ID A0A372GH07_9ACTN Unreviewed; 338 AA. AC A0A372GH07; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-NOV-2019, entry version 6. 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=D0T12_14075 {ECO:0000313|EMBL:RFS84666.1}; OS Actinomadura sp. LHW52907. OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae; OC Actinomadura; unclassified Actinomadura. OX NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS84666.1, ECO:0000313|Proteomes:UP000262882}; RN [1] {ECO:0000313|EMBL:RFS84666.1, ECO:0000313|Proteomes:UP000262882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LHW52907 {ECO:0000313|EMBL:RFS84666.1, RC ECO:0000313|Proteomes:UP000262882}; RA Li L., Lin H.W.; RT "Actinomadura spongicola sp. nov., isolated from marine sponge RT Leucetta chagosensis."; RL Submitted (AUG-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:RFS84666.1}. 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; QVNQ01000004; RFS84666.1; -; Genomic_DNA. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000262882; 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|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956731}; KW Complete proteome {ECO:0000313|Proteomes:UP000262882}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:RFS84666.1}; 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:UP000262882}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:RFS84666.1}. FT DOMAIN 24 140 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 57 59 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 116 117 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 246 250 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT ACT_SITE 214 214 {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 150 150 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 190 190 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 216 216 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 242 242 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 338 AA; 36835 MW; 1FBE989B123B32E5 CRC64; MKHVSVEGEL SEVSGIKASG QKKLMLFTGR ADPDLAREVA DNLHVELTPT SAYDFANGET FVRFLESVRG SDAFVIQSHT APINQWIMEQ LIMVDALKRA SAKRITVVAP FFGYARQDKK HRGREPISAR LMADLFKTAG ADRLITVDLH TAQIQGFFDG PVDHLFALDL LARHFESRLD TSQVTVVAPD AGRVRVTERW SDRLGGVPMA IIHKKRDPDV ANEVKVFDVV GEVEGRTCVV VDDMIDTGGT IVKAADALFD HGATRVVVAA THGVLSGPAV DRLKNSRISD VVLTNTLPIP MEKQFDKLTV LSIAPLIARA INEVFSDGSV TSLFGGHS //