ID D1AP39_SEBTE Unreviewed; 318 AA.
AC D1AP39;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 01-MAY-2013, entry version 27.
DE RecName: Full=Ribose-phosphate pyrophosphokinase;
DE Short=RPPK;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase;
GN Name=prs; OrderedLocusNames=Sterm_0640;
OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Sebaldella.
OX NCBI_TaxID=526218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300;
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.
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
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DR EMBL; CP001739; ACZ07513.1; -; Genomic_DNA.
DR RefSeq; YP_003307444.1; NC_013517.1.
DR ProteinModelPortal; D1AP39; -.
DR EnsemblBacteria; ACZ07513; ACZ07513; Sterm_0640.
DR GeneID; 8596124; -.
DR KEGG; str:Sterm_0640; -.
DR PATRIC; 32405212; VBISebTer81212_0661.
DR HOGENOM; HOG000210449; -.
DR KO; K00948; -.
DR OMA; YVQIQES; -.
DR UniPathway; UPA00087; UER00172.
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:HAMAP.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA: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:HAMAP.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1; -.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF00156; Pribosyltran; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW Transferase.
FT REGION 214 227 5-phosphoribose 1-diphosphate binding (By
FT similarity).
FT METAL 129 129 Magnesium (By similarity).
FT METAL 131 131 Magnesium (By similarity).
FT METAL 140 140 Magnesium (By similarity).
FT METAL 144 144 Magnesium (By similarity).
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
//
