ID   A0A0B5DCU6_9ACTN        Unreviewed;       324 AA.
AC   A0A0B5DCU6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 34.
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=CP978_14585 {ECO:0000313|EMBL:QEV39618.1}, SNOD_14265
GN   {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).
RN   [3] {ECO:0000313|EMBL:QEV39618.1, ECO:0000313|Proteomes:UP000325763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV39618.1,
RC   ECO:0000313|Proteomes:UP000325763};
RA   Lee N., Cho B.-K.;
RT   "Streptomyces genome completion.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 (Rib-
CC       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, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00583};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-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-ribose
CC       1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC       D-ribose 5-phosphate (route I): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00583}.
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 family.
CC       Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
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DR   EMBL; CP009313; AJE41079.1; -; Genomic_DNA.
DR   EMBL; CP023747; QEV39618.1; -; Genomic_DNA.
DR   RefSeq; WP_043440995.1; NZ_CP023747.1.
DR   STRING; 40318.SNOD_14265; -.
DR   EnsemblBacteria; AJE41079; AJE41079; SNOD_14265.
DR   KEGG; snq:CP978_14585; -.
DR   HOGENOM; CLU_033546_2_0_11; -.
DR   OrthoDB; 1011035at2; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000031526; Chromosome.
DR   Proteomes; UP000325763; 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: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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00583}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00583};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00583};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW   Rule:MF_00583}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00583}.
FT   DOMAIN          13..128
FT                   /note="Pribosyltran_N"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   NP_BIND         45..47
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   NP_BIND         104..105
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   REGION          233..237
FT                   /note="Ribose-5-phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   METAL           138
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   METAL           178
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   BINDING         203
FT                   /note="Ribose-5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   BINDING         229
FT                   /note="Ribose-5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-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
//