ID A0A3M0LPZ6_9LACO Unreviewed; 323 AA. AC A0A3M0LPZ6; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 10-APR-2019, 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=F5ESL0246_06775 {ECO:0000313|EMBL:RMC27415.1}; OS Lactobacillus sp. ESL0246. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC 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 RT symbiont 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 CC (Rib-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, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00583, CC ECO:0000256|SAAS:SAAS01115190}; 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: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00087; UER00172. DR Proteomes; UP000279155; Unassembled WGS sequence. 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; 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 ECO:0000256|SAAS:SAAS00956731}; KW Complete proteome {ECO:0000313|Proteomes:UP000279155}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:RMC27415.1}; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:RMC27415.1}. FT DOMAIN 7 123 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 40 42 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 99 100 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 226 230 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT ACT_SITE 196 196 {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 133 133 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 173 173 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 198 198 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 222 222 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT 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 //