ID E0SID1_DICD3 Unreviewed; 195 AA.
AC E0SID1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ADM97812.1};
GN OrderedLocusNames=Dda3937_04095 {ECO:0000313|EMBL:ADM97812.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM97812.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADM97812.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADM97812.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00836}.
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DR EMBL; CP002038; ADM97812.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SID1; -.
DR STRING; 198628.Dda3937_04095; -.
DR KEGG; ddd:Dda3937_04095; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_102477_0_0_6; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000006859; 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; 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 Pfam; PF13238; AAA_18; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00836, ECO:0000313|EMBL:ADM97812.1};
KW Kinase {ECO:0000313|EMBL:ADM97812.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Reference proteome {ECO:0000313|Proteomes:UP000006859};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00836, ECO:0000313|EMBL:ADM97812.1}.
FT DOMAIN 10..188
FT /note="Guanylate kinase/L-type calcium channel beta
FT subunit"
FT /evidence="ECO:0000259|SMART:SM00072"
SQ SEQUENCE 195 AA; 21516 MW; A4DA9407B9A97B0B CRC64;
MGAGTAGVLM ARLIWLTGAS GSGKDSLLDA LRQTNPARLL VAHRYITRPA QAGGENHIAL
SDAEFAYRRE CGLFALHWQA HQYQYGIGVE IDLWLSAGMD VVVNGSRSHH PQVQQRYGDR
LLPVCLQVSP AVLAQRLRQR GREDEAQIAQ RLQRASAMPV PTACRLLNND GSLAQTLLAF
HTLLAAEKRE AEKWK
//
