ID D6GSL8_FILAD Unreviewed; 319 AA.
AC D6GSL8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 01-MAY-2013, entry version 22.
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=HMPREF0389_00576;
OS Filifactor alocis (strain ATCC 35896 / D40 B5) (Fusobacterium alocis).
OC Bacteria; Firmicutes; Clostridia; Clostridiales;
OC Peptostreptococcaceae; Filifactor.
OX NCBI_TaxID=546269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35896 / D40 B5;
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Izard J., Blanton J.M., Baranova O.V.,
RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL Submitted (DEC-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; CP002390; EFE28659.1; -; Genomic_DNA.
DR RefSeq; YP_005054716.1; NC_016630.1.
DR ProteinModelPortal; D6GSL8; -.
DR EnsemblBacteria; EFE28659; EFE28659; HMPREF0389_00576.
DR GeneID; 11570642; -.
DR KEGG; faa:HMPREF0389_00576; -.
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 215 228 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 319 AA; 34894 MW; F8977FB863DEEE2E CRC64;
MNIRGNEIKI FSGNSNITLA QKIADGLGVP LGEAQVKKFS DGEISININE SVRGADTYIV
QSTCDPVNDN LMELLIMIDA LKRASAGRIT AVIPYYGYAR QDRKAKSRDP ITAKLVADLI
EAAGADRVLT MDLHANQIQG YFDIPVDHLL GGPILVDYFA KKQIEDLVVV SPDHGSVKRV
RAVAEKLDIP MAIVDKRRPK ANISEVMNII GDVKDKNILL IDDMIDTAGT LVNAAEAIRK
MGGKEIYASC THPVFSGPAI QRLKDSCIKE IVILDTIALP KEKEMDKIRV ISSAPLFAKA
IYKTFNNESL SILFESTEG
//
