ID A0A0B8N8J7_9NOCA Unreviewed; 326 AA.
AC A0A0B8N8J7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=prpS {ECO:0000313|EMBL:APA95734.1};
GN Synonyms=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN ORFNames=NS07_v2contig00067-0029 {ECO:0000313|EMBL:GAM48195.1},
GN NS506_01664 {ECO:0000313|EMBL:APA95734.1};
OS Nocardia seriolae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM48195.1, ECO:0000313|Proteomes:UP000019401};
RN [1] {ECO:0000313|EMBL:GAM48195.1, ECO:0000313|Proteomes:UP000019401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N-2927 {ECO:0000313|EMBL:GAM48195.1,
RC ECO:0000313|Proteomes:UP000019401};
RA Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA Oshima S.;
RT "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT quinqueradiata) in Kochi Prefecture, Japan.";
RL Genome Announc. 3:e00082-15(2015).
RN [2] {ECO:0000313|EMBL:APA95734.1, ECO:0000313|Proteomes:UP000180166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM150506 {ECO:0000313|EMBL:APA95734.1,
RC ECO:0000313|Proteomes:UP000180166};
RA Han H.-J.;
RT "Genome sequence of Nocardia seriolae strain EM150506, isolated from
RT Anguila japonica.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP017839; APA95734.1; -; Genomic_DNA.
DR EMBL; BAWD02000067; GAM48195.1; -; Genomic_DNA.
DR RefSeq; WP_033088778.1; NZ_RCNK01000060.1.
DR STRING; 37332.NS506_01664; -.
DR GeneID; 61151395; -.
DR KEGG; nsr:NS506_01664; -.
DR PATRIC; fig|37332.12.peg.1699; -.
DR OrthoDB; 9777067at2; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000019401; Unassembled WGS sequence.
DR Proteomes; UP000180166; Chromosome.
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:UP000019401};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00583}.
FT DOMAIN 12..128
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT ACT_SITE 202
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 45..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 104..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 204
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 230
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 234..238
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
SQ SEQUENCE 326 AA; 35389 MW; 8EAC0978EE788144 CRC64;
MTAFSTDNQK NLMLFSGRAH PELAEAVAKE LNVHVTPQTA RDFANGETFV RFEESVRGSD
AFVLQSFPAP LNQWVMEHLI MIDALKRGSA KRITSVLPFY PYARQDKKHR GREPISARLI
ADLLKTAGAD RIITIDLHTD QIQGFFDGPV DHMHAQVQLA EHIRNNYDLH NITVVSPDAG
RVKVAEKWAN SLADAPMAFI HKTRDPLVPN QTVSNRVVGE VEGRTCILID DMIDTGGTIA
GAVKVLKEAG AGDVVIAATH GILSAPAAER LASCGAKEGV VTNTLPIDES KKFPTLTVLS
IAPLLAQTIR EVFENGSVTG LFNGNA
//
