ID   A0A372GH07_9ACTN        Unreviewed;       338 AA.
AC   A0A372GH07;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-FEB-2019, entry version 4.
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=D0T12_14075 {ECO:0000313|EMBL:RFS84666.1};
OS   Actinomadura sp. LHW52907.
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Actinomadura.
OX   NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS84666.1, ECO:0000313|Proteomes:UP000262882};
RN   [1] {ECO:0000313|EMBL:RFS84666.1, ECO:0000313|Proteomes:UP000262882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW52907 {ECO:0000313|EMBL:RFS84666.1,
RC   ECO:0000313|Proteomes:UP000262882};
RA   Li L., Lin H.W.;
RT   "Actinomadura spongicola sp. nov., isolated from marine sponge
RT   Leucetta chagosensis.";
RL   Submitted (AUG-2018) 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
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RFS84666.1}.
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DR   EMBL; QVNQ01000004; RFS84666.1; -; Genomic_DNA.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000262882; Unassembled WGS sequence.
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   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:UP000262882};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:RFS84666.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:RFS84666.1}.
FT   DOMAIN       24    140       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      57     59       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     116    117       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      246    250       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   ACT_SITE    214    214       {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       150    150       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       190    190       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     216    216       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     242    242       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   338 AA;  36835 MW;  1FBE989B123B32E5 CRC64;
     MKHVSVEGEL SEVSGIKASG QKKLMLFTGR ADPDLAREVA DNLHVELTPT SAYDFANGET
     FVRFLESVRG SDAFVIQSHT APINQWIMEQ LIMVDALKRA SAKRITVVAP FFGYARQDKK
     HRGREPISAR LMADLFKTAG ADRLITVDLH TAQIQGFFDG PVDHLFALDL LARHFESRLD
     TSQVTVVAPD AGRVRVTERW SDRLGGVPMA IIHKKRDPDV ANEVKVFDVV GEVEGRTCVV
     VDDMIDTGGT IVKAADALFD HGATRVVVAA THGVLSGPAV DRLKNSRISD VVLTNTLPIP
     MEKQFDKLTV LSIAPLIARA INEVFSDGSV TSLFGGHS
//