ID   PSOC_ASPFU              Reviewed;         271 AA.
AC   Q4WB00;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Methyltransferase psoC {ECO:0000303|PubMed:24082142};
DE            EC=2.1.1.- {ECO:0000269|PubMed:24939566};
DE   AltName: Full=Pseurotin biosynthesis protein C {ECO:0000303|PubMed:24082142};
GN   Name=psoC {ECO:0000303|PubMed:24082142}; ORFNames=AFUA_8G00550;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   INDUCTION.
RX   PubMed=21388144; DOI=10.1021/pr1012812;
RA   Voedisch M., Scherlach K., Winkler R., Hertweck C., Braun H.P., Roth M.,
RA   Haas H., Werner E.R., Brakhage A.A., Kniemeyer O.;
RT   "Analysis of the Aspergillus fumigatus proteome reveals metabolic changes
RT   and the activation of the pseurotin A biosynthesis gene cluster in response
RT   to hypoxia.";
RL   J. Proteome Res. 10:2508-2524(2011).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24082142; DOI=10.1073/pnas.1313258110;
RA   Wiemann P., Guo C.J., Palmer J.M., Sekonyela R., Wang C.C., Keller N.P.;
RT   "Prototype of an intertwined secondary-metabolite supercluster.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:17065-17070(2013).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX   PubMed=24939566; DOI=10.1002/anie.201404804;
RA   Tsunematsu Y., Fukutomi M., Saruwatari T., Noguchi H., Hotta K., Tang Y.,
RA   Watanabe K.;
RT   "Elucidation of pseurotin biosynthetic pathway points to trans-acting C-
RT   methyltransferase: generation of chemical diversity.";
RL   Angew. Chem. Int. Ed. 53:8475-8479(2014).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase
CC       and an inducer of nerve-cell proliferation (PubMed:24082142,
CC       PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible
CC       for the biosynthesis of azaspirene, one of the first intermediates
CC       having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin,
CC       via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-
CC       phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-
CC       functional monooxygenase/methyltransferase psoF seems to be involved in
CC       the addition of the C3 methyl group onto the pseurotin scaffold
CC       (PubMed:24939566). Azaspirene is then converted to synerazol through 4
CC       steps including oxidation of C17 by the cytochrome P450 monooxygenase
CC       psoD, O-methylation of the hydroxy group of C8 by the methyltransferase
CC       psoC, and the trans-to-cis isomerization of the C13 olefin by the
CC       glutathione S-transferase psoE (PubMed:24939566). The fourth step of
CC       synerazol production is performed by the dual-functional
CC       monooxygenase/methyltransferase psoF which seems to catalyze the
CC       epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566).
CC       Synerazol can be attacked by a water molecule nonenzymatically at two
CC       different positions to yield two diol products, pseurotin A and
CC       pseurotin D (PubMed:24939566). {ECO:0000269|PubMed:24082142,
CC       ECO:0000269|PubMed:24939566}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:24082142, ECO:0000269|PubMed:24939566}.
CC   -!- INDUCTION: Expression is induced under hypoxic conditions
CC       (PubMed:21388144). {ECO:0000269|PubMed:21388144}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of pseurotin
CC       (PubMed:24082142, PubMed:24939566). {ECO:0000269|PubMed:24082142,
CC       ECO:0000269|PubMed:24939566}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; AAHF01000014; EAL85112.1; -; Genomic_DNA.
DR   RefSeq; XP_747150.1; XM_742057.1.
DR   AlphaFoldDB; Q4WB00; -.
DR   SMR; Q4WB00; -.
DR   STRING; 746128.CADAFUBP00008380; -.
DR   EnsemblFungi; EAL85112; EAL85112; AFUA_8G00550.
DR   GeneID; 3504509; -.
DR   KEGG; afm:AFUA_8G00550; -.
DR   VEuPathDB; FungiDB:Afu8g00550; -.
DR   eggNOG; ENOG502SIG3; Eukaryota.
DR   HOGENOM; CLU_010595_9_3_1; -.
DR   InParanoid; Q4WB00; -.
DR   OMA; WVQLMEM; -.
DR   OrthoDB; 1242994at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..271
FT                   /note="Methyltransferase psoC"
FT                   /id="PRO_0000438197"
SQ   SEQUENCE   271 AA;  29554 MW;  92CC65B8C3E980D8 CRC64;
     MDNFMEMTKK LGHQPELLRL RALDATYDDA LEGKLVVAPL DMSEPGKKIL DSGTADGTWL
     RNVRSKQSVP HDYYGSDVEG ELFPKDPDGI TYFAHSFKDP WPQQYLGFFD LVHIRGSLAG
     SAPEGPAPVI QNLTTLLKPG GWVQLMEMNA FSPPPNGPAM TDFAKMASEM FTGIGVGDFA
     NNNKSMLEDA GLKNVQEKRV IVNLGKKAKP ELHDQSIHGV TGPIVPLTSV ARTVKSSFTG
     EQLDALPARV KEELETEGGQ VEMIIAFGQK A