Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetolactate synthase catalytic subunit, mitochondrial

Gene

ILV2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Enzyme regulationi

The regulatory subunit ILV6 stimulates enzymatic activity seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP.1 Publication

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391Thiamine pyrophosphate
Binding sitei241 – 2411FAD1 Publication
Metal bindingi550 – 5501Magnesium
Metal bindingi577 – 5771Magnesium
Metal bindingi579 – 5791Magnesium; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi355 – 37622FAD1 PublicationAdd
BLAST
Nucleotide bindingi407 – 42620FAD1 PublicationAdd
BLAST

GO - Molecular functioni

  • acetolactate synthase activity Source: SGD
  • flavin adenine dinucleotide binding Source: SGD
  • magnesium ion binding Source: InterPro
  • thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-29.
BRENDAi2.2.1.6. 984.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ILV2
Synonyms:SMR1
Ordered Locus Names:YMR108W
ORF Names:YM9718.07
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR108W.
SGDiS000004714. ILV2.

Subcellular locationi

GO - Cellular componenti

  • acetolactate synthase complex Source: SGD
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 9090MitochondrionSequence analysisAdd
BLAST
Chaini91 – 687597Acetolactate synthase catalytic subunit, mitochondrialPRO_0000035664Add
BLAST

Proteomic databases

MaxQBiP07342.
PeptideAtlasiP07342.
PRIDEiP07342.

PTM databases

iPTMnetiP07342.

Interactioni

Subunit structurei

Homodimer. The acetolactate synthase complex contains the catalytic regulatory subunit ILV2 and the regulatory small subunit ILV6.1 Publication

Protein-protein interaction databases

BioGridi35284. 30 interactions.
DIPiDIP-1104N.
IntActiP07342. 42 interactions.
MINTiMINT-693321.

Chemistry

BindingDBiP07342.

Structurei

Secondary structure

1
687
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni88 – 914Combined sources
Helixi94 – 10411Combined sources
Beta strandi109 – 1124Combined sources
Helixi116 – 1183Combined sources
Helixi119 – 1246Combined sources
Turni125 – 1273Combined sources
Beta strandi129 – 1346Combined sources
Helixi139 – 15315Combined sources
Beta strandi157 – 1615Combined sources
Helixi165 – 1684Combined sources
Helixi171 – 18010Combined sources
Beta strandi184 – 1907Combined sources
Turni193 – 1975Combined sources
Helixi206 – 2094Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2196Combined sources
Helixi223 – 2253Combined sources
Helixi226 – 23813Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi244 – 2507Combined sources
Helixi251 – 2555Combined sources
Helixi264 – 2674Combined sources
Helixi279 – 2835Combined sources
Helixi285 – 29713Combined sources
Beta strandi300 – 3067Combined sources
Helixi308 – 3125Combined sources
Helixi316 – 32611Combined sources
Beta strandi331 – 3333Combined sources
Helixi335 – 3373Combined sources
Beta strandi348 – 3514Combined sources
Helixi358 – 3669Combined sources
Beta strandi368 – 3747Combined sources
Turni379 – 3813Combined sources
Beta strandi382 – 3843Combined sources
Helixi385 – 3873Combined sources
Helixi390 – 3978Combined sources
Beta strandi402 – 4087Combined sources
Helixi410 – 4123Combined sources
Beta strandi413 – 4175Combined sources
Beta strandi420 – 4256Combined sources
Helixi427 – 4359Combined sources
Helixi445 – 45713Combined sources
Beta strandi467 – 4693Combined sources
Helixi473 – 48513Combined sources
Beta strandi491 – 4955Combined sources
Helixi499 – 5079Combined sources
Helixi528 – 53811Combined sources
Beta strandi542 – 5498Combined sources
Helixi550 – 5567Combined sources
Helixi557 – 5593Combined sources
Helixi560 – 5667Combined sources
Beta strandi571 – 5766Combined sources
Helixi581 – 59010Combined sources
Helixi605 – 6117Combined sources
Beta strandi615 – 6195Combined sources
Helixi622 – 6243Combined sources
Helixi625 – 63410Combined sources
Beta strandi639 – 6457Combined sources
Beta strandi652 – 6543Combined sources
Helixi669 – 68214Combined sources
Turni683 – 6853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSCX-ray2.60A/B58-687[»]
1N0HX-ray2.80A/B58-687[»]
1T9AX-ray2.59A/B58-687[»]
1T9BX-ray2.20A/B58-687[»]
1T9CX-ray2.34A/B58-687[»]
1T9DX-ray2.30A/B/C/D58-687[»]
5FEMX-ray2.17A/B58-687[»]
DisProtiDP00398.
ProteinModelPortaliP07342.
SMRiP07342. Positions 83-687.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07342.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni499 – 57981Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000075465.
HOGENOMiHOG000258448.
InParanoidiP07342.
KOiK01652.
OMAiHSWVVRD.
OrthoDBiEOG7GJ6NH.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP
60 70 80 90 100
ASKRPEPAPS FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE
110 120 130 140 150
MMSRQNVDTV FGYPGGAILP VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA
160 170 180 190 200
RASGKPGVVL VTSGPGATNV VTPMADAFAD GIPMVVFTGQ VPTSAIGTDA
210 220 230 240 250
FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG RPGPVLVDLP
260 270 280 290 300
KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK
310 320 330 340 350
KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD
360 370 380 390 400
MLGMHGCATA NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR
410 420 430 440 450
GGIIHFEVSP KNINKVVQTQ IAVEGDATTN LGKMMSKIFP VKERSEWFAQ
460 470 480 490 500
INKWKKEYPY AYMEETPGSK IKPQTVIKKL SKVANDTGRH VIVTTGVGQH
510 520 530 540 550
QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP ESLVIDIDGD
560 570 580 590 600
ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ
610 620 630 640 650
LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP
660 670 680
VLPMVAGGSG LDEFINFDPE VERQQTELRH KRTGGKH
Length:687
Mass (Da):74,937
Last modified:April 1, 1988 - v1
Checksum:iB03C4D0F38AA1362
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02549 Genomic DNA. Translation: CAA26400.1.
Z49702 Genomic DNA. Translation: CAA89744.1.
AY692995 Genomic DNA. Translation: AAT93014.1.
BK006946 Genomic DNA. Translation: DAA10005.1.
PIRiA23808. YCBYI.
RefSeqiNP_013826.1. NM_001182608.1.

Genome annotation databases

EnsemblFungiiYMR108W; YMR108W; YMR108W.
GeneIDi855135.
KEGGisce:YMR108W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02549 Genomic DNA. Translation: CAA26400.1.
Z49702 Genomic DNA. Translation: CAA89744.1.
AY692995 Genomic DNA. Translation: AAT93014.1.
BK006946 Genomic DNA. Translation: DAA10005.1.
PIRiA23808. YCBYI.
RefSeqiNP_013826.1. NM_001182608.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSCX-ray2.60A/B58-687[»]
1N0HX-ray2.80A/B58-687[»]
1T9AX-ray2.59A/B58-687[»]
1T9BX-ray2.20A/B58-687[»]
1T9CX-ray2.34A/B58-687[»]
1T9DX-ray2.30A/B/C/D58-687[»]
5FEMX-ray2.17A/B58-687[»]
DisProtiDP00398.
ProteinModelPortaliP07342.
SMRiP07342. Positions 83-687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35284. 30 interactions.
DIPiDIP-1104N.
IntActiP07342. 42 interactions.
MINTiMINT-693321.

Chemistry

BindingDBiP07342.
ChEMBLiCHEMBL1075095.

PTM databases

iPTMnetiP07342.

Proteomic databases

MaxQBiP07342.
PeptideAtlasiP07342.
PRIDEiP07342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR108W; YMR108W; YMR108W.
GeneIDi855135.
KEGGisce:YMR108W.

Organism-specific databases

EuPathDBiFungiDB:YMR108W.
SGDiS000004714. ILV2.

Phylogenomic databases

GeneTreeiENSGT00550000075465.
HOGENOMiHOG000258448.
InParanoidiP07342.
KOiK01652.
OMAiHSWVVRD.
OrthoDBiEOG7GJ6NH.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciYEAST:MONOMER3O-29.
BRENDAi2.2.1.6. 984.

Miscellaneous databases

EvolutionaryTraceiP07342.
NextBioi978513.
PROiP07342.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-687 IN COMPLEX WITH FAD; HERBICIDE AND THIAMINE DIPHOSPHATE.

Entry informationi

Entry nameiILVB_YEAST
AccessioniPrimary (citable) accession number: P07342
Secondary accession number(s): D6VZT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 11, 2016
This is version 182 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.