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PHNN_AGRFC
ID   PHNN_AGRFC              Reviewed;         183 AA.
AC   A9CKM5;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-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}; Synonyms=gmk;
GN   OrderedLocusNames=Atu0168; ORFNames=AGR_C_277;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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; AE007869; AAK85987.2; -; Genomic_DNA.
DR   RefSeq; NP_353202.2; NC_003062.2.
DR   AlphaFoldDB; A9CKM5; -.
DR   SMR; A9CKM5; -.
DR   STRING; 176299.Atu0168; -.
DR   EnsemblBacteria; AAK85987; AAK85987; Atu0168.
DR   KEGG; atu:Atu0168; -.
DR   PATRIC; fig|176299.10.peg.158; -.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_102477_0_0_5; -.
DR   OMA; RLIWLTG; -.
DR   PhylomeDB; A9CKM5; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000000813; Chromosome circular.
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; Reference proteome; Transferase.
FT   CHAIN           1..183
FT                   /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT                   /id="PRO_0000412771"
FT   BINDING         6..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00836"
SQ   SEQUENCE   183 AA;  19645 MW;  9A33D9597D4C3FE1 CRC64;
     MIVIVGPSGA GKDTLMDYAA AQLSGRPGFH FTRRVITRSC DAGGENHDAV SMHEFNQLED
     AGAFAVSWQA HGLKYGIPAA VYRHLEAGDV VIANGSRSAL PHFGTAFSRL KVVNIVARPD
     VLARRLEQRG RESRDDILRR LERSSLAVAG DFDVTTVDNS GAIEDAGKTI MQVLQQSAGS
     SQP
 
 
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