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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, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)
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, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)
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)DescriptionActionsGraphical viewLength
Binding sitei139Thiamine pyrophosphate1
Binding sitei241FAD1 Publication1
Metal bindingi550Magnesium1
Metal bindingi577Magnesium1
Metal bindingi579Magnesium; via carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi355 – 376FAD1 PublicationAdd BLAST22
Nucleotide bindingi407 – 426FAD1 PublicationAdd BLAST20

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 databases

ChEMBLiCHEMBL1075095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 90MitochondrionSequence analysisAdd BLAST90
ChainiPRO_000003566491 – 687Acetolactate synthase catalytic subunit, mitochondrialAdd BLAST597

Proteomic databases

MaxQBiP07342.
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. 31 interactors.
DIPiDIP-1104N.
IntActiP07342. 42 interactors.
MINTiMINT-693321.

Chemistry databases

BindingDBiP07342.

Structurei

Secondary structure

1687
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni88 – 91Combined sources4
Helixi94 – 104Combined sources11
Beta strandi109 – 113Combined sources5
Helixi116 – 118Combined sources3
Helixi119 – 124Combined sources6
Turni125 – 127Combined sources3
Beta strandi129 – 134Combined sources6
Helixi139 – 153Combined sources15
Beta strandi157 – 161Combined sources5
Helixi165 – 168Combined sources4
Helixi171 – 180Combined sources10
Beta strandi184 – 190Combined sources7
Turni193 – 197Combined sources5
Helixi206 – 209Combined sources4
Helixi211 – 213Combined sources3
Beta strandi214 – 219Combined sources6
Helixi223 – 225Combined sources3
Helixi226 – 238Combined sources13
Beta strandi239 – 241Combined sources3
Beta strandi244 – 250Combined sources7
Helixi251 – 255Combined sources5
Helixi264 – 267Combined sources4
Helixi279 – 298Combined sources20
Beta strandi300 – 306Combined sources7
Helixi308 – 312Combined sources5
Helixi316 – 327Combined sources12
Beta strandi331 – 333Combined sources3
Helixi335 – 337Combined sources3
Beta strandi348 – 351Combined sources4
Helixi358 – 366Combined sources9
Beta strandi368 – 374Combined sources7
Helixi379 – 382Combined sources4
Helixi385 – 387Combined sources3
Helixi390 – 397Combined sources8
Beta strandi402 – 408Combined sources7
Helixi410 – 412Combined sources3
Beta strandi415 – 417Combined sources3
Beta strandi420 – 425Combined sources6
Helixi427 – 434Combined sources8
Helixi435 – 437Combined sources3
Helixi445 – 457Combined sources13
Beta strandi467 – 469Combined sources3
Helixi473 – 485Combined sources13
Beta strandi491 – 495Combined sources5
Helixi499 – 507Combined sources9
Helixi528 – 538Combined sources11
Beta strandi542 – 549Combined sources8
Helixi550 – 556Combined sources7
Helixi557 – 559Combined sources3
Helixi560 – 566Combined sources7
Beta strandi571 – 576Combined sources6
Helixi581 – 590Combined sources10
Helixi605 – 611Combined sources7
Beta strandi614 – 619Combined sources6
Helixi622 – 624Combined sources3
Helixi625 – 634Combined sources10
Beta strandi639 – 645Combined sources7
Beta strandi652 – 654Combined sources3
Helixi669 – 682Combined sources14
Turni683 – 685Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07342.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni499 – 579Thiamine pyrophosphate bindingAdd BLAST81

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000075465.
HOGENOMiHOG000258448.
InParanoidiP07342.
KOiK01652.
OMAiHSWVVRD.
OrthoDBiEOG092C14MZ.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35284. 31 interactors.
DIPiDIP-1104N.
IntActiP07342. 42 interactors.
MINTiMINT-693321.

Chemistry databases

BindingDBiP07342.
ChEMBLiCHEMBL1075095.

PTM databases

iPTMnetiP07342.

Proteomic databases

MaxQBiP07342.
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.
OrthoDBiEOG092C14MZ.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP07342.
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...

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: November 2, 2016
This is version 187 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.