UniProtKB - P9WKE3 (KPRS_MYCTU)
Protein
Ribose-phosphate pyrophosphokinase
Gene
prs
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) and of the decaprenylphosphoryl-arabinose (DPA), an essential precursor for the mycobacterial cell wall biosynthesis. Catalyzes the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P) to yield phosphoribosyl diphosphate (PRPP) and AMP. It can also use GTP, CTP and UTP as diphosphoryl donors (PubMed:22745722).3 Publications
Catalytic activityi
- ATP + D-ribose 5-phosphate = 5-phospho-α-D-ribose 1-diphosphate + AMP + H+UniRule annotation3 PublicationsEC:2.7.6.1UniRule annotation3 Publications
Cofactori
Mg2+UniRule annotation2 PublicationsNote: Binds 2 Mg2+ ions per subunit (Potential). Can also use Mn2+ (PubMed:21085589, PubMed:21045009).UniRule annotation2 Publications
Activity regulationi
Activated by inorganic phosphate, and to a lesser extent by sulfate ions (PubMed:21085589, PubMed:21045009). In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:21085589, PubMed:21045009). Strongly inhibited by ADP and GDP through competitive binding at the activation site and at a specific allosteric site (PubMed:21085589, PubMed:21045009, PubMed:22745722). Competitively inhibited by Ca2+, Cu2+ and Fe2+ (PubMed:21085589, PubMed:21045009).3 Publications
Kineticsi
Kcat is 37 sec(-1) with Rib-5-P as substrate (PubMed:21085589). Kcat is 0.83 sec(-1) with Rib-5-P as substrate (PubMed:22745722). Kcat is 0.66 sec(-1) with ATP as substrate (PubMed:22745722). Kcat is 0.155 sec(-1) with UTP as substrate (PubMed:22745722). Kcat is 0.140 sec(-1) with GTP as substrate (PubMed:22745722). Kcat is 0.065 sec(-1) with CTP as substrate (PubMed:22745722).2 Publications
- KM=8.2 µM for Rib-5-P1 Publication
- KM=14 µM for Rib-5-P1 Publication
- KM=25 µM for ATP1 Publication
- KM=26 µM for CTP1 Publication
- KM=37 µM for GTP1 Publication
- KM=52 µM for UTP1 Publication
- KM=70 µM for Rib-5-P (without divalent cation)1 Publication
- Vmax=601 µmol/min/mg enzyme with ATP as substrate1 Publication
- Vmax=530 µmol/min/mg enzyme with Rib-5-P as substrate1 Publication
- Vmax=1.41 µmol/min/mg enzyme with Rib-5-P as substrate1 Publication
- Vmax=1.12 µmol/min/mg enzyme with ATP as substrate1 Publication
- Vmax=0.264 µmol/min/mg enzyme with UTP as substrate1 Publication
- Vmax=0.237 µmol/min/mg enzyme with GTP as substrate1 Publication
- Vmax=0.237 µmol/min/mg enzyme with CTP as substrate1 Publication
pH dependencei
Optimum pH is close to 8 (PubMed:21085589). Activities at pH 7 and pH 9.5 are 57% and 70% of the maximal activity, respectively (PubMed:21085589, PubMed:21045009).2 Publications
Temperature dependencei
Thermostable.1 Publication
: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).UniRule annotation1 PublicationProteins known to be involved in this subpathway in this organism are:
- Ribose-phosphate pyrophosphokinase (prs)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.
Pathwayi: cell wall polysaccharide biosynthesis
This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.1 PublicationView 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 |
---|---|---|---|---|
Metal bindingi | 138 | Magnesium 1UniRule annotation | 1 | |
Metal bindingi | 178 | Magnesium 2UniRule annotation | 1 | |
Active sitei | 202 | UniRule annotation | 1 | |
Binding sitei | 204 | Ribose-5-phosphateUniRule annotation | 1 | |
Binding sitei | 230 | Ribose-5-phosphateUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 45 – 47 | ATPUniRule annotation | 3 | |
Nucleotide bindingi | 104 – 105 | ATPUniRule annotation | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- kinase activity Source: UniProtKB-KW
- magnesium ion binding Source: MTBBASE
- manganese ion binding Source: MTBBASE
- ribose phosphate diphosphokinase activity Source: MTBBASE
GO - Biological processi
- 5-phosphoribose 1-diphosphate biosynthetic process Source: MTBBASE
- capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
- cell wall organization Source: UniProtKB-KW
- nucleoside metabolic process Source: InterPro
- nucleotide biosynthetic process Source: GO_Central
- purine nucleotide biosynthetic process Source: GO_Central
- ribonucleoside monophosphate biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Allosteric enzyme, Kinase, Transferase |
Biological process | Cell wall biogenesis/degradation, Nucleotide biosynthesis |
Ligand | ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
UniPathwayi | UPA00087;UER00172 UPA00963 |
Names & Taxonomyi
Protein namesi | Recommended name: Ribose-phosphate pyrophosphokinaseUniRule annotation (EC:2.7.6.1UniRule annotation3 Publications)Short name: RPPKUniRule annotation Alternative name(s): 5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation Phosphoribosyl diphosphate synthaseUniRule annotation Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation Short name: P-Rib-PP synthaseUniRule annotation Short name: PRPP synthase1 PublicationUniRule annotation Short name: PRPPase1 PublicationUniRule annotation |
Gene namesi | Name:prsUniRule annotation Synonyms:prsA1 Publication Ordered Locus Names:Rv1017c ORF Names:MTCY10G2.32 |
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 | Rv1017c |
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cell wall Source: MTBBASE
- cytoplasm Source: GO_Central
- plasma membrane Source: MTBBASE
- ribose phosphate diphosphokinase complex Source: GO_Central
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000141164 | 1 – 326 | Ribose-phosphate pyrophosphokinaseAdd BLAST | 326 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 29 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication |
Keywords - PTMi
Isopeptide bond, Ubl conjugationProteomic databases
PaxDbi | P9WKE3 |
Interactioni
Subunit structurei
Homohexamer.
1 Publication2 PublicationsProtein-protein interaction databases
STRINGi | 83332.Rv1017c |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 234 – 238 | Ribose-5-phosphate bindingUniRule annotation | 5 |
Sequence similaritiesi
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.1 PublicationUniRule annotation
Phylogenomic databases
eggNOGi | COG0462, Bacteria |
OMAi | FGWARQD |
PhylomeDBi | P9WKE3 |
Family and domain databases
CDDi | cd06223, PRTases_typeI, 1 hit |
Gene3Di | 3.40.50.2020, 2 hits |
HAMAPi | MF_00583_B, RibP_PPkinase_B, 1 hit |
InterProi | View protein in InterPro IPR000842, PRib_PP_synth_CS IPR029099, Pribosyltran_N IPR000836, PRibTrfase_dom IPR029057, PRTase-like IPR005946, Rib-P_diPkinase IPR037515, Rib-P_diPkinase_bac |
PANTHERi | PTHR10210, PTHR10210, 1 hit |
Pfami | View protein in Pfam PF14572, Pribosyl_synth, 1 hit PF13793, Pribosyltran_N, 1 hit |
SUPFAMi | SSF53271, SSF53271, 1 hit |
TIGRFAMsi | TIGR01251, ribP_PPkin, 1 hit |
PROSITEi | View protein in PROSITE PS00114, PRPP_SYNTHASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WKE3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSHDWTDNRK NLMLFAGRAH PELAEQVAKE LDVHVTSQDA REFANGEIFV
60 70 80 90 100
RFHESVRGCD AFVLQSCPAP VNRWLMEQLI MIDALKRGSA KRITAVMPFY
110 120 130 140 150
PYARQDKKHR GREPISARLI ADLLKTAGAD RIVTVDLHTD QIQGFFDGPV
160 170 180 190 200
DHMRGQNLLT GYIRDNYPDG NMVVVSPDSG RVRIAEKWAD ALGGVPLAFI
210 220 230 240 250
HKTRDPRVPN QVVSNRVVGD VAGRTCVLID DMIDTGGTIA GAVALLHNDG
260 270 280 290 300
AGDVIIAATH GVLSDPAAQR LASCGAREVI VTNTLPIGED KRFPQLTVLS
310 320
IAPLLASTIR AVFENGSVTG LFDGDA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43767.1 |
PIRi | D70622 |
RefSeqi | NP_215533.1, NC_000962.3 WP_003405263.1, NZ_NVQJ01000018.1 |
Genome annotation databases
EnsemblBacteriai | CCP43767; CCP43767; Rv1017c |
GeneIDi | 23492851 885993 |
KEGGi | mtu:Rv1017c mtv:RVBD_1017c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43767.1 |
PIRi | D70622 |
RefSeqi | NP_215533.1, NC_000962.3 WP_003405263.1, NZ_NVQJ01000018.1 |
3D structure databases
SMRi | P9WKE3 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1017c |
Proteomic databases
PaxDbi | P9WKE3 |
Genome annotation databases
EnsemblBacteriai | CCP43767; CCP43767; Rv1017c |
GeneIDi | 23492851 885993 |
KEGGi | mtu:Rv1017c mtv:RVBD_1017c |
Organism-specific databases
TubercuListi | Rv1017c |
Phylogenomic databases
eggNOGi | COG0462, Bacteria |
OMAi | FGWARQD |
PhylomeDBi | P9WKE3 |
Enzyme and pathway databases
UniPathwayi | UPA00087;UER00172 UPA00963 |
Family and domain databases
CDDi | cd06223, PRTases_typeI, 1 hit |
Gene3Di | 3.40.50.2020, 2 hits |
HAMAPi | MF_00583_B, RibP_PPkinase_B, 1 hit |
InterProi | View protein in InterPro IPR000842, PRib_PP_synth_CS IPR029099, Pribosyltran_N IPR000836, PRibTrfase_dom IPR029057, PRTase-like IPR005946, Rib-P_diPkinase IPR037515, Rib-P_diPkinase_bac |
PANTHERi | PTHR10210, PTHR10210, 1 hit |
Pfami | View protein in Pfam PF14572, Pribosyl_synth, 1 hit PF13793, Pribosyltran_N, 1 hit |
SUPFAMi | SSF53271, SSF53271, 1 hit |
TIGRFAMsi | TIGR01251, ribP_PPkin, 1 hit |
PROSITEi | View protein in PROSITE PS00114, PRPP_SYNTHASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | KPRS_MYCTU | |
Accessioni | P9WKE3Primary (citable) accession number: P9WKE3 Secondary accession number(s): L0T8D7, P65232, P96383 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 38 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