ID A0A7C2XAG2_9DELT Unreviewed; 315 AA. AC A0A7C2XAG2; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 10-FEB-2021, 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=ENN98_06335 {ECO:0000313|EMBL:HET98295.1}; OS Desulfurivibrio alkaliphilus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfurivibrio. OX NCBI_TaxID=427923 {ECO:0000313|EMBL:HET98295.1}; RN [1] {ECO:0000313|EMBL:HET98295.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SpSt-1224 {ECO:0000313|EMBL:HET98295.1}; RX PubMed=31911466; RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.; RT "Genome- and Community-Level Interaction Insights into Carbon Utilization RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal RT Sediment."; RL mSystems 5:e00795-19(2020). 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:HET98295.1}. 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; DSDS01000142; HET98295.1; -; Genomic_DNA. DR UniPathway; UPA00087; UER00172. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 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; 2. 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:HET98295.1}; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00583}. FT DOMAIN 6..122 FT /note="Pribosyltran_N" FT /evidence="ECO:0000259|Pfam:PF13793" FT NP_BIND 39..41 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT NP_BIND 98..99 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT REGION 225..229 FT /note="Ribose-5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT ACT_SITE 195 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 132 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 172 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 197 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 221 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" SQ SEQUENCE 315 AA; 34224 MW; 97BA0E1FB92BA88A CRC64; MAVNEMKIFA GNANPALAES ICAHLNTPLS KAEVRRFSDG EIFVEIGENV RGRDVFVIQP TCPPVNDHLM ELMIIVDALR RASARRITAV LPYYGYARQD RKVAPRVPIT AKVVAEMLMV VGVRRVLTMD LHAGQIQGFF NIPVDNLFAA PVLLDYLTHQ VDVSRVVMVS PDAGGVERTR AFAKRLNASL AIVDKRRERA NECEAMSVIG DVKGKVAVLL DDMVDTAGTL CSAANVLIDS GATEVIACCS HGVLSGPAIE RLEKSRIKNL VITDSVPLRG GARECAKIKV LSVNKLLAEA IRRIHSEDSV SSLFV //