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Database: UniProt
Entry: D5GPW5_TUBMM
LinkDB: D5GPW5_TUBMM
Original site: D5GPW5_TUBMM 
ID   D5GPW5_TUBMM            Unreviewed;       325 AA.
AC   D5GPW5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE            EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN   ORFNames=GSTUM_00012078001 {ECO:0000313|EMBL:CAZ86567.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ86567.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ86567.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ86567.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:456215; EC=2.7.6.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000179};
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000256|ARBA:ARBA00006478}.
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DR   EMBL; FN430379; CAZ86567.1; -; Genomic_DNA.
DR   RefSeq; XP_002842376.1; XM_002842330.1.
DR   AlphaFoldDB; D5GPW5; -.
DR   STRING; 656061.D5GPW5; -.
DR   EnsemblFungi; CAZ86567; CAZ86567; GSTUM_00012078001.
DR   GeneID; 9182310; -.
DR   KEGG; tml:GSTUM_00012078001; -.
DR   eggNOG; KOG1448; Eukaryota.
DR   HOGENOM; CLU_033546_1_0_1; -.
DR   InParanoid; D5GPW5; -.
DR   OMA; CKMKKHR; -.
DR   OrthoDB; 276387at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:EnsemblFungi.
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:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
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   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10210:SF57; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 2.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..120
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
SQ   SEQUENCE   325 AA;  35876 MW;  C2DB26DB6B9CD3A6 CRC64;
     MRRVKIFSGT SHPGLTEAIC ERLGTTLGKC DLKKFSNGET SVDIGCSIRD QDVFIVQSGS
     AKANDSIMEL LILISACKGG SANKITAVMP YFPYSKQSKK KSHRGAITAR MLANLLTVAG
     VDHVITVDLH ASQMQGFFTK PVDNLYAEPL LARWIRHTVP NWRDSVVVSK NPGGTKRVTQ
     LADVLKLNFA LITTDRRRKE DADQIPGNEK MITLVGEVRR KTVLIVDDMI DRAGSWISAA
     EHVKLRGGAK KVICIATHGV FGGNCLKEME DCSCIDQIVV TNSFPIPEDK RKGVKKLVTI
     DLSQLLSEAI RRNHHGKFIP HYLVE
//
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