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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) (PRPP synthase) (PRPPase) (p-Rib-PP synthase)

 F8DGT4_STREP            Unreviewed;       318 AA.
F8DGT4;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
22-NOV-2017, entry version 41.
RecName: Full=Putative 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,
ECO:0000313|EMBL:AEH55480.1};
OrderedLocusNames=HMPREF0833_10449 {ECO:0000313|EMBL:AEH55480.1};
Streptococcus parasanguinis (strain ATCC 15912 / DSM 6778 / CIP 104372
/ LMG 14537).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=760570 {ECO:0000313|EMBL:AEH55480.1, ECO:0000313|Proteomes:UP000001502};
[1] {ECO:0000313|Proteomes:UP000001502}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15912 / DSM 6778 / CIP 104372 / LMG 14537
{ECO:0000313|Proteomes:UP000001502};
Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G.,
Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W.,
Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J.,
Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D.,
Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A.,
Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L.,
Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R.,
Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
Petrosino J., Highlander S., Gibbs R.;
"Complete sequence of Streptococcus parasanguinis strain ATCC 15912.";
Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
-!- 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 1 Mg(2+) ion 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}.
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
family. Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- CAUTION: Part of a set of proteins in which some residues
(ACT_SITE, NP_BIND, REGION and BINDING) are not conserved.
{ECO:0000256|HAMAP-Rule:MF_00583}.
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EMBL; CP002843; AEH55480.1; -; Genomic_DNA.
RefSeq; WP_003015158.1; NC_015678.1.
ProteinModelPortal; F8DGT4; -.
EnsemblBacteria; AEH55480; AEH55480; HMPREF0833_10449.
GeneID; 10834948; -.
KEGG; scp:HMPREF0833_10449; -.
KO; K00948; -.
UniPathway; UPA00087; UER00172.
Proteomes; UP000001502; 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_B; RibP_PPkinase_B; 1.
InterPro; IPR029099; Pribosyltran_N.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR029057; PRTase-like.
InterPro; IPR005946; Rib-P_diPkinase.
Pfam; PF14572; Pribosyl_synth; 1.
Pfam; PF13793; Pribosyltran_N; 1.
SUPFAM; SSF53271; SSF53271; 2.
TIGRFAMs; TIGR01251; ribP_PPkin; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Complete proteome {ECO:0000313|Proteomes:UP000001502};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:AEH55480.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000313|EMBL:AEH55480.1}.
DOMAIN 7 123 Pribosyltran_N.
{ECO:0000259|Pfam:PF13793}.
NP_BIND 40 42 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
NP_BIND 99 100 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
REGION 226 230 Ribose-5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00583}.
METAL 133 133 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 222 222 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
SEQUENCE 318 AA; 34922 MW; 4703AF0ED0610AE9 CRC64;
MSDKKNMKLF SLNSNPEIAQ KIADHAGVPL GKISSRQFSD GEIQVNIEES VRGYDIYIIQ
STSFPVNNHL MELLIMVDAC QRASANTVNV VMPYFGYARQ DRTAAPREPI TAKLVANMLV
KAGVDRVVTL DLHAVQVQGF FDIAVDNLFT IPLFAEHYIN KGLTGSDVVV VSPKNSGVKR
ARSLAEYLDA PIAIIDYEQD DANRDYGYII GDVKGKKAIL IDDILNTGKT FSEASKIVER
EGATEIYAVS SHGLFVKGAV ELLDQAPIKE ILVTDSVAPN GPTPKNINYL TASELIAEAI
VRIQERKPVS PLFAYHKK


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