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Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase)

 B7R2K6_9EURY            Unreviewed;       279 AA.
B7R2K6;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
18-JUL-2018, entry version 53.
RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583};
EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583};
AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000256|HAMAP-Rule:MF_00583};
AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
ORFNames=TAM4_93 {ECO:0000313|EMBL:EEB73805.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB73805.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB73805.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB73805.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- FUNCTION: Involved in the biosynthesis of the central metabolite
phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate
(Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00583};
Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_00583};
-!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
diphosphate from D-ribose 5-phosphate (route I): step 1/1.
{ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
family. Class III (archaeal) subfamily. {ECO:0000256|HAMAP-
Rule:MF_00583}.
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EMBL; CP002952; EEB73805.1; -; Genomic_DNA.
RefSeq; WP_014122613.1; NC_016051.1.
ProteinModelPortal; B7R2K6; -.
STRING; 246969.TAM4_93; -.
EnsemblBacteria; EEB73805; EEB73805; TAM4_93.
GeneID; 7419599; -.
KEGG; tha:TAM4_93; -.
eggNOG; arCOG00067; Archaea.
eggNOG; COG0462; LUCA.
KO; K00948; -.
OrthoDB; POG093Z079F; -.
BioCyc; TSP246969:G1GNJ-1482-MONOMER; -.
UniPathway; UPA00087; UER00172.
Proteomes; UP000009277; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd06223; PRTases_typeI; 1.
HAMAP; MF_00583_A; RibP_PPkinase_A; 1.
InterPro; IPR029099; Pribosyltran_N.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR029057; PRTase-like.
InterPro; IPR005946; Rib-P_diPkinase.
InterPro; IPR037514; Rib-P_diPkinase_arc.
PANTHER; PTHR10210; PTHR10210; 1.
Pfam; PF00156; Pribosyltran; 1.
Pfam; PF13793; Pribosyltran_N; 1.
SUPFAM; SSF53271; SSF53271; 1.
TIGRFAMs; TIGR01251; ribP_PPkin; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Complete proteome {ECO:0000313|Proteomes:UP000009277};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:EEB73805.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|RuleBase:RU004324};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000313|EMBL:EEB73805.1}.
DOMAIN 17 109 Pribosyltran_N.
{ECO:0000259|Pfam:PF13793}.
DOMAIN 142 242 Pribosyltran. {ECO:0000259|Pfam:PF00156}.
NP_BIND 32 34 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
NP_BIND 89 90 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
REGION 213 217 Ribose-5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00583}.
ACT_SITE 183 183 {ECO:0000256|HAMAP-Rule:MF_00583}.
METAL 122 122 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00583}.
METAL 160 160 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 185 185 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 209 209 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
SEQUENCE 279 AA; 30695 MW; 940375779A136C3D CRC64;
MFVIGSGGRH LEGELRKLGG DVLEVELRKF PDGEKYVRVL GSGKEATVVS STFAPQDEKI
VELILIGDAL RERGFERLRA VVPYFAYSRQ DRVTKEGEPI SVRAVMKALG LYYDELYVFD
LHNPETLRYF PGKGVNVSPA GIIADYFREK LGEGIVLAPD RGALGRAKAV AMELGLEYSH
FEKRRISPTE VEMRPVEVDV KGKNVLIVDD IISTGGTMIK AARILRKLGA EKIFVGVTHG
VFAQGAVERV SDAVDELAVT NTIPTPVSKI SIVPEILRL


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