ID A3VEK0_9RHOB Unreviewed; 181 AA.
AC A3VEK0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 72.
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=RB2654_09719 {ECO:0000313|EMBL:EAQ13338.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ13338.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ13338.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ13338.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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:EAQ13338.1}.
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DR EMBL; AAMT01000005; EAQ13338.1; -; Genomic_DNA.
DR RefSeq; WP_008330974.1; NZ_VNHV01000001.1.
DR AlphaFoldDB; A3VEK0; -.
DR STRING; 314271.RB2654_09719; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_102477_0_0_5; -.
DR OrthoDB; 341217at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000002931; 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 PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR PANTHER; PTHR23117:SF8; RIBOSE 1,5-BISPHOSPHATE PHOSPHOKINASE 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 Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT DOMAIN 3..180
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 181 AA; 18916 MW; 9C8C2AF1E49A3866 CRC64;
MSVIGPFAVV GPSGVGKDTV MEAVQAADPS VVLVRRVITR PAEAGGEAFE GVDRAAFAAM
KAAGDFALDW EAHGLAYGIP VSIHDDLGAG RPVLFNVSRA MLAEAVKVFP GLRVLSITAT
DDVLAARLRA RGRESEDQIA QRLARAKLPL PAGLRVTEID NSGALDRAVK AVRAALQPVR
A
//
