ID   GT1_BEAB2               Reviewed;         461 AA.
AC   J4VV61;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=UDP-glucosyltransferase 1 {ECO:0000303|PubMed:34903054};
DE            Short=GT1 {ECO:0000303|PubMed:34903054};
DE            EC=2.4.1.- {ECO:0000269|PubMed:34903054};
GN   ORFNames=BBA_08686;
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860;
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA   St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX   PubMed=34903054; DOI=10.1128/mbio.03279-21;
RA   Chen B., Sun Y., Li S., Yin Y., Wang C.;
RT   "Inductive production of the iron-chelating 2-pyridones benefits the
RT   producing fungus to compete for diverse niches.";
RL   MBio 12:e0327921-e0327921(2021).
CC   -!- FUNCTION: UDP-glucosyltransferase; part of the pathway that mediates
CC       the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds
CC       involved in iron stress tolerance, competition with the natural
CC       competitor fungus Metarhizium robertsii and insect hosts infection
CC       (PubMed:34903054). Targets the N-OH hydroxyl residue of 15-
CC       hydroxytellenin (15-HT) to produce pyridovericin-N-O-(beta-D-
CC       glucopyranoside) which is further methylated by the methyltransferase
CC       MT1 to yield pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside)
CC       (PMGP) (PubMed:34903054). The pathway begins with the assembly of the
CC       polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the
CC       help of the enoyl reductase tenC. These enzymes catalyze the synthesis
CC       of the pyrrolidine-2-dione intermediates pretellinin A, 11-
CC       hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-
CC       hydropretellenin A, 12-oxopretellenin A and prototellinin D. The
CC       cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring
CC       expansion of pretenellin A and 14-hydropretellenin A to form the 2-
CC       pyridone core, leading to pretenellin B and pyridovericin,
CC       respectively. The cytochrome P450 monooxygenase tenB is then required
CC       for the selective N-hydroxylation of the 2-pyridone nitrogen of yield
CC       tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-
CC       glucosyltransferase GT1 and the methyltransferase MT1, located outside
CC       the tenS gene cluster, contribute to the stepwise glycosylation and
CC       methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-
CC       methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds
CC       such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A
CC       are also produced but the enzymes involved in their biosynthesis have
CC       still to be determined (PubMed:34903054).
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor tenR and is induced during cocultures with the
CC       natural competitor fungus Metarhizium robertsii.
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of detectable
CC       pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP).
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JH725187; EJP62360.1; -; Genomic_DNA.
DR   RefSeq; XP_008602005.1; XM_008603783.1.
DR   SMR; J4VV61; -.
DR   STRING; 655819.J4VV61; -.
DR   EnsemblFungi; EJP62360; EJP62360; BBA_08686.
DR   GeneID; 19891698; -.
DR   HOGENOM; CLU_000537_4_1_1; -.
DR   InParanoid; J4VV61; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..461
FT                   /note="UDP-glucosyltransferase 1"
FT                   /id="PRO_0000455690"
SQ   SEQUENCE   461 AA;  50398 MW;  BF093A12E0E64820 CRC64;
     MSPSRSEPLI DNLVDRSNLK IVALASPADG HTFPLLRIVE ELVLRGYDVT FLASEDYRAR
     TAAVGAYFVP VPPYDDIQRI TTELSVIADP GERMNAAMIE LFITPTAGRM ATLYAALEDV
     KREKPLHKVV LLTESFFLGD HPLFLGAPLP KGFTRRPRAI NIHACSYGLS SVDSAPFGLT
     IIPDGTAESR EKYRKLHSDM LTGSLAESVA LQKKVLTELG ATNMDEVEGR NPLDVIATTA
     DVTLQMCPPS LEYRRSDIHP KVRFIGALPP RAPPKTFSAP PFWNTVINGS KRVVVVSQGT
     VAVRYDQLLV PAMHALADRD DIVVVAILGQ KGAELPGEVA IPSNAYTVDY LSYDAMLPYA
     SVFVLNAGYG GFMHGIVNGV PMVLAGGSED KPEVANRGEF AGVGINLRTG TPSQRQIRQG
     VDEILSNPKY KRRVKEIQLE NEKMKAMDSV EKEILKWAAM D