XPTB_EMENI
ID XPTB_EMENI Reviewed; 463 AA.
AC P0DP82;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Xanthone prenyltransferase B {ECO:0000303|PubMed:21351751};
DE EC=2.5.1.- {ECO:0000269|PubMed:23150454};
GN Name=xptB {ECO:0000303|PubMed:21351751}; ORFNames=AN12402;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21351751; DOI=10.1021/ja1096682;
RA Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S., Chiang Y.M.,
RA Wang C.C., Oakley B.R.;
RT "Genome-based deletion analysis reveals the prenyl xanthone biosynthesis
RT pathway in Aspergillus nidulans.";
RL J. Am. Chem. Soc. 133:4010-4017(2011).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=22730213; DOI=10.1002/cbic.201200014;
RA Simpson T.J.;
RT "Genetic and biosynthetic studies of the fungal prenylated xanthone
RT shamixanthone and related metabolites in Aspergillus spp. revisited.";
RL ChemBioChem 13:1680-1688(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=23150454; DOI=10.1002/cbic.201200545;
RA Pockrandt D., Ludwig L., Fan A., Koenig G.M., Li S.M.;
RT "New insights into the biosynthesis of prenylated xanthones: Xptb from
RT Aspergillus nidulans catalyses an O-prenylation of xanthones.";
RL ChemBioChem 13:2764-2771(2012).
CC -!- FUNCTION: Dehydrogenase involved in the conversion of monodictyphenone
CC to the prenyl xanthones such as emericellin, shamixanthone and
CC epishamixanthone (PubMed:21351751, PubMed:22730213). Monodictyphenone
CC is first converted to variecoxanthone A via a paeciloxanthone
CC intermediate by the consecutive actions of the FAD-dependent
CC monooxygenase mdpD and the xanthone prenyltransferase xptB
CC (PubMed:21351751). XptB catalyzes regular O-prenylation at the hydroxy
CC group of C-7 of the xanthone ring (PubMed:23150454). Variecoxanthone A
CC is further prenylated to emericellin by xptA before being reduced to
CC shamixanthone and epishamixanthone by the dehydrogenase xptC
CC (PubMed:21351751). {ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213, ECO:0000269|PubMed:23150454}.
CC -!- ACTIVITY REGULATION: Mn(2+) and Co(2+) strongly enhance prenylation
CC activity (PubMed:23150454). {ECO:0000269|PubMed:23150454}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.327 mM for 1,7-dihydroxy-6-methyl-8-hydroxymethyl-xanthone
CC {ECO:0000269|PubMed:23150454};
CC KM=1.147 mM for 1,7-dihydroxy-6-methylxanthone
CC {ECO:0000269|PubMed:23150454};
CC KM=0.081 mM for 1,7-dihydroxy-6,8-dimethylxanthone
CC {ECO:0000269|PubMed:23150454};
CC KM=0.087 mM for 1,7-dihydroxy-5,6,8-trimethylxanthone
CC {ECO:0000269|PubMed:23150454};
CC KM=0.024 mM for dimethylallyl diphosphate (DMAPP)
CC {ECO:0000269|PubMed:23150454};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:21351751, ECO:0000269|PubMed:23150454}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of the xanthones
CC variecoxanthone A, emericellin, shamixanthone and epishamixanthone; and
CC accumulates several upstream metabolites, including emodin,
CC chrysophanol and monodictyphenone (PubMed:21351751).
CC {ECO:0000269|PubMed:21351751}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BN001302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACD01000137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DP82; -.
DR SMR; P0DP82; -.
DR VEuPathDB; FungiDB:AN12402; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..463
FT /note="Xanthone prenyltransferase B"
FT /id="PRO_0000441130"
SQ SEQUENCE 463 AA; 52371 MW; C5B9EC34D18B3A6A CRC64;
MATDGMVLHK RSLSEGGTST QAWKVLSQTL PSRGPDVDAW WQLTGRHLAV LLDAAAYPIE
KQYECLLYHY HYAAPYLGPA PREGASPPTW KSMLQLDGTP FEFSWKWNNP GGEPDVRFGL
EPIGPMAGTS LDPLNHLAMR EILYKLSSAV PGSDLTWTHH FLATLFDHDY AKYTQKAATM
GSSIGTSLVY SLEFQRKSTG LKTYFHPRKL DQQAFLDIPS WEASFRGLHP NSPSRTAVHE
FLSTNPEGKL LKPFCLSVDN CSPAKARIKW YFNSPHTNFR AIREIMTLGG RIADTETRTK
QFSELFNLLK TVTEEHADFP ETSEFPYVPN NGDSIIPNFA DAPDMLKGCV YFFDIAPGRN
LPAIKVYFPV RNHCRNDLAV TQNLNRWLES RGRGQYGAAF GRALETIADY RRLEDSGGLL
SFLSCQFMED GELDLTSYFN PQAFHSGRLT HRRATRRRGD DRW
