PHNN_PANVC
ID PHNN_PANVC Reviewed; 178 AA.
AC E1SHE4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=Pvag_1844;
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1;
RX PubMed=20952567; DOI=10.1128/jb.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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; CP002206; ADO10029.1; -; Genomic_DNA.
DR RefSeq; WP_013358333.1; NC_014562.1.
DR AlphaFoldDB; E1SHE4; -.
DR SMR; E1SHE4; -.
DR STRING; 712898.Pvag_1844; -.
DR EnsemblBacteria; ADO10029; ADO10029; Pvag_1844.
DR KEGG; pva:Pvag_1844; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_102477_0_0_6; -.
DR OMA; RLIWLTG; -.
DR OrthoDB; 1724909at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000006631; 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..178
FT /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT /id="PRO_0000412792"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00836"
SQ SEQUENCE 178 AA; 19488 MW; A16FBDB87A044AC1 CRC64;
MARLIWLTGP SGSGKDSLLD ALRAAPPPRL LIAHRYITRA ADAGGENHVA LTETEFDRRA
ALGLFAVSWE AHGFRYGIGC ETEQWLLRGQ NVVVNGSRLH LAQAQARFGS QLLPVCLQVT
PAVLAARLRQ RGREDEAEIA RRLARAAQPQ PDGCLILNND GALAETVCQL RQILELHQ