PSOE_ASPFU
ID PSOE_ASPFU Reviewed; 237 AA.
AC Q4WB03;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutathione S-transferase psoE {ECO:0000303|PubMed:24082142};
DE EC=2.5.1.- {ECO:0000269|PubMed:27072782};
DE AltName: Full=Pseurotin biosynthesis protein E {ECO:0000303|PubMed:24082142};
GN Name=psoE {ECO:0000303|PubMed:24082142}; ORFNames=AFUA_8G00580;
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, AND DISRUPTION PHENOTYPE.
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=27072782; DOI=10.1002/anie.201600940;
RA Yamamoto T., Tsunematsu Y., Hara K., Suzuki T., Kishimoto S., Kawagishi H.,
RA Noguchi H., Hashimoto H., Tang Y., Hotta K., Watanabe K.;
RT "Oxidative trans to cis Isomerization of Olefins in Polyketide
RT Biosynthesis.";
RL Angew. Chem. Int. Ed. 55:6207-6210(2016).
CC -!- FUNCTION: Glutathione S-transferase; part of the gene cluster that
CC mediates the biosynthesis of pseurotin A, a competitive inhibitor of
CC chitin synthase and an inducer of nerve-cell proliferation
CC (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA
CC is responsible for the biosynthesis of azaspirene, one of the first
CC intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core
CC of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a
CC L-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, PubMed:27072782). The
CC fourth step of 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, ECO:0000269|PubMed:27072782}.
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:27072782};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27072782, ECO:0000305|PubMed:24082142,
CC ECO:0000305|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 but leads
CC to the accumulation of deepoxy-synerazol (PubMed:24082142,
CC PubMed:24939566). {ECO:0000269|PubMed:24082142,
CC ECO:0000269|PubMed:24939566}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; AAHF01000014; EAL85109.1; -; Genomic_DNA.
DR RefSeq; XP_747147.1; XM_742054.1.
DR PDB; 5F8B; X-ray; 2.54 A; A=1-237.
DR PDB; 5FHI; X-ray; 2.41 A; A=1-237.
DR PDBsum; 5F8B; -.
DR PDBsum; 5FHI; -.
DR AlphaFoldDB; Q4WB03; -.
DR SMR; Q4WB03; -.
DR STRING; 746128.CADAFUBP00008377; -.
DR EnsemblFungi; EAL85109; EAL85109; AFUA_8G00580.
DR GeneID; 3504489; -.
DR KEGG; afm:AFUA_8G00580; -.
DR VEuPathDB; FungiDB:Afu8g00580; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_3_2_1; -.
DR InParanoid; Q4WB03; -.
DR OMA; FECMAIA; -.
DR OrthoDB; 1341490at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..237
FT /note="Glutathione S-transferase psoE"
FT /id="PRO_0000438219"
FT DOMAIN 2..79
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 84..222
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT REGION 208..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5FHI"
FT BINDING 49
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5FHI"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5FHI"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5FHI"
FT BINDING 63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5FHI"
FT BINDING 64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5FHI"
FT BINDING 99
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5F8B"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27072782,
FT ECO:0007744|PDB:5F8B"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5FHI"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:5FHI"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:5FHI"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:5FHI"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5FHI"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 121..141
FT /evidence="ECO:0007829|PDB:5FHI"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5FHI"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:5FHI"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5FHI"
SQ SEQUENCE 237 AA; 26805 MW; 1CD9DE0B34F5B77C CRC64;
MVFGTLYTFP GDQCRTIAIK AVAKANGLDL DIRETPRTPD HLSISKLGKV PAFQGADSFK
LFECMAIALY ITSQNEQTTL LGKDKKEYAE IIKWMSFFNT EIVILMTQQL LPQLGVIPYD
RDQVEFFANM TQRSVDVVEE YLQDRTFLVG DQLSLADLFC AGNISLGFQF FYGKAWRQQN
PNVSRWYEMV CHQPIYAAVT DKFQLLDEPK LTNNPPEKKP ETVPKNGAAV AIEATQA
