ID   AFUMC_ASPFC             Reviewed;         391 AA.
AC   B0Y567;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Glycosyltransferase afumC {ECO:0000303|PubMed:30977375};
DE            EC=2.4.1.- {ECO:0000269|PubMed:30977375};
DE   AltName: Full=Fumihopaside A biosynthesis cluster protein C {ECO:0000303|PubMed:30977375};
GN   Name=afumC {ECO:0000303|PubMed:30977375}; ORFNames=AFUB_071569;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
RX   PubMed=30977375; DOI=10.1021/acs.orglett.9b00984;
RA   Ma K., Zhang P., Tao Q., Keller N.P., Yang Y., Yin W.B., Liu H.;
RT   "Characterization and Biosynthesis of a Rare Fungal Hopane-Type
RT   Triterpenoid Glycoside Involved in the Antistress Property of Aspergillus
RT   fumigatus.";
RL   Org. Lett. 21:3252-3256(2019).
CC   -!- FUNCTION: Glycosyltransferase; part of the gene cluster that mediates
CC       the biosynthesis fumihopaside A, a hopane-type glucoside that enhances
CC       the thermotolerance and UV resistance of N.fumigata (PubMed:30977375).
CC       The first step of fumihopaside A biosynthesis is performed by the
CC       squalene hopane cyclase afumA that catalyzes the cyclization of 3S-
CC       oxidosqualene into the hopene 21-beta-H-hopane-3-beta,22-diol
CC       (PubMed:30977375). The cytochrome P450 monooxygenase afumB is
CC       responsible for both hydroxylation at C-24 and oxidations at C-30 of
CC       the afumA product (PubMed:30977375). The glycosyltransferase afumC then
CC       catalyzes the glycosylation at C-24, using UDP-D-glucose as a donor, to
CC       produce fumihopaside A (PubMed:30977375). AfumC is also able to accept
CC       UDP-D-galactose and UDP-D-glucuronic acid as donors to yield minor
CC       derivatives (PubMed:30977375). Fumihopaside B, another minor derivative
CC       produced, is different from fumihopaside A due to the presence of a
CC       double bond between C-22 and C-29 (PubMed:30977375).
CC       {ECO:0000269|PubMed:30977375}.
CC   -!- ACTIVITY REGULATION: Activity is significantly decreased by addition of
CC       divalent cations such as Mg(2+), Mn(2+), Zn(2+), Ca(2+), Co(2+),
CC       Cu(2+), and Ni(2+); while Fe(2+) has little effect.
CC       {ECO:0000269|PubMed:30977375}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.33 mM for the agylcone intermediate (in presence of UDP-D-
CC         glucose) {ECO:0000269|PubMed:30977375};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:30977375};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:30977375};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:30977375}.
CC   -!- DISRUPTION PHENOTYPE: Failed to produce fumihopaside A, but leads to
CC       the accumulation of the aglycone intermediate.
CC       {ECO:0000269|PubMed:30977375}.
CC   -!- SIMILARITY: Belongs to the afumC glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; DS499598; EDP50816.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y567; -.
DR   EnsemblFungi; EDP50816; EDP50816; AFUB_071569.
DR   VEuPathDB; FungiDB:AFUB_071569; -.
DR   HOGENOM; CLU_061936_0_0_1; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   InterPro; IPR008441; AfumC-like_glycosyl_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF05704; Caps_synth; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..391
FT                   /note="Glycosyltransferase afumC"
FT                   /id="PRO_0000452740"
SQ   SEQUENCE   391 AA;  44642 MW;  DA091C7A15E09B7B CRC64;
     MAIPTKERGS RLTDADILSD LQMYKPVTDS DTRNVWAFWD KGLSNSPAWN QRNVISWVRR
     LSPKWTVRVL DLVEGSPNHV SQFIPREMLT DVFWNRTMTG PHVGQHSSDL IRLPLLYLYG
     GVWLDVGMLL FRSLDALCWN ALEDPETPYE VAAFKVSMGP ELSFLFNGFI AARRGSVCIK
     YWHEIFRTLW DGATSCAGMH SHPLLAHLPV YEPPSLNGKR PPFMYAQFAD YLAQVFCLER
     LRHLVDSKTG WDGPKFFEEK VLLFDCVTEA YWAQRLTDWN GRKQYELLDL QRGEDGLDNA
     RVKEAEALVQ GVLSMSSTMK LSHGLVTAGR EYLADIWDSP KNHDADIRPG TFAAYLREAS
     ETFEQTKELV PLRMPVIEKA LLRAGVTEVV R