ID F4A2M9_MAHA5 Unreviewed; 317 AA.
AC F4A2M9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 03-APR-2013, entry version 13.
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=Mahau_1011;
OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX NCBI_TaxID=697281;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H.,
RA Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Mahella australiensis DSM 15567.";
RL Submitted (NOV-2010) 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; CP002360; AEE96209.1; -; Genomic_DNA.
DR RefSeq; YP_004463031.1; NC_015520.1.
DR EnsemblBacteria; AEE96209; AEE96209; Mahau_1011.
DR GeneID; 10607761; -.
DR KEGG; mas:Mahau_1011; -.
DR PATRIC; 54630663; VBIMahAus157719_1036.
DR KO; K00948; -.
DR BioCyc; MAUS697281:GH33-1045-MONOMER; -.
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 217 230 5-phosphoribose 1-diphosphate binding (By
FT similarity).
FT METAL 132 132 Magnesium (By similarity).
FT METAL 134 134 Magnesium (By similarity).
FT METAL 143 143 Magnesium (By similarity).
FT METAL 147 147 Magnesium (By similarity).
SQ SEQUENCE 317 AA; 34335 MW; B5D305DB38FA115C CRC64;
MMSRSTNIKI FTGNANPILA KEIADHIGVP MGDCLVTTFS DGEISVNFFE TVRGFDVFII
QPTCAPVNNN LMELLIMIDA CKRASAGMIT AVVPYYGYAR QDRKAKARDP ITAKLVADLL
SKAGADRVLT MDLHAAQIQG FFDIPVDHLL GVPILAQYFL ERDFAGDDLV VVSPDLGSVT
RARGFAHKLD APLAIIDKRR PKANVAEVMN IIGDVKGKRT ILIDDLVDTA GTLVEGAAAL
VNNGAKEVYA CATHGVLSGP AIERLQNSAI KELVITNTIP LLPEKQLDKI KVLSVAPLFS
EAIERIYEHL PVSVLFD
//
