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Database: UniProt/TrEMBL
Entry: D1AP39_SEBTE
LinkDB: D1AP39_SEBTE
Original site: D1AP39_SEBTE 
ID   D1AP39_SEBTE            Unreviewed;       318 AA.
AC   D1AP39;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   28-FEB-2018, entry version 61.
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=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=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN   OrderedLocusNames=Sterm_0640 {ECO:0000313|EMBL:ACZ07513.1};
OS   Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Sebaldella.
OX   NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ07513.1, ECO:0000313|Proteomes:UP000000845};
RN   [1] {ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.;
RT   "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ07513.1, ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX   PubMed=21304705;
RA   Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M.,
RA   Beck B., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Chen F.;
RT   "Complete genome sequence of Sebaldella termitidis type strain
RT   (NCTC 11300).";
RL   Stand. Genomic Sci. 2:220-227(2010).
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
CC       (Rib-5-P). {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       ECO:0000256|SAAS:SAAS00956745}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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-
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, ECO:0000256|SAAS:SAAS00956751}.
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
CC       family. Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
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DR   EMBL; CP001739; ACZ07513.1; -; Genomic_DNA.
DR   RefSeq; WP_012860109.1; NC_013517.1.
DR   ProteinModelPortal; D1AP39; -.
DR   STRING; 526218.Sterm_0640; -.
DR   EnsemblBacteria; ACZ07513; ACZ07513; Sterm_0640.
DR   KEGG; str:Sterm_0640; -.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; PYARMDK; -.
DR   OrthoDB; POG091H018X; -.
DR   BioCyc; STER526218:G1GG4-630-MONOMER; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000000845; 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: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-UniRule.
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   InterPro; IPR037515; Rib-P_diPkinase_bac.
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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956731};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000845};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:ACZ07513.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956743};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956748};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956760};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956754};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000845};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:ACZ07513.1}.
FT   DOMAIN        6    121       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      38     40       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND      97     98       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      225    229       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   ACT_SITE    195    195       {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       131    131       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       172    172       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     197    197       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     221    221       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   318 AA;  34890 MW;  34C1739032C98909 CRC64;
     MEKDFQIYAG SSSKALARQI AQKLGVELGS VDLIKFADGE TFAKVNQSVR GCMVFIVQST
     SKPVNESIME LLIFMDSLKR ASAAEIIPVI PYYGYARQDR KASPREPITS KLIADILTVA
     GASRVVTMDL HARQIQGFFD IPVDHMEALP ILAKYFIKNE LVGDDIVVVS PDVGGVKRAR
     SLAKWLHAPL AIIDKRRAKA NVSEVMNIIG DVAGKKAILI DDMIDTAGTI CNAAYALKEK
     GATEVFACAT HAILSDPAVE RLKAAPFNKV IVTDTIELPD NKRFENLEIL STDTMFSETI
     KRIVNDQAIS DLFELPHE
//
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