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UniProtKB - P9WG39 (ILVG_MYCTU)
Protein
Acetolactate synthase large subunit IlvG
Gene
ilvG
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.
1 PublicationCatalytic 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
Kineticsi
- KM=11.89 mM for pyruvate1 Publication
- Vmax=1.39 µmol/min/mg enzyme1 Publication
pH dependencei
Optimum pH is between 6 and 7.1 Publication
Temperature dependencei
Optimum temperature is between 35 and 40 degrees Celsius.1 Publication
: 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 | 57 | Thiamine pyrophosphateBy similarity | 1 | |
Binding sitei | 159 | FADBy similarity | 1 | |
Metal bindingi | 439 | MagnesiumBy similarity | 1 | |
Metal bindingi | 466 | MagnesiumBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 299 – 318 | 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: UniProtKB
- valine biosynthetic process Source: UniProtKB
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 IlvG (EC:2.2.1.6)Short name: ALS Alternative name(s): Acetohydroxy-acid synthase large subunit Short name: AHAS |
Gene namesi | Name:ilvG Ordered Locus Names:Rv1820 ORF Names:MTCY1A11.23c |
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 | Rv1820 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000090805 | 2 – 547 | Acetolactate synthase large subunit IlvGAdd BLAST | 546 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | P9WG39 |
PTM databases
iPTMneti | P9WG39 |
Expressioni
Inductioni
The expression is almost identical during the mid-exponential and extended stationary phase.1 Publication
Interactioni
Subunit structurei
Heterodimer of large catalytic subunit and small regulatory subunit.
By similarityProtein-protein interaction databases
STRINGi | 83332.Rv1820 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 388 – 468 | Thiamine pyrophosphate bindingAdd BLAST | 81 |
Sequence similaritiesi
Belongs to the TPP enzyme family.Curated
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
OMAi | PGPYGCL |
PhylomeDBi | P9WG39 |
Family and domain databases
InterProi | View protein in InterPro 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 |
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
P9WG39-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTDTAPAQT MHAGRLIARR LKASGIDTVF TLSGGHLFSI YDGCREEGIR
60 70 80 90 100
LIDTRHEQTA AFAAEGWSKV TRVPGVAALT AGPGITNGMS AMAAAQQNQS
110 120 130 140 150
PLVVLGGRAP ALRWGMGSLQ EIDHVPFVAP VARFAATAQS AENAGLLVDQ
160 170 180 190 200
ALQAAVSAPS GVAFVDFPMD HAFSMSSDNG RPGALTELPA GPTPAGDALD
210 220 230 240 250
RAAGLLSTAQ RPVIMAGTNV WWGHAEAALL RLVEERHIPV LMNGMARGVV
260 270 280 290 300
PADHRLAFSR ARSKALGEAD VALIVGVPMD FRLGFGGVFG STTQLIVADR
310 320 330 340 350
VEPAREHPRP VAAGLYGDLT ATLSALAGSG GTDHQGWIEE LATAETMARD
360 370 380 390 400
LEKAELVDDR IPLHPMRVYA ELAALLERDA LVVIDAGDFG SYAGRMIDSY
410 420 430 440 450
LPGCWLDSGP FGCLGSGPGY ALAAKLARPQ RQVVLLQGDG AFGFSGMEWD
460 470 480 490 500
TLVRHNVAVV SVIGNNGIWG LEKHPMEALY GYSVVAELRP GTRYDEVVRA
510 520 530 540
LGGHGELVSV PAELRPALER AFASGLPAVV NVLTDPSVAY PRRSNLA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44586.1 |
PIRi | E70720 |
RefSeqi | NP_216336.1, NC_000962.3 WP_003409218.1, NZ_NVQJ01000013.1 |
Genome annotation databases
GeneIDi | 885738 |
KEGGi | mtu:Rv1820 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44586.1 |
PIRi | E70720 |
RefSeqi | NP_216336.1, NC_000962.3 WP_003409218.1, NZ_NVQJ01000013.1 |
3D structure databases
AlphaFoldDBi | P9WG39 |
SMRi | P9WG39 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1820 |
PTM databases
iPTMneti | P9WG39 |
Proteomic databases
PaxDbi | P9WG39 |
Protocols and materials databases
DNASUi | 885738 |
Genome annotation databases
GeneIDi | 885738 |
KEGGi | mtu:Rv1820 |
Organism-specific databases
TubercuListi | Rv1820 |
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
OMAi | PGPYGCL |
PhylomeDBi | P9WG39 |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
BRENDAi | 2.2.1.6, 3445 |
Family and domain databases
InterProi | View protein in InterPro 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 |
PROSITEi | View protein in PROSITE PS00187, TPP_ENZYMES, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ILVG_MYCTU | |
Accessioni | P9WG39Primary (citable) accession number: P9WG39 Secondary accession number(s): L0T9C7, P66946, Q50613 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | May 25, 2022 | |
This is version 44 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