PHNN_FRAIE
ID PHNN_FRAIE Reviewed; 190 AA.
AC E3J0E1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=FraEuI1c_3563;
OS Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298654;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45817 / CECT 9037 / EuI1c;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Beauchemin N., Sen A.,
RA Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT "Complete sequence of Frankia sp. EuI1c.";
RL Submitted (OCT-2010) 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; CP002299; ADP81570.1; -; Genomic_DNA.
DR RefSeq; WP_013424688.1; NC_014666.1.
DR AlphaFoldDB; E3J0E1; -.
DR SMR; E3J0E1; -.
DR STRING; 298654.FraEuI1c_3563; -.
DR EnsemblBacteria; ADP81570; ADP81570; FraEuI1c_3563.
DR KEGG; fri:FraEuI1c_3563; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_102477_0_0_11; -.
DR OMA; RLIWLTG; -.
DR OrthoDB; 1724909at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000002484; 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..190
FT /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT /id="PRO_0000412786"
FT REGION 135..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 190 AA; 20107 MW; 3416DC1624487BF0 CRC64;
MTERIGPGAF VAVVGASGVG KDALMAYARE RSEAVAHFPR RVITRPSGPG EDHEPVTEEQ
FTAARERGEL AVWWPAHGLR YGIPASADVA VGAGRVVVAN VSRAVLDELA GRYQRLVVVR
VTVSDEVRAQ RLRARGREPE PGIGQRLARP DPAPGHQADT VIQNDGTLAD GGDQLLRVIL
DAAGAPLATG
