ID A0A1S6QG22_9LACO Unreviewed; 319 AA. AC A0A1S6QG22; DT 10-MAY-2017, integrated into UniProtKB/TrEMBL. DT 10-MAY-2017, sequence version 1. DT 27-SEP-2017, entry version 5. 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=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583}; DE Short=p-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583}; GN ORFNames=PL11_000665 {ECO:0000313|EMBL:AQW20551.1}; OS Lactobacillus curieae. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW20551.1, ECO:0000313|Proteomes:UP000030361}; RN [1] {ECO:0000313|EMBL:AQW20551.1, ECO:0000313|Proteomes:UP000030361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW20551.1, RC ECO:0000313|Proteomes:UP000030361}; RX PubMed=26021929; RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.; RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel RT Producer of Gamma-aminobutyric Acid."; RL Genome Announc. 3:0-0(2015). 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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; CP018906; AQW20551.1; -; Genomic_DNA. DR RefSeq; WP_035168532.1; NZ_CP018906.1. DR KEGG; lcu:PL11_000665; -. DR KO; K00948; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000030361; 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: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 Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 2. 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 Complete proteome {ECO:0000313|Proteomes:UP000030361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:AQW20551.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000030361}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583}. FT DOMAIN 10 124 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 43 45 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 102 105 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 149 150 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 312 314 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 134 134 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 136 136 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 145 145 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 149 149 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 110 110 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 136 136 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 141 141 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 176 176 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 319 AA; 35070 MW; 2C01405877E7925F CRC64; MTDDNTRPNI KLFSLNSNRE LAEKISKAVG VPLGKATTKK FSDDEIKISV DESIRGTEVY VIQSISDPVN TNLMELLIMV DALRRASAGS INVVIPYYGY SRADRKARSR EPITAKLLSS FLEMDGVDRV VTLDLHADQI QGFFDIPVDH LRAARLLAKF FESKHGKDDL VIISPDHASV SRARTFAELL DAPIAIIDNR SPEDANTIPE SVIGDVEGKR AVVVDDMIDT AIKTQIASET LKKAGASEVY AVATHAIFSG DAVKRLEEAP IKNVIVTDSI KLSDEHKFDK LELVSVDKLF GEAINLIHNQ QSVGKLFGR //