ID A1CL68_ASPCL Unreviewed; 442 AA.
AC A1CL68;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000313|EMBL:EAW09892.1};
GN ORFNames=ACLA_041080 {ECO:0000313|EMBL:EAW09892.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09892.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09892.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006478}.
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DR EMBL; DS027056; EAW09892.1; -; Genomic_DNA.
DR RefSeq; XP_001271318.1; XM_001271317.1.
DR AlphaFoldDB; A1CL68; -.
DR STRING; 344612.A1CL68; -.
DR EnsemblFungi; EAW09892; EAW09892; ACLA_041080.
DR GeneID; 4702911; -.
DR KEGG; act:ACLA_041080; -.
DR VEuPathDB; FungiDB:ACLA_041080; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_0_1_1; -.
DR OMA; MMLVGDI; -.
DR OrthoDB; 276387at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:EnsemblFungi.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:EnsemblFungi.
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 CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 3.
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.
PE 3: Inferred from homology;
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 6..101
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT REGION 115..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47752 MW; 6016F293D8EC9E14 CRC64;
MVRNIIVIGG NSHPQLTQTI CSVLGIPPAE VLLSKFAVGE TRVEIKESVR EKDVYIIQSG
GLKVNDSLME LLITVSACKT ASAKRVTAVL PLFPYSRQSD IPYNKIGAPL VKSSADVKPG
SSNGYTFEST PPTPHPGKVD NGNLLNHVES LQKGLAKAQL DDVSNGSPVK KRVPNGLPRP
DTADSLKSEA SRSTVTNGQT NDDNASVGSA PSKISSFQPR PGYKQWVAQA GTLVADLLTC
AGADHIITMD LHDPQYQGFF DIPVDNLYGR PLLKSYIQQN IPYYRQAVVV SPDAGGAKRA
TAIADSMGME FALIHKERRP TKITDRQNAT MMLVGDVKDR TAILIDDLAD TSNTITRAAK
LLKKEGASKV YALVTHGILS GDAIDRINAS ALDKVVVTNS VDQADHLRRC PKLEVLEVGH
VFAEAIRRVH HGESISVLFQ YD
//
