We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback.
Take me to UniProt BETA
UniProtKB - O53554 (ILVX_MYCTU)
Protein
Putative acetolactate synthase large subunit IlvX
Gene
ilvX
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.
By similarityMiscellaneous
Was identified as a high-confidence drug target.
Catalytic activityi
- EC:2.2.1.6
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
: 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 | 48 | Thiamine pyrophosphateBy similarity | 1 | |
Metal bindingi | 407 | MagnesiumBy similarity | 1 | |
Metal bindingi | 434 | MagnesiumBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 249 – 269 | FADBy similarityAdd BLAST | 21 | |
Nucleotide bindingi | 283 – 302 | FADBy similarityAdd BLAST | 20 |
GO - Molecular functioni
- acetolactate synthase activity Source: GO_Central
- flavin adenine dinucleotide binding Source: GO_Central
- metal ion binding Source: UniProtKB-KW
- thiamine pyrophosphate binding Source: InterPro
GO - Biological processi
- 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: Putative acetolactate synthase large subunit IlvX (EC:2.2.1.6)Short name: ALS Alternative name(s): Acetohydroxy-acid synthase large subunit Short name: AHAS |
Gene namesi | Name:ilvX Ordered Locus Names:Rv3509c |
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 | Rv3509c |
Subcellular locationi
Cell Wall
- cell wall Source: MTBBASE
Extracellular region or secreted
- extracellular region Source: MTBBASE
Plasma Membrane
- plasma membrane Source: MTBBASE
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000396953 | 1 – 515 | Putative acetolactate synthase large subunit IlvXAdd BLAST | 515 |
Proteomic databases
PaxDbi | O53554 |
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.
By similarityProtein-protein interaction databases
STRINGi | 83332.Rv3509c |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 357 – 436 | Thiamine pyrophosphate bindingBy similarityAdd BLAST | 80 |
Sequence similaritiesi
Belongs to the TPP enzyme family.Curated
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
InParanoidi | O53554 |
OMAi | DFRHEEP |
PhylomeDBi | O53554 |
Family and domain databases
InterProi | View protein in InterPro IPR029061, THDP-binding IPR012001, Thiamin_PyroP_enz_TPP-bd_dom IPR045229, TPP_enz IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR18968, PTHR18968, 2 hits |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits |
i Sequence
Sequence statusi: Complete.
O53554-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNGAQALINT LVDGGVDVCF ANPGTSEMHF VAALDAVPRM RGMLTLFEGV
60 70 80 90 100
ATGAADGYAR IAGRPAAVLL HLGPGLGNGL ANLHNARRAR VPMVVVVGDH
110 120 130 140 150
ATYHKKYDAP LESDIDAVAG TVSGWVRRTE AAADVGADAE AAIAASRSGS
160 170 180 190 200
QIATLILPAD VCWSDGAHAA AGVPAQAAAA PVDVGPVAGV LRSGEPAMML
210 220 230 240 250
IGGDATRGPG LTAAARIVQA TGARWLCETF PTCLERGAGI PAVERLAYFA
260 270 280 290 300
EGAAAQLDGV KHLVLAGARS PVSFFAYPGM PSDLVPAGCE VHVLAEPGGA
310 320 330 340 350
ADALAALADE VAPGTVAPVA GASRPQLPTG DLTSVSAADV VGALLPERAI
360 370 380 390 400
VVDESNTCGV LLPQATAGAP AHDWLTLTGG AIGYGIPAAV GAAVAAPDRP
410 420 430 440 450
VLCLESDGSA MYTISGLWSQ ARENLDVTTV IYNNGAYDIL RIELQRVGAG
460 470 480 490 500
SDPGPKALDL LDISRPTMDF VKIAEGMGVP ARRVTTCEEF ADALRAAFAE
510
PGPHLIDVVV PSLVG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46331.1 |
PIRi | G70806 |
RefSeqi | NP_218026.1, NC_000962.3 WP_003900872.1, NZ_NVQJ01000085.1 |
Genome annotation databases
GeneIDi | 888267 |
KEGGi | mtu:Rv3509c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46331.1 |
PIRi | G70806 |
RefSeqi | NP_218026.1, NC_000962.3 WP_003900872.1, NZ_NVQJ01000085.1 |
3D structure databases
AlphaFoldDBi | O53554 |
SMRi | O53554 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv3509c |
Proteomic databases
PaxDbi | O53554 |
Protocols and materials databases
DNASUi | 888267 |
Genome annotation databases
GeneIDi | 888267 |
KEGGi | mtu:Rv3509c |
Organism-specific databases
TubercuListi | Rv3509c |
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
InParanoidi | O53554 |
OMAi | DFRHEEP |
PhylomeDBi | O53554 |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
BRENDAi | 2.2.1.6, 3445 |
Family and domain databases
InterProi | View protein in InterPro IPR029061, THDP-binding IPR012001, Thiamin_PyroP_enz_TPP-bd_dom IPR045229, TPP_enz IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR18968, PTHR18968, 2 hits |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ILVX_MYCTU | |
Accessioni | O53554Primary (citable) accession number: O53554 Secondary accession number(s): L0TFM4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 10, 2010 |
Last sequence update: | June 1, 1998 | |
Last modified: | May 25, 2022 | |
This is version 111 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