ID A0A1S6QG22_9LACO Unreviewed; 319 AA. AC A0A1S6QG22; DT 10-MAY-2017, integrated into UniProtKB/TrEMBL. DT 10-MAY-2017, sequence version 1. DT 05-FEB-2025, entry version 33. 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 synthase {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 Lentilactobacillus curieae. OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lentilactobacillus. 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 (Rib- CC 5-P). {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribose 5-phosphate + ATP = 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:ARBA00049535, 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CAUTION: Part of a set of proteins in which some residues (ACT_SITE, CC NP_BIND, REGION and BINDING) are not conserved. {ECO:0000256|HAMAP- CC 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 AlphaFoldDB; A0A1S6QG22; -. DR KEGG; lcu:PL11_000665; -. DR eggNOG; COG0462; Bacteria. DR OrthoDB; 9777067at2; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000030361; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:TreeGrafter. 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-UniRule. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro. DR CDD; cd06223; PRTases_typeI; 1. DR FunFam; 3.40.50.2020:FF:000001; Ribose-phosphate pyrophosphokinase; 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 NCBIfam; TIGR01251; ribP_PPkin; 1. DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1. DR PANTHER; PTHR10210:SF41; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1, CHLOROPLASTIC; 1. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SMART; SM01400; Pribosyltran_N; 1. DR SUPFAM; SSF53271; PRTase-like; 2. 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 Magnesium {ECO:0000256|ARBA:ARBA00022842, 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 Reference proteome {ECO:0000313|Proteomes:UP000030361}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00583}. FT DOMAIN 10..126 FT /note="Ribose-phosphate pyrophosphokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF13793" FT BINDING 43..45 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 136 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 225 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-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 //