Acetolactate synthase catalytic subunit, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

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=AHAS
Short name=ALS

Gene names

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

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	687 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)

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.5
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.
Sequence similarities	Belongs to the TPP enzyme family.

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 Reference proteome
Gene Ontology (GO)
Biological_process	branched-chain amino acid biosynthetic process Inferred from direct assay PubMed 2406721. Source: SGD isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway valine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	acetolactate synthase complex Inferred from direct assay Ref.5. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278 PubMed 16823961. Source: SGD
Molecular_function	acetolactate synthase activity Inferred from direct assay Ref.5. Source: SGD flavin adenine dinucleotide binding Inferred from direct assay PubMed 15709745. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: InterPro thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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.7

Secondary structure

1

.

687

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07342 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: B03C4D0F38AA1362
Show »

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

« Hide

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] [Europe PMC] [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] [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]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: RECONSTITUTION OF THE ACETOLACTATE SYNTHASE COMPLEX, ENZYME REGULATION.
[6]	"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].
[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 SER-270, MASS SPECTROMETRY.
[8]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 58-687.
[9]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-687 IN COMPLEX WITH FAD; HERBICIDE AND THIAMINE DIPHOSPHATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02549 Genomic DNA. Translation: CAA26400.1.
Z49702 Genomic DNA. Translation: CAA89744.1.
AY692995 Genomic DNA. Translation: AAT93014.1.
BK006946 Genomic DNA. Translation: DAA10005.1.

PIR

YCBYI. A23808.

RefSeq

NP_013826.1. NM_001182608.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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.

ProteinModelPortal

P07342.

SMR

P07342. Positions 83-687.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1104N.

IntAct

P07342. 39 interactions.

MINT

MINT-693321.

STRING

4932.YMR108W.

Proteomic databases

PaxDb

P07342.

PeptideAtlas

P07342.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR108W; YMR108W; YMR108W.

GeneID

855135.

KEGG

sce:YMR108W.

Organism-specific databases

CYGD

YMR108w.

SGD

S000004714. ILV2.

Phylogenomic databases

eggNOG

COG0028.

GeneTree

ENSGT00550000075465.

HOGENOM

HOG000258448.

KO

K01652.

OMA

NNEEQGM.

OrthoDB

EOG44TSH5.

Enzyme and pathway databases

UniPathway

UPA00047; UER00055.
UPA00049; UER00059.

Gene expression databases

Genevestigator

P07342.

GermOnline

YMR108W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR012846. Acetolactate_synth_lsu.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]

PANTHER

PTHR18968:SF13. PTHR18968:SF13. 1 hit.

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

BindingDB

P07342.

ChEMBL

CHEMBL1075095.

EvolutionaryTrace

P07342.

NextBio

978513.

Entry information

Entry name

ILVB_YEAST

Accession

Primary (citable) accession number: P07342
Secondary accession number(s): D6VZT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	April 3, 2013
This is version 155 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program