ID G4USH8_NEUT9 Unreviewed; 412 AA.
AC G4USH8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN ORFNames=NEUTE2DRAFT_158936 {ECO:0000313|EMBL:EGZ70554.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ70554.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ70554.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891247; EGZ70554.1; -; Genomic_DNA.
DR AlphaFoldDB; G4USH8; -.
DR STRING; 510952.G4USH8; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_0_1_1; -.
DR OMA; MMLVGDI; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:UniProt.
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:UniProt.
DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:UniProt.
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:SF36; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 5; 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, ECO:0000313|EMBL:EGZ70554.1};
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:UP000008513};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..102
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
SQ SEQUENCE 412 AA; 44766 MW; 90C08F3C45917997 CRC64;
MVRNIVVLGG NSHPELVESI CGILGLPACS RILTKFSSGE SRCEIQDSVR GKDVYIIQTG
FGGNGSRLND HFMDLCIMIS ACKTGSARRV TAVLPLFPYS RQPDLPYNKA GAPLYKAPTP
NGENGKNQYT FDSVPPTPGP GVPKTSGLTN SSDIANQMIK NALTNGSSKE QYTTHDYENL
SIVNGFQAKP GYKQWVAQAG TLVANLLTCA GCDHVITMDL HDPQVQGFFD IPVDNLYGQP
LLKRYIQQHI PNWRDAVIIS PDAGGAKRAT AIADSLGMEF ALIHKERRPT KITDRQNASM
MLVGNVTDRV CILLDDIADT GNTITRAAKL LKKEGATTIY ALLTHGVFSG DAISRVKASA
IDKLVVTNSV PQDEHKKQLG SKLDVLDISP IFAEAMRRVH HGESISVLFN YE
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