PHNN_ACICJ
ID PHNN_ACICJ Reviewed; 181 AA.
AC A5G2M7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Acry_2919;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ32109.1; -; Genomic_DNA.
DR RefSeq; WP_012040412.1; NC_009484.1.
DR AlphaFoldDB; A5G2M7; -.
DR SMR; A5G2M7; -.
DR STRING; 349163.Acry_2919; -.
DR EnsemblBacteria; ABQ32109; ABQ32109; Acry_2919.
DR KEGG; acr:Acry_2919; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_102477_0_0_5; -.
DR OMA; RLIWLTG; -.
DR OrthoDB; 1724909at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000000245; 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..181
FT /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT /id="PRO_0000412770"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00836"
SQ SEQUENCE 181 AA; 19252 MW; E3B93CEAE1510E09 CRC64;
MPRSGRLVLV VGPSGAGKDT VLREARRRLG HAPDIVFPRR VITRPPDPAE DHEPVSDDEF
QRRAFALSWS AHGLSYGIPA SIVGDLDAGR IVVVNVSRAI VADARRRFPC FVVAVTAAPA
ILAARLAVRR RETAAEIGAR LARAAAPVEA DAVVANETTP EAAGAAFLGI LLRCRDLPCL
P
