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PHNN_RHIE6
ID   PHNN_RHIE6              Reviewed;         197 AA.
AC   B3PXI8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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};
GN   OrderedLocusNames=RHECIAT_CH0000198;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) 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; CP001074; ACE89194.1; -; Genomic_DNA.
DR   RefSeq; WP_004677184.1; NC_010994.1.
DR   AlphaFoldDB; B3PXI8; -.
DR   EnsemblBacteria; ACE89194; ACE89194; RHECIAT_CH0000198.
DR   GeneID; 45955578; -.
DR   KEGG; rec:RHECIAT_CH0000198; -.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_102477_0_0_5; -.
DR   OMA; RLIWLTG; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000008817; 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; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012699; PhnN.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02322; phosphon_PhnN; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..197
FT                   /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT                   /id="PRO_0000412797"
FT   BINDING         21..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00836"
SQ   SEQUENCE   197 AA;  21102 MW;  9929467E725A853C CRC64;
     MTHEPHPGAG AERGIMVVVV GPSGAGKDTL MNLAARHFSG RADVHFTRRV ITRHRGAGGE
     DHLSVSLQGF AAMEQSGSFA VWWEAHGLKY GIPAEVSVAL SKGHIVVANG SRSALHRFQA
     AFPRLKVINV TASAEVLAGR LEARGRETHE DIMARLARGP LTVRGDYDVT ELDNSGSIEE
     AEQKMIAILD GLLAEVH
 
 
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