ID   PSOB_ASPFU              Reviewed;         445 AA.
AC   Q4WAZ8;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Alpha/beta hydrolase psoB {ECO:0000303|PubMed:24082142};
DE            EC=3.7.1.- {ECO:0000305|PubMed:24939566};
DE   AltName: Full=Pseurotin biosynthesis protein B {ECO:0000303|PubMed:24082142};
GN   Name=psoB {ECO:0000303|PubMed:24082142}; ORFNames=AFUA_8G00530;
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.
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: Alpha/beta hydrolase; part of the gene cluster that mediates
CC       the biosynthesis of pseurotin A, a competitive inhibitor of chitin
CC       synthase 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:0000305|PubMed:24082142}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q93NG6}.
CC   -!- INDUCTION: Expression is induced under hypoxic conditions
CC       (PubMed:21388144). {ECO:0000269|PubMed:21388144}.
CC   -!- DISRUPTION PHENOTYPE: Results in significant reduction of pseurotin
CC       production (PubMed:24082142). {ECO:0000269|PubMed:24082142}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; AAHF01000014; EAL85114.1; -; Genomic_DNA.
DR   RefSeq; XP_747152.1; XM_742059.1.
DR   AlphaFoldDB; Q4WAZ8; -.
DR   SMR; Q4WAZ8; -.
DR   STRING; 746128.CADAFUBP00008382; -.
DR   ESTHER; aspfu-psoB; Duf_1100-S.
DR   EnsemblFungi; EAL85114; EAL85114; AFUA_8G00530.
DR   GeneID; 3504511; -.
DR   KEGG; afm:AFUA_8G00530; -.
DR   VEuPathDB; FungiDB:Afu8g00530; -.
DR   eggNOG; ENOG502QPTG; Eukaryota.
DR   HOGENOM; CLU_034451_0_0_1; -.
DR   InParanoid; Q4WAZ8; -.
DR   OMA; MGAYYAL; -.
DR   OrthoDB; 1133794at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..445
FT                   /note="Alpha/beta hydrolase psoB"
FT                   /id="PRO_0000438196"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WZB3"
SQ   SEQUENCE   445 AA;  49102 MW;  B85027A2AE1637FD CRC64;
     MATIHKLFKS PFFDFEFLRL LAMAPYEGAE IGEVLEAAAK IKDQDPESWY STLLETGGKA
     EAIAKQAEAS GDRVGARRAY LRSSNYLRAA QFMLNEGPIG HDERVLPTLE RAIANFRKGV
     QYRDGKTIFL EIPYEGGKTL PGYLYLPPAA RRIPGRKIPI LLNSGGGDST QEEIYFVNPA
     YGPDLGYAVL TFEGPGQGIV LRRDKLPMRP DWESVTGPVL DHLFDLATRH PELELDLDHI
     AVTGASMGGY FALRAAADPR IKACVSVDGF YSLSSFVGGR MPGPLFNGFM SGWLSDWMFN
     GILGVLKKLA FQARWEFNHL RWATGSTTDA DVMRSFGAYT LQKADGTEYL ADVKCPTLVT
     GAGASFYFDP ATTTDKIYDC LTSLQDGVDK EKWIATDVAY GGLQAKIGAF GYSAQKTFEW
     LDQRFGIQRE PLAASSRLED LVSRL