ID A0A3M0LPZ6_9LACO Unreviewed; 323 AA. AC A0A3M0LPZ6; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 07-APR-2021, entry version 9. 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=F5ESL0246_06775 {ECO:0000313|EMBL:RMC27415.1}; OS Lactobacillus sp. ESL0246. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus; unclassified Lactobacillus. OX NCBI_TaxID=2069359 {ECO:0000313|EMBL:RMC27415.1, ECO:0000313|Proteomes:UP000279155}; RN [1] {ECO:0000313|EMBL:RMC27415.1, ECO:0000313|Proteomes:UP000279155} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESL0246 {ECO:0000313|EMBL:RMC27415.1, RC ECO:0000313|Proteomes:UP000279155}; RA Ellegaard K.M., Brochet S., Bonilla-Rosso G., Emery O., Glover N., RA Hadadi N., Jaron K.S., Van Der Meer J.R., Sentchilo V., Tagini F., RA Sage Class S., Engel P.; RT "Genomic changes underlying host specialization in the bee gut symbiont RT Lactobacillus Firm5."; RL Submitted (OCT-2018) 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: 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:RMC27415.1}. 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; REHC01000012; RMC27415.1; -; Genomic_DNA. DR EnsemblBacteria; RMC27415; RMC27415; F5ESL0246_06775. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000279155; 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 ECO:0000313|EMBL:RMC27415.1}; 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, ECO:0000313|EMBL:RMC27415.1}. FT DOMAIN 7..123 FT /note="Pribosyltran_N" FT /evidence="ECO:0000259|Pfam:PF13793" FT NP_BIND 40..42 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT NP_BIND 99..100 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT REGION 226..230 FT /note="Ribose-5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT ACT_SITE 196 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 133 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 173 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 198 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 222 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" SQ SEQUENCE 323 AA; 35361 MW; 37D10B9A6BF3A37A CRC64; MSYKDNMMLF ALNSNLPLAE KIAERVGVAL SKSSVQRFSD GEIQINIDES VRGKDVYLIQ SLSVPVNDNL MELLIMIDAV RRASAQTINI VIPYYGYARQ DRKTRPREPI TAKLVADMLQ EAGATRVLSL DLHAPQIQGF FDIPVDNLMG APLLADYFLC NHLEKDAVVV SPDHGGVTRA RKLAEFLGTS IAIVDKRRPR ANVAEVMNII GDVKGKRAII IDDMIDTAGT ITLAAQALID AGATEVYASA THAVLSGPAI ERLNASPIKN LVLTDSINQP EEKKLDKTLL VSVGSLMGDA IKCIQKNEPL SPLFNTRYQE NKH //