ID A0A7X6HM55_9CYAN Unreviewed; 329 AA. AC A0A7X6HM55; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. 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}. 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; JAAUVD010000106; NJK67431.1; -; Genomic_DNA. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000534992; Unassembled WGS sequence. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 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 //