ID F3KBP2_9GAMM Unreviewed; 315 AA.
AC F3KBP2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583};
DE EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583};
DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN ORFNames=imdm_1535 {ECO:0000313|EMBL:EGH00212.1};
OS gamma proteobacterium IMCC2047.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=434085 {ECO:0000313|EMBL:EGH00212.1, ECO:0000313|Proteomes:UP000004485};
RN [1] {ECO:0000313|EMBL:EGH00212.1, ECO:0000313|Proteomes:UP000004485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=imcc2047 {ECO:0000313|Proteomes:UP000004485};
RX PubMed=21602327; DOI=10.1128/JB.05226-11;
RA Kang I., Kang D., Oh H.M., Kim H., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT "Genome sequence of strain IMCC2047, a novel marine member of the
RT Gammaproteobacteria.";
RL J. Bacteriol. 193:3688-3689(2011).
CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC 5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00583};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00583};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00583};
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 I): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00583}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
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:EGH00212.1}.
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DR EMBL; AEGL01000038; EGH00212.1; -; Genomic_DNA.
DR AlphaFoldDB; F3KBP2; -.
DR PATRIC; fig|434085.3.peg.140; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000004485; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR NCBIfam; TIGR01251; ribP_PPkin; 1.
DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10210:SF119; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SMART; SM01400; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00583}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00583};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00583};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW Rule:MF_00583}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW Reference proteome {ECO:0000313|Proteomes:UP000004485};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00583}.
FT DOMAIN 6..122
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT ACT_SITE 194
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 38..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 97..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 196
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 220
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 224..228
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
SQ SEQUENCE 315 AA; 33982 MW; 4C66AE3CF76F1561 CRC64;
MAANLTIFTG NANPELAKKV VKHLSMSLGN ASVSQFSDGE TSAEIKDHVR GKDVFIIQST
CAPTNDNLME LLVMVDAVRR ASAASITAVV PYFGYARQDR RVRSVRVPIT AKVVAMMMDT
VGIDRVLTVD LHADQIQGFF NCPVDNIYGS PVLLEHITRQ RYEDMVVVSP DIGGVVRARA
LAKQLNCELA IIDKRRPKAN VSEVMNIIGD IDGKTCILID DMVDTAGTLC KAADALKVKG
ATKVVAYCTH AVLSGAAIEN ITNSTLDQLV VTDTIPLSDA ATECPSIHQL SISALLAESI
RRVRNAESIS ALFQE
//
