ID A0A1V6R3H9_9EURO Unreviewed; 491 AA.
AC A0A1V6R3H9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN ORFNames=PENSOL_c019G04312 {ECO:0000313|EMBL:OQD95752.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD95752.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD95752.1}.
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DR EMBL; MDYO01000019; OQD95752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R3H9; -.
DR STRING; 60172.A0A1V6R3H9; -.
DR OrthoDB; 276387at2759; -.
DR Proteomes; UP000191612; 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; -; 4.
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; 3.
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:UP000191612};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..120
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT REGION 228..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 53321 MW; 2A16B013A310FCB2 CRC64;
MRGVQIFSGN SHPGLADTIC ERLGTVPAKA NLGKFANGET SVNIGTSVRN QDVYIIQSGS
EKINDSVMEL LIMISACKGG SAKSITAVMP YFPYSRQSKK KSHRGAITAR MLANLLTIAG
VDHVITMDLH ASQMQGFFGK PVDNLFAEPF IARWLRMNVP GWKDAVVVSK NAGGTKRVTS
LADTLKLNFG IVTTDRRRPK VPVATMSDST VFFDAVDEDP ISTKEARPFE LHMHSSNRTP
ATPPIPEEPE PVSPPPERYL LRPETPPAAR RPSELEAAYE YTDVRVRDVI TGRLVQGQLV
DDDYRINEES QSGGTTPGGG SSSHDNTEAI PDSMVNSMIS NASSQPPDHA LGGSFDAVES
DDEASVCGGH VDERTITLVG EVRDRSVFLV DDMIDKSGSW IAAAETVVKR GGASKVYCIA
THGLFGENSL DQMEACRSID HIVVTNTFPI SPSMLRRSKK LIVIDVSSLL AESIRRHHYG
ESVSALFHLN D
//
