(data stored in ACNUC7421 zone)

SWISSPROT: D4YXS4_SPHJU

ID   D4YXS4_SPHJU            Unreviewed;       311 AA.
AC   D4YXS4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 49.
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 {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=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=p-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
GN   Name=prsA {ECO:0000313|EMBL:BAI95156.1};
GN   Synonyms=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN   OrderedLocusNames=SJA_C1-03220 {ECO:0000313|EMBL:BAI95156.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95156.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95156.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate.
CC       Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-
CC       5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.
CC       {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC       alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00583};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00583};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}.
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DR   EMBL; AP010803; BAI95156.1; -; Genomic_DNA.
DR   RefSeq; WP_013038943.1; NC_014006.1.
DR   ProteinModelPortal; D4YXS4; -.
DR   STRING; 452662.SJA_C1-03220; -.
DR   EnsemblBacteria; BAI95156; BAI95156; SJA_C1-03220.
DR   GeneID; 29272024; -.
DR   KEGG; sjp:SJA_C1-03220; -.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; FGWARQD; -.
DR   OrthoDB; POG091H018X; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd06223; PRTases_typeI; 1.
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   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXS4.
DR   SWISS-2DPAGE; D4YXS4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:BAI95156.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000313|EMBL:BAI95156.1}.
FT   DOMAIN        1    117       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      34     36       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND      93     96       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      191    193       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      218    225       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      305    307       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       125    125       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       127    127       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       136    136       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       140    140       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     101    101       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     127    127       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     132    132       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     167    167       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   311 AA;  33142 MW;  0073B4611B087FC8 CRC64;
     MKLMTGNSNK PLAAAIADYI EIPLTDASVR RFADEEVFVE IHENVRGEDV FVIQSTSYPT
     NDNLMELLIM IDALKRASAK RITAVVPYFG YARQDRKPGP RTPISAKLVA NLITTAGANR
     VLSVDLHAGQ IQGFFDIPTD NLFGAPVMSA DIQARFGDRN LMVVSPDVGG VVRARALAKR
     LDNAPLAIVD KRRERAGESE VMNIIGDVKG RFCVLIDDIV DSAGTLCNAA GALKAAGAEE
     VVAYVSHGVL SGGAVARVEA SELKELVITD SIQGTDAVCG ASSIRHLPIA PLLGEAIKRI
     ADESSVSSLF D
//

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