ID K8PI78_9BRAD Unreviewed; 192 AA.
AC K8PI78;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF9696_00507 {ECO:0000313|EMBL:EKS42342.1};
OS Afipia clevelandensis ATCC 49720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=883079 {ECO:0000313|EMBL:EKS42342.1, ECO:0000313|Proteomes:UP000001095};
RN [1] {ECO:0000313|EMBL:EKS42342.1, ECO:0000313|Proteomes:UP000001095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49720 {ECO:0000313|EMBL:EKS42342.1,
RC ECO:0000313|Proteomes:UP000001095};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Afipia clevelandensis ATCC 49720.";
RL Submitted (APR-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKS42342.1}.
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DR EMBL; AGWY01000002; EKS42342.1; -; Genomic_DNA.
DR RefSeq; WP_002711373.1; NZ_KB375281.1.
DR AlphaFoldDB; K8PI78; -.
DR PATRIC; fig|883079.3.peg.526; -.
DR HOGENOM; CLU_102477_0_0_5; -.
DR OrthoDB; 341217at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000001095; 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:EKS42342.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT DOMAIN 17..187
FT /note="Guanylate kinase/L-type calcium channel beta
FT subunit"
FT /evidence="ECO:0000259|SMART:SM00072"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00836"
SQ SEQUENCE 192 AA; 20471 MW; 1178F968C66C6741 CRC64;
MSETVVLPDT SAGLIGPGRL ILVVGPSGAG KDTLIGLAMA ARTQDRAIVF PQRVVTREAS
SFENNEAVSA IVFGQMLGRG DFAFQWEAHG LRYGIPRTIV DDIRAGRTVV INASRTIIDF
ARRSYARVTV VAVIAPPDIL AQRVAARGRA SDGRIDDRLR RAVSSPEPDA TINNVGPADA
HAAELLKFID GV
//
