ID A0A1S6QG22_9LACO Unreviewed; 319 AA. AC A0A1S6QG22; DT 10-MAY-2017, integrated into UniProtKB/TrEMBL. DT 10-MAY-2017, sequence version 1. DT 18-JUL-2018, entry version 8. DE RecName: Full=Putative 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=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 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: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583, CC ECO:0000256|SAAS:SAAS00956745}. 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: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CAUTION: Part of a set of proteins in which some residues CC (ACT_SITE, NP_BIND, REGION and BINDING) are not conserved. CC {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 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; 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 ECO:0000256|SAAS:SAAS00956731}; KW Complete proteome {ECO:0000313|Proteomes:UP000030361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:AQW20551.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000030361}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956753}. FT DOMAIN 10 124 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 43 45 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 136 136 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 176 176 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 225 225 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 //