UniProtKB - P9WGS9 (DPRE2_MYCTU)
Protein
Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase
Gene
dprE2
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans (PubMed:16291675, PubMed:19299584). DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX) (PubMed:22733761). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex (PubMed:25789990). DprE2 then catalyzes the second step of epimerization, the NAD+-dependent reduction of DPX that leads to the formation of DPA (PubMed:22733761, PubMed:25789990). Appears to be essential for the growth and survival of M.tuberculosis (PubMed:12657046, PubMed:24517327).1 Publication5 Publications
Miscellaneous
Was identified as a high-confidence drug target.1 Publication
Catalytic activityi
- NAD+ + trans,octa-cis-decaprenylphospho-β-D-arabinofuranose = H+ + NADH + trans,octa-cis-decaprenylphospho-β-D-erythro-pentofuranosid-2-uloseBy similarity1 PublicationEC:1.1.1.333By similarity1 Publication
: cell wall polysaccharide biosynthesis Pathwayi
This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.2 PublicationsView all proteins of this organism that are known to be involved in the pathway cell wall polysaccharide biosynthesis and in Cell wall biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 67 | NADBy similarity | 1 | |
Active sitei | 160 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Binding sitei | 164 | NADBy similarity | 1 |
GO - Molecular functioni
- oxidoreductase activity Source: UniProtKB-KW
GO - Biological processi
- arabinan biosynthetic process Source: MTBBASE
- capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
- cell wall organization Source: UniProtKB-KW
- cell wall polysaccharide biosynthetic process Source: MTBBASE
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Cell wall biogenesis/degradation |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-8087-MONOMER MTBH37RV:G185E-8087-MONOMER |
UniPathwayi | UPA00963 |
Names & Taxonomyi
Protein namesi | Recommended name: Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductaseCurated (EC:1.1.1.333By similarity1 Publication)Alternative name(s): Decaprenyl-phospho-2'-keto-D-arabinose reductaseCurated Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductaseCurated Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE21 Publication Short name: Decaprenyl-phosphoribose 2'-epimerase subunit 21 Publication NAD-dependent decaprenylphosphoryl-D-2-keto-erythropentose reductaseCurated |
Gene namesi | Name:dprE21 Publication Ordered Locus Names:Rv3791 ORF Names:MTCY13D12.25 |
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 | Rv3791 |
Subcellular locationi
- Periplasm 1 Publication
GO - Cellular componenti
- periplasmic space Source: UniProtKB-SubCell
- plasma membrane Source: MTBBASE
Keywords - Cellular componenti
PeriplasmPathology & Biotechi
Disruption phenotypei
Traditional knockout mutant with dprE2 disruption could not be achieved, suggesting this gene is essential (PubMed:24517327). Conditional knock-down mutant of dprE2 show that down-regulation of DprE2 results in growth arrest in vitro (PubMed:24517327). Cells lacking this gene display impaired growth (PubMed:12657046).2 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000054860 | 1 – 254 | Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductaseAdd BLAST | 254 |
Proteomic databases
PaxDbi | P9WGS9 |
Interactioni
Subunit structurei
Interacts with DprE1 to form an epimerase complex.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv3791 |
Family & Domainsi
Sequence similaritiesi
Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated
Phylogenomic databases
eggNOGi | ENOG4108RG3 Bacteria COG1028 LUCA |
KOi | K16652 |
OMAi | INAVGNP |
PhylomeDBi | P9WGS9 |
Family and domain databases
InterProi | View protein in InterPro IPR036291 NAD(P)-bd_dom_sf IPR020904 Sc_DH/Rdtase_CS IPR002347 SDR_fam |
Pfami | View protein in Pfam PF00106 adh_short, 1 hit |
PRINTSi | PR00081 GDHRDH |
SUPFAMi | SSF51735 SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00061 ADH_SHORT, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WGS9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVLDAVGNPQ TVLLLGGTSE IGLAICERYL HNSAARIVLA CLPDDPRRED
60 70 80 90 100
AAAAMKQAGA RSVELIDFDA LDTDSHPKMI EAAFSGGDVD VAIVAFGLLG
110 120 130 140 150
DAEELWQNQR KAVQIAEINY TAAVSVGVLL AEKMRAQGFG QIIAMSSAAG
160 170 180 190 200
ERVRRANFVY GSTKAGLDGF YLGLSEALRE YGVRVLVIRP GQVRTRMSAH
210 220 230 240 250
LKEAPLTVDK EYVANLAVTA SAKGKELVWA PAAFRYVMMV LRHIPRSIFR
KLPI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46620.1 |
PIRi | C70697 |
RefSeqi | NP_218308.1, NC_000962.3 WP_003420632.1, NZ_NVQJ01000009.1 |
Genome annotation databases
EnsemblBacteriai | CCP46620; CCP46620; Rv3791 |
GeneIDi | 886124 |
KEGGi | mtu:Rv3791 mtv:RVBD_3791 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46620.1 |
PIRi | C70697 |
RefSeqi | NP_218308.1, NC_000962.3 WP_003420632.1, NZ_NVQJ01000009.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 83332.Rv3791 |
Proteomic databases
PaxDbi | P9WGS9 |
Genome annotation databases
EnsemblBacteriai | CCP46620; CCP46620; Rv3791 |
GeneIDi | 886124 |
KEGGi | mtu:Rv3791 mtv:RVBD_3791 |
Organism-specific databases
TubercuListi | Rv3791 |
Phylogenomic databases
eggNOGi | ENOG4108RG3 Bacteria COG1028 LUCA |
KOi | K16652 |
OMAi | INAVGNP |
PhylomeDBi | P9WGS9 |
Enzyme and pathway databases
UniPathwayi | UPA00963 |
BioCyci | MetaCyc:G185E-8087-MONOMER MTBH37RV:G185E-8087-MONOMER |
Family and domain databases
InterProi | View protein in InterPro IPR036291 NAD(P)-bd_dom_sf IPR020904 Sc_DH/Rdtase_CS IPR002347 SDR_fam |
Pfami | View protein in Pfam PF00106 adh_short, 1 hit |
PRINTSi | PR00081 GDHRDH |
SUPFAMi | SSF51735 SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00061 ADH_SHORT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DPRE2_MYCTU | |
Accessioni | P9WGS9Primary (citable) accession number: P9WGS9 Secondary accession number(s): L0TGS1, P66783, P72057 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | September 18, 2019 | |
This is version 31 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
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways