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P19414 (ACON_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aconitate hydratase, mitochondrial

Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
Name:ACO1
Synonyms:GLU1
Ordered Locus Names:YLR304C
ORF Names:L8003.22
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for growth on nonfermentable carbon sources and for biosynthesis of glutamate.

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Enzyme regulation

Subject to catabolite regulation.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.

Subunit structure

Monomer.

Subcellular location

Mitochondrion. Cytoplasm. Note: Mitochondrial and extramitochondrial.

Miscellaneous

Present with 96700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 778Aconitate hydratase, mitochondrialPRO_0000000547

Regions

Region188 – 1903Substrate binding By similarity
Region667 – 6682Substrate binding By similarity

Sites

Metal binding3821Iron-sulfur (4Fe-4S) By similarity
Metal binding4451Iron-sulfur (4Fe-4S) By similarity
Metal binding4481Iron-sulfur (4Fe-4S) By similarity
Binding site951Substrate By similarity
Binding site4711Substrate By similarity
Binding site4761Substrate By similarity
Binding site6041Substrate By similarity

Amino acid modifications

Modified residue3511Phosphothreonine Ref.7
Modified residue4091Phosphothreonine Ref.6
Modified residue5561Phosphoserine Ref.5

Experimental info

Sequence conflict527 – 54923DGLPQ…PADRS → RWFASKEVMMLVRTLTKLHL QTVA in AAA34389. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19414 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: AA9EB9A24388090E

FASTA77885,368
        10         20         30         40         50         60 
MLSARSAIKR PIVRGLATVS NLTRDSKVNQ NLLEDHSFIN YKQNVETLDI VRKRLNRPFT 

        70         80         90        100        110        120 
YAEKILYGHL DDPHGQDIQR GVSYLKLRPD RVACQDATAQ MAILQFMSAG LPQVAKPVTV 

       130        140        150        160        170        180 
HCDHLIQAQV GGEKDLKRAI DLNKEVYDFL ASATAKYNMG FWKPGSGIIH QIVLENYAFP 

       190        200        210        220        230        240 
GALIIGTDSH TPNAGGLGQL AIGVGGADAV DVMAGRPWEL KAPKILGVKL TGKMNGWTSP 

       250        260        270        280        290        300 
KDIILKLAGI TTVKGGTGKI VEYFGDGVDT FSATGMGTIC NMGAEIGATT SVFPFNKSMI 

       310        320        330        340        350        360 
EYLEATGRGK IADFAKLYHK DLLSADKDAE YDEVVEIDLN TLEPYINGPF TPDLATPVSK 

       370        380        390        400        410        420 
MKEVAVANNW PLDVRVGLIG SCTNSSYEDM SRSASIVKDA AAHGLKSKTI FTVTPGSEQI 

       430        440        450        460        470        480 
RATIERDGQL ETFKEFGGIV LANACGPCIG QWDRRDIKKG DKNTIVSSYN RNFTSRNDGN 

       490        500        510        520        530        540 
PQTHAFVASP ELVTAFAIAG DLRFNPLTDK LKDKDGNEFM LKPPHGDGLP QRGYDAGENT 

       550        560        570        580        590        600 
YQAPPADRST VEVKVSPTSD RLQLLKPFKP WDGKDAKDMP ILIKAVGKTT TDHISMAGPW 

       610        620        630        640        650        660 
LKYRGHLENI SNNYMIGAIN AENKKANCVK NVYTGEYKGV PDTARDYRDQ GIKWVVIGDE 

       670        680        690        700        710        720 
NFGEGSSREH AALEPRFLGG FAIITKSFAR IHETNLKKQG LLPLNFKNPA DYDKINPDDR 

       730        740        750        760        770 
IDILGLAELA PGKPVTMRVH PKNGKPWDAV LTHTFNDEQI EWFKYGSALN KIKADEKK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate."
Gangloff S.P., Marguet D., Lauquin G.J.-M.
Mol. Cell. Biol. 10:3551-3561(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 44774 / DBY747.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, MASS SPECTROMETRY.
Strain: ADR376.
[6]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409, MASS SPECTROMETRY.
Strain: ATCC 76625 / YPH499.
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33131 Genomic DNA. Translation: AAA34389.1.
U17243 Genomic DNA. Translation: AAB67348.1.
BK006945 Genomic DNA. Translation: DAA09613.1.
PIRS50387.
RefSeqNP_013407.1. NM_001182192.1.

3D structure databases

ProteinModelPortalP19414.
SMRP19414. Positions 26-778.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4679N.
IntActP19414. 23 interactions.
MINTMINT-557728.
STRING4932.YLR304C.

Proteomic databases

PaxDbP19414.
PeptideAtlasP19414.
PRIDEP19414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR304C; YLR304C; YLR304C.
GeneID851013.
KEGGsce:YLR304C.

Organism-specific databases

CYGDYLR304c.
SGDS000004295. ACO1.

Phylogenomic databases

eggNOGCOG1048.
GeneTreeENSGT00530000063060.
HOGENOMHOG000224293.
KOK01681.
OMAAINAENK.
OrthoDBEOG4HX885.

Enzyme and pathway databases

ReactomeREACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.
UniPathwayUPA00223; UER00718.

Gene expression databases

GenevestigatorP19414.
GermOnlineYLR304C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF5. PTHR11670:SF5. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01340. aconitase_mito. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967571.

Entry information

Entry nameACON_YEAST
AccessionPrimary (citable) accession number: P19414
Secondary accession number(s): D6VYU7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families