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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) (P-Rib-PP synthase) (PRPP synthase) (PRPPase)

 A0A1W9NHC7_9GAMM        Unreviewed;       317 AA.
A0A1W9NHC7;
05-JUL-2017, integrated into UniProtKB/TrEMBL.
05-JUL-2017, sequence version 1.
16-JAN-2019, entry version 8.
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=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
ORFNames=B0D94_00950 {ECO:0000313|EMBL:OQX32417.1};
Gammaproteobacteria bacterium LUC14_002_19_P1.
Bacteria; Proteobacteria; Gammaproteobacteria;
sulfur-oxidizing symbionts.
NCBI_TaxID=1940819 {ECO:0000313|EMBL:OQX32417.1};
[1] {ECO:0000313|EMBL:OQX32417.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LUC14_002_19_P1 {ECO:0000313|EMBL:OQX32417.1};
Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C.,
Campbell B.J.;
"Novel co-symbiosis in the unique lucinid bivalve Phacoides
pectinatus.";
Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the biosynthesis of the central metabolite
phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate
(Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017,
ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1;
Evidence={ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS01115190};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00583};
Note=Binds 2 Mg(2+) ions 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, ECO:0000256|SAAS:SAAS00956751}.
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
-!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
family. Class I subfamily. {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:OQX32417.1}.
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EMBL; MUHZ01000070; OQX32417.1; -; Genomic_DNA.
UniPathway; UPA00087; UER00172.
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.
InterPro; IPR037515; Rib-P_diPkinase_bac.
PANTHER; PTHR10210; PTHR10210; 1.
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,
ECO:0000256|SAAS:SAAS00956731};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:OQX32417.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS00956743};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS00956748};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS00956760};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS00956731};
Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:OQX32417.1}.
DOMAIN 6 123 Pribosyltran_N.
{ECO:0000259|Pfam:PF13793}.
NP_BIND 39 41 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
NP_BIND 98 99 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
REGION 226 230 Ribose-5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00583}.
ACT_SITE 196 196 {ECO:0000256|HAMAP-Rule:MF_00583}.
METAL 133 133 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
METAL 172 172 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 198 198 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
BINDING 222 222 Ribose-5-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00583}.
SEQUENCE 317 AA; 34212 MW; CC0E2760B24FBB24 CRC64;
MPTSGMMVFA GNANPELVAE ITGRLSIRLG KAVVGQFSDG EVMAEVQESV RGRDVYVVQS
TSQPTNDHLM ELLVLIDALR LSSAKRIVAV IPYFGYARQD RRPRSSRAPI TARLVAKQLA
AAGADQLVTV DLHADQIAGF FDIPVDNIYA LPTLLADVWR QKYSDLIVVS PDVGGVVRAR
ALAKHLDDAE LAIIDKRRPQ ANVAQVMNII GDVRGKSCVL IDDMVDTAGT LCKAAAALKE
HGAKRVVAYC THPVLSGPAV SNINQSELDE LVVSNTISLQ PDARACEKIR QISIAELVAE
TMRRIATGES VSSLFMD


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