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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)

 A9NE81_ACHLI            Unreviewed;       321 AA.
A9NE81;
05-FEB-2008, integrated into UniProtKB/TrEMBL.
05-FEB-2008, sequence version 1.
22-NOV-2017, entry version 77.
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=prsA {ECO:0000313|EMBL:ABX80661.1};
Synonyms=prs {ECO:0000256|HAMAP-Rule:MF_00583};
OrderedLocusNames=ACL_0018 {ECO:0000313|EMBL:ABX80661.1};
Acholeplasma laidlawii (strain PG-8A).
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX80661.1, ECO:0000313|Proteomes:UP000008558};
[1] {ECO:0000313|EMBL:ABX80661.1, ECO:0000313|Proteomes:UP000008558}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PG-8A {ECO:0000313|EMBL:ABX80661.1,
ECO:0000313|Proteomes:UP000008558};
PubMed=21784942; DOI=10.1128/JB.05059-11;
Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M.,
Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y.,
Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S.,
Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N.,
Rogov S.I., Alexeev D.G., Ladygina V.G., Govorun V.M.;
"Complete genome and proteome of Acholeplasma laidlawii.";
J. Bacteriol. 193:4943-4953(2011).
-!- 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: 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 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}.
-!- 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}.
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EMBL; CP000896; ABX80661.1; -; Genomic_DNA.
RefSeq; WP_012241992.1; NC_010163.1.
ProteinModelPortal; A9NE81; -.
STRING; 441768.ACL_0018; -.
EnsemblBacteria; ABX80661; ABX80661; ACL_0018.
KEGG; acl:ACL_0018; -.
eggNOG; ENOG4105C5T; Bacteria.
eggNOG; COG0462; LUCA.
HOGENOM; HOG000210449; -.
KO; K00948; -.
OMA; FGWARQD; -.
OrthoDB; POG091H018X; -.
UniPathway; UPA00087; UER00172.
Proteomes; UP000008558; Chromosome.
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; IPR000842; PRib_PP_synth_CS.
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.
PROSITE; PS00114; PRPP_SYNTHASE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
Complete proteome {ECO:0000313|Proteomes:UP000008558};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:ABX80661.1};
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:UP000008558};
Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
ECO:0000313|EMBL:ABX80661.1}.
DOMAIN 9 124 Pribosyltran_N.
{ECO:0000259|Pfam:PF13793}.
NP_BIND 41 43 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
NP_BIND 100 101 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 134 134 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00583}.
METAL 173 173 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 321 AA; 34915 MW; 6F9A99448FF6222F CRC64;
MTIDEKKAKL FTLSANKPLA EKIAKSAGIP LSNVEVIRFA DGEITVNIEE SVRGNHVFVI
QPTSEPANDH LMEVLVLTDA LKRASAASIT IIMPYFGYSR QDRKVKSRQP ITAKLVANLL
TVAGVDRVVS IDLHAAQIQG FFDIPIDNFP AAPTLASYFR RKKLENVVVV SPDHGGVTRA
RVFASFFNAP LAIIDKRRPE PNKAEVMNII GDVKGATCIM IDDIIDTGGT LMAGANALKE
AGAKEVYAAA THGVLTSNAT ERLQNSVINE IVITDTIYLD PAKNQPKLKQ LSIGALLGEA
IIHILQDEPI SQIFNRIQED Q


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