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Database: UniProt
Entry: W9SW40_9PSED
LinkDB: W9SW40_9PSED
Original site: W9SW40_9PSED 
ID   W9SW40_9PSED            Unreviewed;       184 AA.
AC   W9SW40;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN {ECO:0000256|HAMAP-Rule:MF_00836};
DE            EC=2.7.4.23 {ECO:0000256|HAMAP-Rule:MF_00836};
DE   AltName: Full=Ribose 1,5-bisphosphokinase {ECO:0000256|HAMAP-Rule:MF_00836};
GN   Name=phnN {ECO:0000256|HAMAP-Rule:MF_00836,
GN   ECO:0000313|EMBL:EXF42503.1};
GN   ORFNames=BAY1663_05097 {ECO:0000313|EMBL:EXF42503.1};
OS   Pseudomonas sp. BAY1663.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF42503.1, ECO:0000313|Proteomes:UP000019475};
RN   [1] {ECO:0000313|EMBL:EXF42503.1, ECO:0000313|Proteomes:UP000019475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAY1663 {ECO:0000313|EMBL:EXF42503.1,
RC   ECO:0000313|Proteomes:UP000019475};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of Pseudomonas sp. BAY1663.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC       5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000256|HAMAP-
CC       Rule:MF_00836}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-
CC         ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:68688, ChEBI:CHEBI:456216;
CC         EC=2.7.4.23; Evidence={ECO:0000256|ARBA:ARBA00000373,
CC         ECO:0000256|HAMAP-Rule:MF_00836};
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 II): step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005069, ECO:0000256|HAMAP-Rule:MF_00836}.
CC   -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00836}.
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:EXF42503.1}.
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DR   EMBL; AZSV01000206; EXF42503.1; -; Genomic_DNA.
DR   RefSeq; WP_037045439.1; NZ_AZSV01000206.1.
DR   AlphaFoldDB; W9SW40; -.
DR   STRING; 1439940.BAY1663_05097; -.
DR   PATRIC; fig|1439940.3.peg.5052; -.
DR   eggNOG; COG3709; Bacteria.
DR   OrthoDB; 341217at2; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000019475; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019634; P:organic phosphonate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00836; PhnN; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012699; PhnN.
DR   NCBIfam; TIGR02322; phosphon_PhnN; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   PANTHER; PTHR23117:SF8; RIBOSE 1,5-BISPHOSPHATE PHOSPHOKINASE PHNN; 1.
DR   Pfam; PF13238; AAA_18; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00836, ECO:0000313|EMBL:EXF42503.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019475};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT   DOMAIN          2..181
FT                   /note="Guanylate kinase/L-type calcium channel beta
FT                   subunit"
FT                   /evidence="ECO:0000259|SMART:SM00072"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00836"
SQ   SEQUENCE   184 AA;  20133 MW;  87173229315EE4DB CRC64;
     MQGRLIYLIG PSGAGKDSLL DAARTLLAER GVRIARRVIT RSAEAVGEAA QSVSTEQFER
     MEAEQAFALS WRANGLAYGI PAQIDAWLAA GEHVLVNGSR GHLQQARARY PELLAVLLSV
     EHDVLRQRLR ARGRETHAEI EARLARNALF AGELDDYLRL DNSATLGESV ERLLALVDEH
     APCA
//
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