ID C9STP6_VERA1 Unreviewed; 406 AA.
AC C9STP6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN ORFNames=VDBG_08317 {ECO:0000313|EMBL:EEY22207.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(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; DS985225; EEY22207.1; -; Genomic_DNA.
DR RefSeq; XP_003001272.1; XM_003001226.1.
DR AlphaFoldDB; C9STP6; -.
DR STRING; 526221.C9STP6; -.
DR GeneID; 9529320; -.
DR KEGG; val:VDBG_08317; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_678263_0_0_1; -.
DR OrthoDB; 276387at2759; -.
DR Proteomes; UP000008698; 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:SF57; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1; 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:EEY22207.1};
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:UP000008698};
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 221..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 44218 MW; 31539DD46FBD985A CRC64;
MRSTLIFAGS SCPALTGQIC ENLGMQPAEA ELTQFSNGET RVRILTSVRE KDVFIVQSGS
PKVNDTIMEL LIMISACKGG SANKVTAVLP YFPYSRQSKK KSHRGAITAR MLANLLTMAG
IKHVITVDLH ATQMQGFFKC PVDNLHAEPL IARWIRHNVA NWKEAVVVSK NAGGTKRVTS
LADALKLNFG MVTTEKKKHR GANMSASVIM GHLHSFNREP VLESSATSKP AEAKTEALEE
PAASEPQNVR RNRVRANTQG SPQRSNGPPL RTADVNRVVR PTTPTKNSSG QQQDEDESDA
QYDDGPAYEV TQGRLVQGHI VDDDYPSPAT STAGGSSREE PDPMTCRMPR PSSPILQPRR
ARASCAGRFR RRRGRIGRGG STLKDPSRAM IHWSGRGTAP PSSLMT
//
