ID   A0A0B5DCU6_9ACTN        Unreviewed;       324 AA.
AC   A0A0B5DCU6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   13-NOV-2019, entry version 24.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583};
DE            EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583};
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000256|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
GN   Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN   ORFNames=SNOD_14265 {ECO:0000313|EMBL:AJE41079.1};
OS   Streptomyces nodosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE41079.1, ECO:0000313|Proteomes:UP000031526};
RN   [1] {ECO:0000313|Proteomes:UP000031526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA   Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT   "Sequence of the Streptomyces nodosus genome.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJE41079.1, ECO:0000313|Proteomes:UP000031526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE41079.1,
RC   ECO:0000313|Proteomes:UP000031526};
RX   PubMed=26497174;
RA   Sweeney P., Murphy C.D., Caffrey P.;
RT   "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT   antibiotic production.";
RL   Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
CC   -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC       phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC       pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate
CC       (Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00583,
CC         ECO:0000256|SAAS:SAAS01115190};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00583};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00583};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS00956751}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family. Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP009313; AJE41079.1; -; Genomic_DNA.
DR   RefSeq; WP_043440995.1; NZ_CP009313.1.
DR   EnsemblBacteria; AJE41079; AJE41079; SNOD_14265.
DR   OrthoDB; 1011035at2; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000031526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR   InterPro; IPR000842; PRib_PP_synth_CS.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   InterPro; IPR037515; Rib-P_diPkinase_bac.
DR   PANTHER; PTHR10210; PTHR10210; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956731};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031526};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:AJE41079.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956743};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956748};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956760};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956754};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:AJE41079.1}.
FT   DOMAIN       13    128       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      45     47       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     104    105       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      233    237       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   ACT_SITE    201    201       {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       138    138       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       178    178       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     203    203       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     229    229       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   324 AA;  35335 MW;  F6C3AA3D4A3D8104 CRC64;
     MTGIKTTGQK KLMFFSGRAH PELAEEVAQQ LGVGVVPTKA FDFANGEIYV RYQESARGAD
     CFLIQSHTAP INKWIMEQLI MIDALKRASA RSITVIVPFY GYARQDKKHR GREPISARLI
     ADLMKTAGAD RILTVDLHTD QIQGFFDGPV DHLFALPLLA DYVGQKVDRA KLTVVSPDAG
     RVRVADRWCD RLGAPLAIVH KRRDKDVANQ VTVHEVVGEV KGRVCVLVDD MIDTGGTICA
     AADALFAHGA EDVIVTATHG VLSGPAADRL KNSKVSEFVF TDTLPTPGEL DLDKITVLSI
     APTIARAVRE VFEDGSVTSL FDEQ
//