ID   A0A7X6HM55_9CYAN        Unreviewed;       329 AA.
AC   A0A7X6HM55;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   19-JAN-2022, entry version 3.
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=HC941_13600 {ECO:0000313|EMBL:NJK67431.1};
OS   Microcoleus sp. SU_5_3.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Microcoleus; unclassified Microcoleus.
OX   NCBI_TaxID=2720482 {ECO:0000313|EMBL:NJK67431.1, ECO:0000313|Proteomes:UP000534992};
RN   [1] {ECO:0000313|EMBL:NJK67431.1, ECO:0000313|Proteomes:UP000534992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SU_5_3 {ECO:0000313|EMBL:NJK67431.1};
RA   Waterworth S.C., Isemonger E.W., Rees E.R., Dorrington R.A., Kwan J.C.;
RT   "Conserved bacterial genomes from two geographically distinct peritidal
RT   stromatolite formations shed light on potential functional guilds.";
RL   Submitted (MAR-2020) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000179, 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NJK67431.1}.
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DR   EMBL; JAAUVD010000106; NJK67431.1; -; Genomic_DNA.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000534992; 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   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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00583}.
FT   DOMAIN          21..137
FT                   /note="Pribosyltran_N"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   NP_BIND         54..56
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   REGION          240..244
FT                   /note="Ribose-5-phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   METAL           147
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   METAL           186
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   BINDING         212
FT                   /note="Ribose-5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT   BINDING         236
FT                   /note="Ribose-5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
SQ   SEQUENCE   329 AA;  35953 MW;  BB40538803E3F858 CRC64;
     MRSAALPISL PEPPISAHDR LRLFSGSANV PLAQEVAGYL GIDLGPMVRK RFADGELYVQ
     IQESIRGCDV YLIQPTCCPV NDRLMELLIM IDACRRASAR QITAVIPYYG YARADRKTAG
     RESITAKLVA NLITKAGAGR VLAMDLHSAQ IQGYFDIPFD HVYGSPILLD YLKSKQLSDI
     VVVSPDVGGV ARARAFAKKL NDAPLAIIDK RRQAHNVAEV MNLIGDVKGK TAVLVDDMID
     TAGTISEGAR LLRREGARQV YACATHAVFS PPAIERLSSG VLEEVIVTNT IPVPEENRFE
     QLTVLSVANL LGETIWRIHE DSSVSSMFR
//