ID   PHNN_DICZ5              Reviewed;         188 AA.
AC   D2C357;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=Dd586_2592;
OS   Dickeya zeae (strain Ech586) (Dickeya dadantii (strain Ech586)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya; Dickeya parazeae.
OX   NCBI_TaxID=590409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech586;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya dadantii Ech586.";
RL   Submitted (DEC-2009) 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; CP001836; ACZ77438.1; -; Genomic_DNA.
DR   RefSeq; WP_012885250.1; NC_013592.1.
DR   AlphaFoldDB; D2C357; -.
DR   SMR; D2C357; -.
DR   STRING; 590409.Dd586_2592; -.
DR   EnsemblBacteria; ACZ77438; ACZ77438; Dd586_2592.
DR   KEGG; ddc:Dd586_2592; -.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_102477_0_0_6; -.
DR   OMA; RLIWLTG; -.
DR   OrthoDB; 1724909at2; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000001446; 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; Transferase.
FT   CHAIN           1..188
FT                   /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT                   /id="PRO_0000412781"
SQ   SEQUENCE   188 AA;  21150 MW;  D4AE36885FB144CD CRC64;
     MARLIWLTGA SGSGKDTLLD ALRQTEPVRL LVAHRYITRP AQAGGENHIA LSEAEFAYRR
     EHNLFALHWQ AHQYQYGIGI EVDHWLSAGL DVVVNGSRSH HQQAQQRYGS RLLPVCLQVS
     AAVLAQRLRQ RGREDEAQIA LRLQRADAMD ILPATCRRLN NDGPLAQTLQ AFHTLLAAEK
     SDFWQISL