ID   USTS_ASPFN              Reviewed;         276 AA.
AC   B8NM79;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Glutathione S-transferase-like protein ustS {ECO:0000303|PubMed:24841822};
DE            EC=2.5.1.- {ECO:0000305|PubMed:24841822};
DE   AltName: Full=Ustiloxin B biosynthesis protein S {ECO:0000303|PubMed:24841822};
GN   Name=ustS {ECO:0000303|PubMed:24841822}; ORFNames=AFLA_095110;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX   PubMed=24841822; DOI=10.1016/j.fgb.2014.04.011;
RA   Umemura M., Nagano N., Koike H., Kawano J., Ishii T., Miyamura Y.,
RA   Kikuchi M., Tamano K., Yu J., Shin-ya K., Machida M.;
RT   "Characterization of the biosynthetic gene cluster for the ribosomally
RT   synthesized cyclic peptide ustiloxin B in Aspergillus flavus.";
RL   Fungal Genet. Biol. 68:23-30(2014).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX   PubMed=27166860; DOI=10.1002/anie.201602611;
RA   Ye Y., Minami A., Igarashi Y., Izumikawa M., Umemura M., Nagano N.,
RA   Machida M., Kawahara T., Shin-Ya K., Gomi K., Oikawa H.;
RT   "Unveiling the biosynthetic pathway of the ribosomally synthesized and
RT   post-translationally modified peptide ustiloxin B in filamentous fungi.";
RL   Angew. Chem. Int. Ed. 55:8072-8075(2016).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26703898; DOI=10.1016/j.fgb.2015.12.010;
RA   Nagano N., Umemura M., Izumikawa M., Kawano J., Ishii T., Kikuchi M.,
RA   Tomii K., Kumagai T., Yoshimi A., Machida M., Abe K., Shin-ya K., Asai K.;
RT   "Class of cyclic ribosomal peptide synthetic genes in filamentous fungi.";
RL   Fungal Genet. Biol. 86:58-70(2016).
CC   -!- FUNCTION: Glutathione S-transferase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of the secondary metabolite
CC       ustiloxin B, an antimitotic tetrapeptide (PubMed:24841822,
CC       PubMed:27166860, PubMed:26703898). First, ustA is processed by the
CC       subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene
CC       cluster, at the C-terminal side of Arg-Lys, after transfer to Golgi
CC       apparatus through the endoplasmic reticulum (ER) (PubMed:24841822).
CC       Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI
CC       (PubMed:24841822). To process the precursor peptide further, at least
CC       two peptidases are necessary to cleave the N-terminal and C-terminal
CC       sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for
CC       the synthesis of ustiloxin B, through cyclization and modification of
CC       the tyrosine with a non-protein coding amino acid, norvaline
CC       (PubMed:24841822). One of the two peptidases must be the serine
CC       peptidase ustP; and the other pepdidase is probably ustH
CC       (PubMed:24841822). Macrocyclization of the core peptide derived from
CC       ustA requires the tyrosinase ustQ, as well as the homologous oxidases
CC       ustYa and ustYb, and leads to the production of the first cyclization
CC       product N-desmethylustiloxin F (PubMed:27166860, PubMed:26703898). For
CC       the formation of N-desmethylustiloxin F, three oxidation steps are
CC       required, hydroxylation at the benzylic position, hydroxylation at
CC       either the aromatic ring of Tyr or beta-position of Ile, and oxidative
CC       cyclization (PubMed:27166860). UstQ may catalyze the oxidation of a
CC       phenol moiety, whereas the ustYa and ustYb are most likely responsible
CC       for the remaining two-step oxidations (PubMed:27166860). N-
CC       desmethylustiloxin F is then methylated by ustM to yield ustiloxin F
CC       which in turn substrate of the cytochrome P450 monooxygenase ustC which
CC       catalyzes the formation of S-deoxyustiloxin H (PubMed:27166860). The
CC       flavoprotein monooxygenases ustF1 and ustF2 then participate in the
CC       modification of the side chain of S-deoxyustiloxin H, leading to the
CC       synthesis of an oxime intermediate, via ustiloxin H (PubMed:27166860).
CC       Finally, carboxylative dehydration performed by the cysteine
CC       desulfurase-like protein ustD yields ustiloxin B (PubMed:27166860).
CC       {ECO:0000269|PubMed:24841822, ECO:0000269|PubMed:26703898,
CC       ECO:0000269|PubMed:27166860}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:24841822}.
CC   -!- DISRUPTION PHENOTYPE: Does not alter the production of ustiloxin B
CC       (PubMed:24841822, PubMed:26703898). {ECO:0000269|PubMed:24841822,
CC       ECO:0000269|PubMed:26703898}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED49430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EQ963480; EED49430.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002381331.1; XM_002381290.1.
DR   AlphaFoldDB; B8NM79; -.
DR   SMR; B8NM79; -.
DR   EnsemblFungi; EED49430; EED49430; AFLA_095110.
DR   eggNOG; ENOG502SAAV; Eukaryota.
DR   HOGENOM; CLU_011226_4_2_1; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..276
FT                   /note="Glutathione S-transferase-like protein ustS"
FT                   /id="PRO_0000437305"
FT   DOMAIN          16..109
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
SQ   SEQUENCE   276 AA;  30963 MW;  FAEE87CE1F27BDD7 CRC64;
     MTKTEESPLH FFDIFSTLPG TSKSWSSNVL KIRMVLNYKG IPYTQSFHSY PDIAPLLQSL
     SVPPHKQGRF KYTLPAICHP SSVKSSPSGA MMDSLPIACH LDETYPDPPL FPSGEASYAL
     ALAIGKLMVP AALKTCDLLL PKAEEVLDDR GKEYFVRTRT EIFGKPLSEL RPKTEEGVRA
     IVDGMKADME VFISMLRGRG EGKKSGPFLE GEKPGYADFI LVTFLSWSHR FDMELWREIM
     DMGNGEFRAL WHASVQWLEG QGEEKEWAVP QLSTVD