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Database: UniProt
Entry: A5ENP0_BRASB
LinkDB: A5ENP0_BRASB
Original site: A5ENP0_BRASB 
ID   A5ENP0_BRASB            Unreviewed;       214 AA.
AC   A5ENP0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN {ECO:0000256|HAMAP-Rule:MF_00836};
DE            EC=2.7.4.23 {ECO:0000256|HAMAP-Rule:MF_00836};
DE   AltName: Full=Ribose 1,5-bisphosphokinase {ECO:0000256|HAMAP-Rule:MF_00836};
GN   Name=phnN {ECO:0000256|HAMAP-Rule:MF_00836,
GN   ECO:0000313|EMBL:ABQ37784.1};
GN   OrderedLocusNames=BBta_5841 {ECO:0000313|EMBL:ABQ37784.1};
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ37784.1, ECO:0000313|Proteomes:UP000000246};
RN   [1] {ECO:0000313|EMBL:ABQ37784.1, ECO:0000313|Proteomes:UP000000246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC       5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000256|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:0000256|ARBA:ARBA00000373,
CC         ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00005069, ECO:0000256|HAMAP-Rule:MF_00836}.
CC   -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00836}.
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DR   EMBL; CP000494; ABQ37784.1; -; Genomic_DNA.
DR   RefSeq; WP_012045743.1; NC_009485.1.
DR   AlphaFoldDB; A5ENP0; -.
DR   STRING; 288000.BBta_5841; -.
DR   KEGG; bbt:BBta_5841; -.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_102477_0_0_5; -.
DR   OrthoDB; 341217at2; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000000246; 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; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR02322; phosphon_PhnN; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   PANTHER; PTHR23117:SF8; RIBOSE 1,5-BISPHOSPHATE PHOSPHOKINASE PHNN; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00836, ECO:0000313|EMBL:ABQ37784.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT   DOMAIN          18..192
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          195..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         25..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00836"
SQ   SEQUENCE   214 AA;  22875 MW;  5D0CE24F44FC16C5 CRC64;
     MSEAAAVAQD LREKLGPGRL VLVVGPSGAG KDTLLNVARR DCAGDDRVVF PQRIVTRAAS
     AFEDNLEMSA AGFREALDAG QFALHWDAHG HGYGVPRSIN DDILAGRTVV VNVSRTVIAA
     ARRSYAHVIV VTITAPPDVL AERLGKRHRP SDGDISERLH RAVNDDDVAA DVTIVNVGDP
     EPHGHRLTQI IRGPREATPV EATEGGSHVG HHHD
//
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