ID   PHNN_JANMA              Reviewed;         453 AA.
AC   A6SU94;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN;
DE            EC=2.7.4.23;
DE   AltName: Full=Ribose 1,5-bisphosphokinase;
GN   Name=phnN; OrderedLocusNames=mma_0151;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC       5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000250}.
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;
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   -!- SIMILARITY: In the C-terminal section; belongs to the ribose 1,5-
CC       bisphosphokinase family. {ECO:0000305}.
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DR   EMBL; CP000269; ABR90087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6SU94; -.
DR   SMR; A6SU94; -.
DR   STRING; 375286.mma_0151; -.
DR   EnsemblBacteria; ABR90087; ABR90087; mma_0151.
DR   KEGG; mms:mma_0151; -.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_603790_0_0_4; -.
DR   OMA; RATQANE; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000006388; 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; IPR009389; DUF1045.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012699; PhnN.
DR   Pfam; PF06299; DUF1045; 1.
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..453
FT                   /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT                   /id="PRO_0000412787"
FT   REGION          1..271
FT                   /note="unknown"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..453
FT                   /note="Ribose 1,5-bisphosphokinase"
SQ   SEQUENCE   453 AA;  50253 MW;  2D8B6A0D332A5CFC CRC64;
     MHGSTGFVQG TRPAGDQADP LPVVRVSSES MTRYALYFTP VDDSPWAQAG SSWLGRHPAS
     PEPVQQVNIP GIPRILLSSL TADARRYGFH ATLKAPFRLF EGFNEEHLLQ MARAFCAAQK
     AIVLDEVRVR PLMDFLALQV NGPLDEIGGL AMRCVTYFDL LRAPLTEPEL AKRRRAGLNA
     RQSALLQRWG YPYTEEFYRF HMTLTDALMH ADADVIFTIR KAAEQHFAAA VAAVPLAIDA
     LTIAREEYPG APFVEWQRIP FSGQGERASL PHSGRIFFCV GPSGVGKDSL LNWVREHSAG
     DEKLVFAQRT ITRATQANEA HEAVDTASFW RLAAGGQFAM VWQANDLCYG IRRGIEADLK
     AGRDVVINGS RAYVPQLLQA FPDAIVIWID ASENLLRERL EARQREQGPA LLKRLKRAKE
     FAPSEQAQVI RLDNSGALEA GGQKLLDILR QAK