ID A0A0K6GR57_9BACI Unreviewed; 316 AA. AC A0A0K6GR57; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 06-JUL-2016, entry version 6. 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}; GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583}; GN ORFNames=Ga0061060_11933 {ECO:0000313|EMBL:CUA81016.1}; OS Anoxybacillus suryakundensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=1325335 {ECO:0000313|EMBL:CUA81016.1}; RN [1] {ECO:0000313|EMBL:CUA81016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 27374 {ECO:0000313|EMBL:CUA81016.1}; RA Rikkerink E.H.A., Fineran P.C.; RT "Complete DNA Sequence of Pseudomonas syringae pv. actinidiae, the RT Causal Agent of Kiwifruit Canker Disease."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. CC Catalyzes the transfer of pyrophosphoryl group from ATP to ribose- CC 5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. CC {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion 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}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {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; CYGZ01000019; CUA81016.1; -; Genomic_DNA. DR RefSeq; WP_035021116.1; NZ_LIOK01000019.1. DR UniPathway; UPA00087; UER00172. 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-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. 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-HAMAP. 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; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:CUA81016.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583}. FT DOMAIN 9 125 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 42 44 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 101 104 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 148 149 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 197 199 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 224 231 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 310 312 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 133 133 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 135 135 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 144 144 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 148 148 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 109 109 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 135 135 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 140 140 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 174 174 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 316 AA; 34621 MW; D930D586903E8440 CRC64; MSQYLNSNLK LFSLNSNPIL AQEIAKVIGV ELGKCSVSRF SDGEIQINIE ESIRGCDVYV IQSTSAPVNE HLMELLIMID ALKRASAKTI NIVMPYYGYA RQDRKARSRE PITAKLVANL LETAGASRVI TLDLHAPQIQ GFFDIPIDHL MGVPILADYF KEKQLDDIVI VSPDHGGVTR ARKMADRLKA PIAIIDKRRP KPNVAEVMNI IGNVQGKTTI LVDDIIDTAG TITLAANALA EHGAKEVYAC CTHPVLSGPA IERIQNSKIK ELVVTNTIAI PEEKKTNKIV ELSVAPLIGE AIIRVHEEQS ISALFD //