD. DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD. DR GO; GO:0019541; P:propionate metabolic process; IEP:SGD. DR GO; GO:0042493; P:response to drug; IMP:SGD. DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:SGD. DR InterPro; IPR012084; Aco_LysF. DR InterPro; IPR000573; Aconitase_C. DR InterPro; IPR006248; Aconitase_mito. DR InterPro; IPR001030; Aconitase_N. DR PANTHER; PTHR11670:SF5; Aconitase_mito; 1. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PIRSF; PIRSF001417; LysF; 1. DR PRINTS; PR00415; ACONITASE. DR ProDom; PD000511; Aconitase_N; 1. DR TIGRFAMs; TIGR01340; aconitase_mito; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Lyase; KW Metal-binding; Mitochondrion; Phosphoprotein; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1 ? Mitochondrion. FT CHAIN ? 778 Aconitate hydratase. FT /FTId=PRO_0000000547. 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 MOD_RES 409 409 Phosphothreonine. FT MOD_RES 556 556 Phosphoserine. 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 //