Aconitate hydratase, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P19414 (ACON_YEAST) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	778 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial genome maintenance Inferred from mutant phenotype PubMed 15692048. Source: SGD tricarboxylic acid cycle Inferred from direct assay Ref.1. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 15975908. Source: SGD mitochondrial intermembrane space Traceable author statement. Source: Reactome mitochondrial nucleoid Inferred from direct assay PubMed 10869431. Source: SGD
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from direct assay Ref.1. Source: SGD citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC double-stranded DNA binding Inferred from direct assay PubMed 17698960. Source: SGD isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Inferred from direct assay PubMed 17698960. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion

Chain

? – 778

Aconitate hydratase, mitochondrial

PRO_0000000547

Regions

Region

188 – 190

Substrate binding By similarity

Region

667 – 668

Substrate binding By similarity

Sites

Metal binding

382

Iron-sulfur (4Fe-4S) By similarity

Metal binding

445

Iron-sulfur (4Fe-4S) By similarity

Metal binding

448

Iron-sulfur (4Fe-4S) By similarity

Binding site

Substrate By similarity

Binding site

471

Substrate By similarity

Binding site

476

Substrate By similarity

Binding site

604

Substrate By similarity

Amino acid modifications

Modified residue

351

Phosphothreonine Ref.7

Modified residue

409

Phosphothreonine Ref.6

Modified residue

556

Phosphoserine Ref.5

Experimental info

Sequence conflict

527 – 549

DGLPQ…PADRS → RWFASKEVMMLVRTLTKLHL QTVA in AAA34389. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P19414 [UniParc].

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

FASTA

778

85,368

        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' referencesShow '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. 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.
PIR	S50387.
RefSeq	NP_013407.1. NM_001182192.1.
3D structure databases
ProteinModelPortal	P19414.
SMR	P19414. Positions 26-778.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4679N.
IntAct	P19414. 23 interactions.
MINT	MINT-557728.
STRING	4932.YLR304C.
Proteomic databases
PaxDb	P19414.
PeptideAtlas	P19414.
PRIDE	P19414.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR304C; YLR304C; YLR304C.
GeneID	851013.
KEGG	sce:YLR304C.
Organism-specific databases
CYGD	YLR304c.
SGD	S000004295. ACO1.
Phylogenomic databases
eggNOG	COG1048.
GeneTree	ENSGT00530000063060.
HOGENOM	HOG000224293.
KO	K01681.
OMA	AINAENK.
OrthoDB	EOG4HX885.
Enzyme and pathway databases
Reactome	REACT_118590. Mitochondrial Protein Import (yeast). REACT_85873. Metabolism of proteins.
UniPathway	UPA00223; UER00718.
Gene expression databases
Genevestigator	P19414.
GermOnline	YLR304C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
InterPro	IPR015931. 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]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF5. PTHR11670:SF5. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01340. aconitase_mito. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967571.

Entry information

Entry name

ACON_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents