Acetolactate synthase catalytic subunit, mitochondrial precursor - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
    Acetolactate synthase catalytic subunit, mitochondrial
    EC=2.2.1.6
Alternative name(s):
    Acetohydroxy-acid synthase catalytic subunit
      Short name=ALS
      Short name=AHAS

Gene names

Name:	ILV2
Synonyms:	SMR1
Ordered Locus Names:	YMR108W
ORF Names:	YM9718.07

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	687 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)

Catalytic activity	2 pyruvate = 2-acetolactate + CO₂.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Enzyme regulation	The regulatory subunit ILV6 stimulates enzymatic activity seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP. Ref.4
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
Subunit structure	Homodimer. The acetolactate synthase complex contains the catalytic regulatory subunit ILV2 and the regulatory small subunit ILV6.
Subcellular location	Mitochondrion.
Miscellaneous	Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry. Present with 31900 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the TPP enzyme family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from direct assay. Source: SGD
Cellular component	acetolactate synthase complex Ref.4 Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	FAD binding Inferred from direct assay. Source: SGD acetolactate synthase activity Ref.4 Inferred from direct assay. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 90

90

Mitochondrion Potential

Chain

91 – 687

597

Acetolactate synthase catalytic subunit, mitochondrial

PRO_0000035664

Regions

Nucleotide binding

355 – 376

22

FAD

Nucleotide binding

407 – 426

20

FAD

Region

499 – 579

81

Thiamine pyrophosphate binding

Sites

Metal binding

550

1

Magnesium

Metal binding

577

1

Magnesium

Metal binding

579

1

Magnesium; via carbonyl oxygen

Binding site

139

1

Thiamine pyrophosphate

Binding site

241

1

FAD

Amino acid modifications

Modified residue

270

1

Phosphoserine Ref.6

Secondary structure

1

.

687

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P07342-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: B03C4D0F38AA1362
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FASTA

687

74,937

        10         20         30         40         50         60 
MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP ASKRPEPAPS 

        70         80         90        100        110        120 
FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE MMSRQNVDTV FGYPGGAILP 

       130        140        150        160        170        180 
VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA RASGKPGVVL VTSGPGATNV VTPMADAFAD 

       190        200        210        220        230        240 
GIPMVVFTGQ VPTSAIGTDA FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG 

       250        260        270        280        290        300 
RPGPVLVDLP KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK 

       310        320        330        340        350        360 
KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD MLGMHGCATA 

       370        380        390        400        410        420 
NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR GGIIHFEVSP KNINKVVQTQ 

       430        440        450        460        470        480 
IAVEGDATTN LGKMMSKIFP VKERSEWFAQ INKWKKEYPY AYMEETPGSK IKPQTVIKKL 

       490        500        510        520        530        540 
SKVANDTGRH VIVTTGVGQH QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP 

       550        560        570        580        590        600 
ESLVIDIDGD ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ 

       610        620        630        640        650        660 
LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP VLPMVAGGSG 

       670        680 
LDEFINFDPE VERQQTELRH KRTGGKH

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate synthase." Falco S.C., Dumas K.S., Livak K.J. Nucleic Acids Res. 13:4011-4027(1985) [PubMed: 2989783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase." Pang S.S., Duggleby R.G. Biochemistry 38:5222-5231(1999) [PubMed: 10213630] [Abstract] Cited for: RECONSTITUTION OF THE ACETOLACTATE SYNTHASE COMPLEX, ENZYME REGULATION.
[5]	"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].
[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 SER-270, MASS SPECTROMETRY.
[7]	"Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors." Pang S.S., Duggleby R.G., Guddat L.W. J. Mol. Biol. 317:249-262(2002) [PubMed: 11902841] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 58-687.
[8]	"Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase." Pang S.S., Guddat L.W., Duggleby R.G. J. Biol. Chem. 278:7639-7644(2003) [PubMed: 12496246] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-687 IN COMPLEX WITH FAD; HERBICIDE AND THIAMINE DIPHOSPHATE.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X02549 Genomic DNA. Translation: CAA26400.1.
Z49702 Genomic DNA. Translation: CAA89744.1.
AY692995 Genomic DNA. Translation: AAT93014.1.

PIR

YCBYI. A23808.

RefSeq

NP_013826.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JSC	X-ray	2.60	A/B	58-687	[»]
1N0H	X-ray	2.80	A/B	58-687	[»]
1T9A	X-ray	2.59	A/B	58-687	[»]
1T9B	X-ray	2.20	A/B	58-687	[»]
1T9C	X-ray	2.34	A/B	58-687	[»]
1T9D	X-ray	2.30	A/B/C/D	58-687	[»]

DisProt

DP00398.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1104N.

IntAct

P07342. 43 interactions.

Proteomic databases

PeptideAtlas

P07342.

PRIDE

P07342.

Genome annotation databases

Ensembl

YMR108W. Saccharomyces cerevisiae. [Contig view]

GeneID

855135.

GenomeReviews

Gene locus YMR108W in contig Z71257_GR.

KEGG

sce:YMR108W.

NMPDR

fig|4932.3.peg.4874.

Organism-specific databases

CYGD

YMR108w.

SGD

S000004714. ILV2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P07342.

OMA

P07342. QGLGAFD.

Enzyme and pathway databases

BRENDA

2.2.1.6. 250.

Gene expression databases

ArrayExpress

P07342.

GermOnline

YMR108W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR012846. Acetolactate_synth_lsu.
IPR000399. TPP_bd_CS.
IPR012001. TPP_bd_enzyme_N.
IPR011766. TPP_enzyme_bd_C.
IPR012000. TPP_enzyme_M.
[Graphical view]

Pfam

PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00118. acolac_lg. 1 hit.

PROSITE

PS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

978513.

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Entry information

Entry name

ILVB_YEAST

Accession

Primary (citable) accession number: P07342

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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