ID ACON_YEAST Reviewed; 778 AA.
AC P19414; D6VYU7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-APR-2013, entry version 129.
DE RecName: Full=Aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3;
DE AltName: Full=Citrate hydro-lyase;
DE Flags: Precursor;
GN Name=ACO1; Synonyms=GLU1; OrderedLocusNames=YLR304C;
GN ORFNames=L8003.22;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44774 / DBY747;
RX 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 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, AND MASS
RP SPECTROMETRY.
RC STRAIN=ADR376;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409, AND MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 76625 / YPH499;
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, AND MASS
RP SPECTROMETRY.
RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth
RT phosphoproteome analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Required for growth on nonfermentable carbon sources and
CC for biosynthesis of glutamate.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via
CC cis-aconitate (By similarity).
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 isocitrate from oxaloacetate: step 2/2.
CC -!- SUBUNIT: Monomer.
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 http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M33131; AAA34389.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67348.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09613.1; -; Genomic_DNA.
DR PIR; S50387; S50387.
DR RefSeq; NP_013407.1; NM_001182192.1.
DR ProteinModelPortal; P19414; -.
DR SMR; P19414; 26-778.
DR DIP; DIP-4679N; -.
DR IntAct; P19414; 23.
DR MINT; MINT-557728; -.
DR STRING; 4932.YLR304C; -.
DR PaxDb; P19414; -.
DR PeptideAtlas; P19414; -.
DR PRIDE; P19414; -.
DR EnsemblFungi; YLR304C; YLR304C; YLR304C.
DR GeneID; 851013; -.
DR KEGG; sce:YLR304C; -.
DR CYGD; YLR304c; -.
DR SGD; S000004295; ACO1.
DR eggNOG; COG1048; -.
DR GeneTree; ENSGT00530000063060; -.
DR HOGENOM; HOG000224293; -.
DR KO; K01681; -.
DR OMA; AINAENK; -.
DR OrthoDB; EOG4HX885; -.
DR Reactome; REACT_118590; Mitochondrial Protein Import (yeast).
DR Reactome; REACT_85873; Metabolism of proteins.
DR UniPathway; UPA00223; UER00718.
DR NextBio; 967571; -.
DR Genevestigator; P19414; -.
DR GermOnline; YLR304C; Saccharomyces cerevisiae.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IDA:SGD.
DR GO; GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:SGD.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR015937; Acoase/IPM_deHydtase.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF5; PTHR11670:SF5; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 1.
DR SUPFAM; SSF53732; 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; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1 ? Mitochondrion.
FT CHAIN ? 778 Aconitate hydratase, mitochondrial.
FT /FTId=PRO_0000000547.
FT REGION 188 190 Substrate binding (By similarity).
FT REGION 667 668 Substrate binding (By similarity).
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 BINDING 95 95 Substrate (By similarity).
FT BINDING 471 471 Substrate (By similarity).
FT BINDING 476 476 Substrate (By similarity).
FT BINDING 604 604 Substrate (By similarity).
FT MOD_RES 351 351 Phosphothreonine.
FT MOD_RES 409 409 Phosphothreonine.
FT MOD_RES 556 556 Phosphoserine.
FT CONFLICT 527 549 DGLPQRGYDAGENTYQAPPADRS -> RWFASKEVMMLVRT
FT LTKLHLQTVA (in Ref. 1; AAA34389).
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
//
