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Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (PRPP synthase) (PRPPase) (p-Rib-PP synthase)

 A0A0A3IIA4_9BACI        Unreviewed;       319 AA.
A0A0A3IIA4;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
27-SEP-2017, entry version 17.
RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583};
EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583};
AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000256|HAMAP-Rule:MF_00583};
AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=p-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
ORFNames=CD30_19445 {ECO:0000313|EMBL:KGR82558.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR82558.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR82558.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR82558.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate.
Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-
5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.
{ECO:0000256|HAMAP-Rule:MF_00583}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00583};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00583};
-!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
diphosphate from D-ribose 5-phosphate (route I): step 1/1.
{ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
family. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR82558.1}.
-----------------------------------------------------------------------
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EMBL; JPVQ01000090; KGR82558.1; -; Genomic_DNA.
RefSeq; WP_036180577.1; NZ_JPVQ01000090.1.
EnsemblBacteria; KGR82558; KGR82558; CD30_19445.
UniPathway; UPA00087; UER00172.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd06223; PRTases_typeI; 1.
HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
InterPro; IPR029099; Pribosyltran_N.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR029057; PRTase-like.
InterPro; IPR005946; Rib-P_diPkinase.
Pfam; PF14572; Pribosyl_synth; 1.
Pfam; PF13793; Pribosyltran_N; 1.
SUPFAM; SSF53271; SSF53271; 1.
TIGRFAMs; TIGR01251; ribP_PPkin; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:KGR82558.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Reference proteome {ECO:0000313|Proteomes:UP000030595};
Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000313|EMBL:KGR82558.1}.
DOMAIN 10 126 Pribosyltran_N.
{ECO:0000259|Pfam:PF13793}.
NP_BIND 43 45 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
NP_BIND 102 105 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
NP_BIND 149 150 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
REGION 200 202 Ribose-5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00583}.
REGION 227 234 Ribose-5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00583}.
REGION 313 315 Ribose-5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00583}.
METAL 134 134 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
METAL 136 136 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
METAL 145 145 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
METAL 149 149 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 110 110 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 136 136 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
BINDING 141 141 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
BINDING 177 177 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
SEQUENCE 319 AA; 35026 MW; 88B204A52CA2F71C CRC64;
MPYQYANSSL KIFSLNSNYP LAQEIAELMG VELGKSSVKH FSDGEVQISI EESIRGCDVF
IVQSTSAPVN EHLMELLIMV DAVKRASART VNVVIPYYGY ARQDRKAKAR EPITAKLVAN
LLETAGATRV IVLDLHAPQI QGFFDILIDH LMAVPLLSDY FLSKNYSPEE LVVVSPDHGG
VTRARKMAER LKAPIAIIDK RRPKPNVAEV MNIVGNIEGK VCILIDDIID TAGTITLGAN
ALKENGAKEV YACCSHPVLS GPAIERIENS PIKELIVTNT IQLPDEKRSP KVKQLSVANL
MAEAISRVYE NKSVSTLFD


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