Aconitate hydratase, mitochondrial precursor - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P19414 (ACON_YEAST)

Last modified November 3, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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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.

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General annotation (Comments)

Function	Required for growth on nonfermentable carbon sources and for biosynthesis of glutamate.
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.
Subunit structure	Monomer.
Subcellular location	Mitochondrion. Cytoplasm. Note: Mitochondrial and extramitochondrial.
Miscellaneous	Present with 96700 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

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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
Gene Ontology (GO)
Biological process	citrate metabolic process Traceable author statement. Source: SGD glutamate biosynthetic process Traceable author statement. Source: SGD mitochondrial genome maintenance Inferred from mutant phenotype. Source: SGD propionate metabolic process Inferred from expression pattern. Source: SGD response to drug Inferred from mutant phenotype. Source: SGD tricarboxylic acid cycle Traceable author statement. Source: SGD
Cellular component	cytosol Traceable author statement. Source: SGD mitochondrial nucleoid Inferred from direct assay. Source: SGD
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Traceable author statement. Source: SGD double-stranded DNA binding Inferred from direct assay. Source: SGD iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct single-stranded DNA binding Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAS2	P40555	1	EBI-2104,EBI-14024

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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

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

Amino acid modifications

Modified residue

351

Phosphothreonine Ref.6

Modified residue

409

Phosphothreonine Ref.5

Modified residue

556

Phosphoserine Ref.4

Experimental info

Sequence conflict

527 – 549

DGLPQ…PADRS → RWFASKEVMMLVRTLTKLHL QTVA Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P19414-1 [UniParc].

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

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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: 1972545] [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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, MASS SPECTROMETRY.
[5]	"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: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409, MASS SPECTROMETRY.
[6]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M33131 Genomic DNA. Translation: AAA34389.1. U17243 Genomic DNA. Translation: AAB67348.1.
PIR	S50387.
RefSeq	NP_013407.1.
3D structure databases
HSSP	HSSP built from PDB template 1AMJ based on UniProtKB P20004.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4679N.
IntAct	P19414. 55 interactions.
STRING	P19414.
Proteomic databases
PeptideAtlas	P19414.
PRIDE	P19414.
Genome annotation databases
Ensembl	YLR304C; YLR304C; YLR304C; Saccharomyces cerevisiae. [Genome view]
GeneID	851013.
GenomeReviews	Gene locus YLR304C in contig Y13138_GR.
KEGG	sce:YLR304C.
NMPDR	fig\|4932.3.peg.4425.
Organism-specific databases
CYGD	YLR304c.
SGD	S000004295. ACO1.
Phylogenomic databases
HOGENOM	P19414.
OMA	PGKPLKC.
Enzyme and pathway databases
BRENDA	4.2.1.3. 250.
Gene expression databases
ArrayExpress	P19414.
Genevestigator	P19414.
GermOnline	YLR304C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. 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]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF5. Aconitase_mito. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01340. aconitase_mito. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967571.

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Entry information

Entry name

ACON_YEAST

Accession

Primary (citable) accession number: P19414

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents