UniProtKB - P07342 (ILVB_YEAST)
Acetolactate synthase catalytic subunit, mitochondrial
ILV2
Functioni
Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.
1 PublicationMiscellaneous
Catalytic activityi
- EC:2.2.1.61 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:2.2.1.61 PublicationThis reaction proceeds in the forward1 Publication direction.
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
Activity regulationi
Kineticsi
- KM=8.6 mM for pyruvate (catalytic subunit only)1 Publication
- KM=18.1 mM for pyruvate (reconstituted into the acetolactate synthase complex with the regulatory subunit)1 Publication
pH dependencei
: L-isoleucine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.1 Publication 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.1 Publication 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 139 | Thiamine pyrophosphate | 1 | |
Binding sitei | 241 | FAD1 Publication | 1 | |
Metal bindingi | 550 | Magnesium | 1 | |
Metal bindingi | 577 | Magnesium | 1 | |
Metal bindingi | 579 | Magnesium; via carbonyl oxygen | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 355 – 376 | FAD1 PublicationAdd BLAST | 22 | |
Nucleotide bindingi | 407 – 426 | FAD1 PublicationAdd BLAST | 20 |
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
- branched-chain amino acid biosynthetic process Source: SGD
- isoleucine biosynthetic process Source: GO_Central
- valine biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | Amino-acid biosynthesis, Branched-chain amino acid biosynthesis |
Ligand | Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BRENDAi | 2.2.1.6, 984 |
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
Names & Taxonomyi
Protein namesi | Recommended name: Acetolactate synthase catalytic subunit, mitochondrialCurated (EC:2.2.1.61 Publication)Alternative name(s): Acetohydroxy-acid synthase catalytic subunit1 Publication Short name: AHAS Short name: ALS |
Gene namesi | Name:ILV2 Synonyms:SMR1 Ordered Locus Names:YMR108W ORF Names:YM9718.07 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000004714, ILV2 |
VEuPathDBi | FungiDB:YMR108W |
Subcellular locationi
Mitochondrion
- Mitochondrion 1 Publication
Mitochondrion
- mitochondrion Source: SGD
Other locations
- acetolactate synthase complex Source: SGD
Keywords - Cellular componenti
MitochondrionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 90 | MitochondrionSequence analysisAdd BLAST | 90 | |
ChainiPRO_0000035664 | 91 – 687 | Acetolactate synthase catalytic subunit, mitochondrialAdd BLAST | 597 |
Proteomic databases
MaxQBi | P07342 |
PaxDbi | P07342 |
PRIDEi | P07342 |
PTM databases
CarbonylDBi | P07342 |
iPTMneti | P07342 |
Interactioni
Subunit structurei
Homodimer. The acetolactate synthase complex contains the catalytic subunit ILV2 and the regulatory small subunit ILV6.
1 PublicationProtein-protein interaction databases
BioGRIDi | 35284, 79 interactors |
ComplexPortali | CPX-3034, Acetolactate synthase complex |
DIPi | DIP-1104N |
IntActi | P07342, 73 interactors |
MINTi | P07342 |
STRINGi | 4932.YMR108W |
Chemistry databases
BindingDBi | P07342 |
Miscellaneous databases
RNActi | P07342, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P07342 |
SMRi | P07342 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07342 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 43 – 68 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 499 – 579 | Thiamine pyrophosphate bindingAdd BLAST | 81 |
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG4166, Eukaryota |
GeneTreei | ENSGT00940000176650 |
HOGENOMi | CLU_013748_1_2_1 |
InParanoidi | P07342 |
OMAi | CFGTSGP |
Family and domain databases
CDDi | cd02015, TPP_AHAS, 1 hit |
DisProti | DP00398 |
InterProi | View protein in InterPro IPR012846, Acetolactate_synth_lsu IPR039368, AHAS_TPP 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 IPR045229, TPP_enz IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR18968, PTHR18968, 1 hit |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF00205, TPP_enzyme_M, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00118, acolac_lg, 1 hit |
PROSITEi | View protein in PROSITE PS00187, TPP_ENZYMES, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
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 |
PIRi | A23808, YCBYI |
RefSeqi | NP_013826.1, NM_001182608.1 |
Genome annotation databases
EnsemblFungii | YMR108W_mRNA; YMR108W; YMR108W |
GeneIDi | 855135 |
KEGGi | sce:YMR108W |
Similar proteinsi
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 |
PIRi | A23808, YCBYI |
RefSeqi | NP_013826.1, NM_001182608.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
5FEM | X-ray | 2.17 | A/B | 58-687 | [»] | |
5IMS | X-ray | 1.98 | A/B | 58-687 | [»] | |
5WKC | X-ray | 2.33 | A/B/D/E | 58-687 | [»] | |
6BD3 | X-ray | 2.28 | A/B | 58-687 | [»] | |
6BD9 | X-ray | 1.98 | A/B | 58-687 | [»] | |
6U9D | X-ray | 3.19 | A/B/E/F/I/J/M/N/Q/R/U/V | 58-687 | [»] | |
AlphaFoldDBi | P07342 | |||||
SMRi | P07342 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 35284, 79 interactors |
ComplexPortali | CPX-3034, Acetolactate synthase complex |
DIPi | DIP-1104N |
IntActi | P07342, 73 interactors |
MINTi | P07342 |
STRINGi | 4932.YMR108W |
Chemistry databases
BindingDBi | P07342 |
ChEMBLi | CHEMBL1075095 |
PTM databases
CarbonylDBi | P07342 |
iPTMneti | P07342 |
Proteomic databases
MaxQBi | P07342 |
PaxDbi | P07342 |
PRIDEi | P07342 |
Genome annotation databases
EnsemblFungii | YMR108W_mRNA; YMR108W; YMR108W |
GeneIDi | 855135 |
KEGGi | sce:YMR108W |
Organism-specific databases
SGDi | S000004714, ILV2 |
VEuPathDBi | FungiDB:YMR108W |
Phylogenomic databases
eggNOGi | KOG4166, Eukaryota |
GeneTreei | ENSGT00940000176650 |
HOGENOMi | CLU_013748_1_2_1 |
InParanoidi | P07342 |
OMAi | CFGTSGP |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
BRENDAi | 2.2.1.6, 984 |
Miscellaneous databases
EvolutionaryTracei | P07342 |
PROi | PR:P07342 |
RNActi | P07342, protein |
Family and domain databases
CDDi | cd02015, TPP_AHAS, 1 hit |
DisProti | DP00398 |
InterProi | View protein in InterPro IPR012846, Acetolactate_synth_lsu IPR039368, AHAS_TPP 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 IPR045229, TPP_enz IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR18968, PTHR18968, 1 hit |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF00205, TPP_enzyme_M, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00118, acolac_lg, 1 hit |
PROSITEi | View protein in PROSITE PS00187, TPP_ENZYMES, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ILVB_YEAST | |
Accessioni | P07342Primary (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 25, 2022 | |
This is version 226 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families