ID   TPCF_ASPFU              Reviewed;         225 AA.
AC   Q4WQZ2;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Glutathione S-transferase-like protein tpcF {ECO:0000303|PubMed:26242966};
DE            EC=2.5.1.- {ECO:0000305|PubMed:26242966};
DE   AltName: Full=Trypacidin synthesis protein E {ECO:0000303|PubMed:26242966};
GN   Name=tpcF {ECO:0000303|PubMed:26242966};
GN   Synonyms=tynF {ECO:0000303|PubMed:26278536}; ORFNames=AFUA_4G14530;
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   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22319557; DOI=10.1371/journal.pone.0029906;
RA   Gauthier T., Wang X., Sifuentes Dos Santos J., Fysikopoulos A., Tadrist S.,
RA   Canlet C., Artigot M.P., Loiseau N., Oswald I.P., Puel O.;
RT   "Trypacidin, a spore-borne toxin from Aspergillus fumigatus, is cytotoxic
RT   to lung cells.";
RL   PLoS ONE 7:E29906-E29906(2012).
RN   [3]
RP   FUNCTION.
RX   PubMed=26278536; DOI=10.1007/s00253-015-6898-1;
RA   Mattern D.J., Schoeler H., Weber J., Novohradska S., Kraibooj K.,
RA   Dahse H.M., Hillmann F., Valiante V., Figge M.T., Brakhage A.A.;
RT   "Identification of the antiphagocytic trypacidin gene cluster in the human-
RT   pathogenic fungus Aspergillus fumigatus.";
RL   Appl. Microbiol. Biotechnol. 99:10151-10161(2015).
RN   [4]
RP   FUNCTION.
RX   PubMed=26242966; DOI=10.1111/1462-2920.13007;
RA   Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
RT   "Redundant synthesis of a conidial polyketide by two distinct secondary
RT   metabolite clusters in Aspergillus fumigatus.";
RL   Environ. Microbiol. 18:246-259(2016).
CC   -!- FUNCTION: Glutathione S-transferase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of trypacidin, a mycotoxin with
CC       antiprotozoal activity and that plays a role in the infection process
CC       (PubMed:26278536, PubMed:26242966). The pathway begins with the
CC       synthesis of atrochrysone thioester by the polyketide synthase (PKS)
CC       tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB
CC       then breaks the thioester bond and releases the atrochrysone carboxylic
CC       acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts
CC       atrochrysone carboxylic acid to atrochrysone which is further reduced
CC       into emodin anthrone (PubMed:26242966). The next step is performed by
CC       the emodin anthrone oxygenase tpcL that catalyzes the oxidation of
CC       emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase
CC       encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin
CC       to form questin (PubMed:26242966). Ring cleavage of questin by questin
CC       oxidase tpcI leads to desmethylsulochrin via several intermediates
CC       including questin epoxide (By similarity). Another methylation step
CC       catalyzed by tpcM leads to the formation of sulochrin which is further
CC       converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes
CC       the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966).
CC       Trypacidin is toxic for human pulmonary and bronchial epithelial cells
CC       by initiating the intracellular formation of nitric oxide (NO) and
CC       hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death
CC       (PubMed:22319557). The trypacidin pathway is also able to produce
CC       endocrocin via a distinct route from the endocrocin Enc pathway
CC       (PubMed:26242966). {ECO:0000250|UniProtKB:Q0CCY0,
CC       ECO:0000269|PubMed:22319557, ECO:0000269|PubMed:26242966,
CC       ECO:0000269|PubMed:26278536}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26278536}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in conidia
CC       (PubMed:22319557). {ECO:0000305|PubMed:22319557}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000005; EAL89342.1; -; Genomic_DNA.
DR   RefSeq; XP_751380.1; XM_746287.1.
DR   AlphaFoldDB; Q4WQZ2; -.
DR   SMR; Q4WQZ2; -.
DR   STRING; 330879.Q4WQZ2; -.
DR   EnsemblFungi; EAL89342; EAL89342; AFUA_4G14530.
DR   GeneID; 3509604; -.
DR   KEGG; afm:AFUA_4G14530; -.
DR   VEuPathDB; FungiDB:Afu4g14530; -.
DR   HOGENOM; CLU_011226_14_2_1; -.
DR   InParanoid; Q4WQZ2; -.
DR   OMA; NEKEWFE; -.
DR   OrthoDB; 1231780at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:AspGD.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:AspGD.
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   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..225
FT                   /note="Glutathione S-transferase-like protein tpcF"
FT                   /id="PRO_0000437069"
FT   DOMAIN          4..85
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT   DOMAIN          92..225
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ   SEQUENCE   225 AA;  25031 MW;  B2AEBF68D76148B2 CRC64;
     MPDIQPITVY GKGGPNPPRV AIILAELDLP HKVIEVPLSK VKEPDYVAIN PNGRIPAIYD
     PNTDLTLWES GAIVEYLVSH YDPDHRISFP AGSNLAALAT QWLFFQASGQ GPYYGQASWF
     KKFHHEKVPS AIERYVKEIN RVTGVLEGHL SRQKVAADGD GPWLVGGKCS FADLAWIPWQ
     VIVTAIIQPE DGYTVEDYPH VKNWLDRMMA RPGVQKGMAD IFPST