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Database: UniProt/TrEMBL
Entry: F4A2M9_MAHA5
LinkDB: F4A2M9_MAHA5
Original site: F4A2M9_MAHA5 
ID   F4A2M9_MAHA5            Unreviewed;       317 AA.
AC   F4A2M9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   22-JUL-2015, entry version 29.
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};
GN   Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN   OrderedLocusNames=Mahau_1011 {ECO:0000313|EMBL:AEE96209.1};
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 {ECO:0000313|EMBL:AEE96209.1, ECO:0000313|Proteomes:UP000008457};
RN   [1] {ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
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   -!- 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}.
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DR   EMBL; CP002360; AEE96209.1; -; Genomic_DNA.
DR   RefSeq; WP_013780639.1; NC_015520.1.
DR   ProteinModelPortal; F4A2M9; -.
DR   STRING; 697281.Mahau_1011; -.
DR   EnsemblBacteria; AEE96209; AEE96209; Mahau_1011.
DR   KEGG; mas:Mahau_1011; -.
DR   PATRIC; 54630663; VBIMahAus157719_1036.
DR   KO; K00948; -.
DR   OMA; PVNEHLM; -.
DR   BioCyc; MAUS697281:GH33-1045-MONOMER; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000008457; 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-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:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR   InterPro; IPR000842; PRib_PP_synth_CS.
DR   InterPro; IPR029099; Pribosyltran_N.
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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008457};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:AEE96209.1};
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:UP000008457};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000313|EMBL:AEE96209.1}.
FT   NP_BIND      41     43       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     100    103       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     147    148       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      198    200       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      225    232       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       132    132       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       134    134       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       143    143       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       147    147       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     108    108       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     134    134       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     139    139       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     175    175       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
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
//
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