ID   PHNN_SALAR              Reviewed;         184 AA.
AC   A9MGI9;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN {ECO:0000255|HAMAP-Rule:MF_00836};
DE            EC=2.7.4.23 {ECO:0000255|HAMAP-Rule:MF_00836};
DE   AltName: Full=Ribose 1,5-bisphosphokinase {ECO:0000255|HAMAP-Rule:MF_00836};
GN   Name=phnN {ECO:0000255|HAMAP-Rule:MF_00836}; OrderedLocusNames=SARI_03381;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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:0000255|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:0000255|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. {ECO:0000255|HAMAP-
CC       Rule:MF_00836}.
CC   -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00836}.
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DR   EMBL; CP000880; ABX23213.1; -; Genomic_DNA.
DR   RefSeq; WP_000517227.1; NC_010067.1.
DR   AlphaFoldDB; A9MGI9; -.
DR   SMR; A9MGI9; -.
DR   STRING; 41514.SARI_03381; -.
DR   EnsemblBacteria; ABX23213; ABX23213; SARI_03381.
DR   KEGG; ses:SARI_03381; -.
DR   HOGENOM; CLU_102477_0_0_6; -.
DR   OMA; RLIWLTG; -.
DR   OrthoDB; 1724909at2; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000002084; Chromosome.
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; -; 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   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02322; phosphon_PhnN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..184
FT                   /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT                   /id="PRO_0000412799"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00836"
SQ   SEQUENCE   184 AA;  20708 MW;  04E09AB32FDB7DB5 CRC64;
     MGKLIWLMGP SGSGKDSLLA ELRQQEHEQL LIAHRYITRA ANAGNENHIA LSQQEFFIRA
     KQNLLALSWY ANGFYYGLGI EIDLWLHAGF DVVVNGSRAH LSQAQARYGT SLLPVCLTVS
     PDILRQRLQT RGRENDAEIA ARLERAAHYP PFNCHTVNND GSLLQSVERL LILMGRKEEH
     YASL