ID   ACLG_ASPOR              Reviewed;         221 AA.
AC   Q2UPB2;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Glutathione S-transferase aclG {ECO:0000303|PubMed:25302411};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:A4GYZ0};
DE   AltName: Full=Aspirochlorine biosynthesis protein G {ECO:0000303|PubMed:25302411};
GN   Name=aclG {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000040;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=25302411; DOI=10.1002/anie.201407624;
RA   Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA   Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT   "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT   involves a cryptic amino acid conversion.";
RL   Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC   -!- FUNCTION: Glutathione S-transferase; part of the gene cluster that
CC       mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an
CC       unusual halogenated spiro compound with distinctive antifungal
CC       properties due to selective inhibition of protein biosynthesis, and
CC       which is also active against bacteria, viruses, and murine tumor cells
CC       (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is
CC       responsible the formation of the diketopiperazine (DKP) core from the
CC       condensation of 2 phenylalanine residues (PubMed:25302411). One Phe
CC       residue is tailored into chlorotyrosine by hydroxylation and
CC       chlorination, whereas the second Phe undergoes an unprecedented C-C
CC       bond cleavage to be converted into glycine (PubMed:25302411). After
CC       formation of the DKP, sulfur is incorporated into the DKP by
CC       conjugation with glutathione by aclG, followed by its stepwise
CC       degradation to the thiol by aclI, aclJ and aclK, and the dithiol
CC       oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB,
CC       aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as
CC       tailoring enzymes to produce the intermediate dechloroaspirochlorine
CC       (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine
CC       by the halogenase aclH is the last step in the aspirochlorine pathway
CC       (PubMed:25302411). {ECO:0000269|PubMed:25302411}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:A4GYZ0};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; AP007154; BAE56603.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UPB2; -.
DR   SMR; Q2UPB2; -.
DR   EnsemblFungi; BAE56603; BAE56603; AO090001000040.
DR   HOGENOM; CLU_011226_14_2_1; -.
DR   OMA; FAMPWMF; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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   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   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..221
FT                   /note="Glutathione S-transferase aclG"
FT                   /id="PRO_0000441205"
FT   DOMAIN          1..91
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT   DOMAIN          97..221
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ   SEQUENCE   221 AA;  25776 MW;  23522DBCB5CC30A6 CRC64;
     MEYDGRVILY IIKADETSYI NYIKPLILAE EIQFPHVLSV IDTRDEWFYS IHPERMVPSL
     KDQDPVTGEK VIVFESTACL QYLVDRFDTD GTWSGRTVAE KGAVLSWTAY QTAALGPTAK
     YWLYFKRGYP TRANPVQLPR TIEKQWDILE KRLKEPGQQY IALKDRPTLA DLSYFPFAMP
     WMFTFLGVDI KDWPHIQRWS ERMLSRPAVA RVLQRAPTLG H