ID A0A285NNF8_9PSED Unreviewed; 194 AA.
AC A0A285NNF8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=SAMN05660463_01747 {ECO:0000313|EMBL:SNZ11042.1};
OS Pseudomonas sp. URIL14HWK12:I9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ11042.1, ECO:0000313|Proteomes:UP000232228};
RN [1] {ECO:0000313|EMBL:SNZ11042.1, ECO:0000313|Proteomes:UP000232228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ11042.1,
RC ECO:0000313|Proteomes:UP000232228};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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: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; OBEM01000003; SNZ11042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285NNF8; -.
DR OrthoDB; 341217at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000232228; Unassembled WGS sequence.
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 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};
KW Kinase {ECO:0000313|EMBL:SNZ11042.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Reference proteome {ECO:0000313|Proteomes:UP000232228};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT DOMAIN 3..189
FT /note="Guanylate kinase/L-type calcium channel beta
FT subunit"
FT /evidence="ECO:0000259|SMART:SM00072"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00836"
SQ SEQUENCE 194 AA; 20967 MW; 87DDB87D3D7A4ED6 CRC64;
MYSGLLVYLM GPSGSGKDSV IDAAREQLAT LGVEVVQRVI TRSAESRGER ALGATPEAFA
QMREAGAFAL CWRANELWYG IPNTIEACLA AGESVLINGS RGHLPEALAR YPDLLPIMLT
VAPGVLEERL RGRGRETDEA IESRLMRNDA LLKEPGQWQV GGVDIVRIDN SGDLAVTVRA
VVGVIDAALR RQRN
//
