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UniProtKB - P9WG41 (ILVB1_MYCTU)
Protein
Acetolactate synthase large subunit IlvB1
Gene
ilvB1
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate.
2 PublicationsCatalytic activityi
- EC:2.2.1.61 Publication
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
Inhibited by valine, sulfometuron methyl (SM), sulfonylureas (SU) and imidazolinones (IM). Pyrazosulfuron ethyl (PSE), promisulfuron methyl (PSM), sulfometuron methyl (SMM), metsulfuron methyl (MSM), and chlorimuron ethyl (CE) inhibited more than 80% of the activity.2 Publications
Kineticsi
- KM=2.76 mM for pyruvate (with the catalytic subunit alone at pH 7.5 and at 37 degrees Celsius)2 Publications
- KM=1.56 mM for pyruvate (with the catalytic and regulatory subunits at pH 7.5 and at 37 degrees Celsius)2 Publications
pH dependencei
Optimum pH is between 6 and 7.2 Publications
Temperature dependencei
Optimum temperature is between 35 and 40 degrees Celsius.2 Publications
: L-isoleucine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate. 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. 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 | 85 | Thiamine pyrophosphateBy similarity | 1 | |
Binding sitei | 187 | FADBy similarity | 1 | |
Metal bindingi | 480 | MagnesiumBy similarity | 1 | |
Metal bindingi | 507 | MagnesiumBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 293 – 314 | FADBy similarityAdd BLAST | 22 | |
Nucleotide bindingi | 336 – 355 | FADBy similarityAdd BLAST | 20 |
GO - Molecular functioni
- acetolactate synthase activity Source: MTBBASE
- flavin adenine dinucleotide binding Source: GO_Central
- magnesium ion binding Source: MTBBASE
- thiamine pyrophosphate binding Source: MTBBASE
GO - Biological processi
- branched-chain amino acid biosynthetic process Source: MTBBASE
- isoleucine biosynthetic process Source: MTBBASE
- valine biosynthetic process Source: MTBBASE
Keywordsi
Molecular function | Transferase |
Biological process | Amino-acid biosynthesis, Branched-chain amino acid biosynthesis |
Ligand | FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BRENDAi | 2.2.1.6, 3445 |
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
Names & Taxonomyi
Protein namesi | Recommended name: Acetolactate synthase large subunit IlvB1 (EC:2.2.1.6)Short name: ALS Alternative name(s): Acetohydroxy-acid synthase large subunit Short name: AHAS |
Gene namesi | Name:ilvB1 Ordered Locus Names:Rv3003c ORF Names:MTV012.17c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv3003c |
Subcellular locationi
Cell Wall
- cell wall Source: MTBBASE
Other locations
- acetolactate synthase complex Source: GO_Central
Pathology & Biotechi
Disruption phenotypei
Auxotrophic for all of the 3 branched-chain amino acids (isoleucine, leucine and valine), when grown with either C6 or C2 carbon sources. Depletion of these branched chain amino acids in the medium led to loss of viability.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000090803 | 1 – 618 | Acetolactate synthase large subunit IlvB1Add BLAST | 618 |
Proteomic databases
PaxDbi | P9WG41 |
Expressioni
Inductioni
The expression is high during the mid-exponential phase and low during the stationary phase.1 Publication
Interactioni
Subunit structurei
Heterodimer of large catalytic subunit and small regulatory subunit.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv3003c |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 30 | DisorderedSequence analysisAdd BLAST | 30 | |
Regioni | 429 – 509 | Thiamine pyrophosphate bindingAdd BLAST | 81 |
Sequence similaritiesi
Belongs to the TPP enzyme family.Curated
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
OMAi | CFGTSGP |
PhylomeDBi | P9WG41 |
Family and domain databases
CDDi | cd02015, TPP_AHAS, 1 hit |
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.
P9WG41-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSAPTKPHSP TFKPEPHSAA NEPKHPAARP KHVALQQLTG AQAVIRSLEE
60 70 80 90 100
LGVDVIFGIP GGAVLPVYDP LFDSKKLRHV LVRHEQGAGH AASGYAHVTG
110 120 130 140 150
RVGVCMATSG PGATNLVTPL ADAQMDSIPV VAITGQVGRG LIGTDAFQEA
160 170 180 190 200
DISGITMPIT KHNFLVRSGD DIPRVLAEAF HIAASGRPGA VLVDIPKDVL
210 220 230 240 250
QGQCTFSWPP RMELPGYKPN TKPHSRQVRE AAKLIAAARK PVLYVGGGVI
260 270 280 290 300
RGEATEQLRE LAELTGIPVV TTLMARGAFP DSHRQNLGMP GMHGTVAAVA
310 320 330 340 350
ALQRSDLLIA LGTRFDDRVT GKLDSFAPEA KVIHADIDPA EIGKNRHADV
360 370 380 390 400
PIVGDVKAVI TELIAMLRHH HIPGTIEMAD WWAYLNGVRK TYPLSYGPQS
410 420 430 440 450
DGSLSPEYVI EKLGEIAGPD AVFVAGVGQH QMWAAQFIRY EKPRSWLNSG
460 470 480 490 500
GLGTMGFAIP AAMGAKIALP GTEVWAIDGD GCFQMTNQEL ATCAVEGIPV
510 520 530 540 550
KVALINNGNL GMVRQWQSLF YAERYSQTDL ATHSHRIPDF VKLAEALGCV
560 570 580 590 600
GLRCEREEDV VDVINQARAI NDCPVVIDFI VGADAQVWPM VAAGTSNDEI
610
QAARGIRPLF DDITEGHA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45809.1 |
PIRi | F70855 |
RefSeqi | WP_003415168.1, NZ_NVQJ01000041.1 YP_177917.1, NC_000962.3 |
Genome annotation databases
GeneIDi | 887286 |
KEGGi | mtu:Rv3003c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45809.1 |
PIRi | F70855 |
RefSeqi | WP_003415168.1, NZ_NVQJ01000041.1 YP_177917.1, NC_000962.3 |
3D structure databases
AlphaFoldDBi | P9WG41 |
SMRi | P9WG41 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv3003c |
Proteomic databases
PaxDbi | P9WG41 |
Protocols and materials databases
DNASUi | 887286 |
Genome annotation databases
GeneIDi | 887286 |
KEGGi | mtu:Rv3003c |
Organism-specific databases
TubercuListi | Rv3003c |
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
OMAi | CFGTSGP |
PhylomeDBi | P9WG41 |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
BRENDAi | 2.2.1.6, 3445 |
Family and domain databases
CDDi | cd02015, TPP_AHAS, 1 hit |
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 | ILVB1_MYCTU | |
Accessioni | P9WG41Primary (citable) accession number: P9WG41 Secondary accession number(s): L0TCV7, O53250, P0A622 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | May 25, 2022 | |
This is version 40 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families