ID   VERT_CLORO              Reviewed;         327 AA.
AC   A0A1U9YHZ1;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Thioredoxin reductase verT {ECO:0000250|UniProtKB:E9RAH5};
DE            EC=1.8.1.- {ECO:0000250|UniProtKB:E9RAH5};
DE   AltName: Full=Verticillin biosynthesis cluster protein T {ECO:0000303|PubMed:28376389};
GN   Name=verT {ECO:0000303|PubMed:28376389};
OS   Clonostachys rogersoniana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX   NCBI_TaxID=122658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=XZC04-CC-302;
RX   PubMed=28376389; DOI=10.1016/j.fgb.2017.03.007;
RA   Wang Y., Hu P., Pan Y., Zhu Y., Liu X., Che Y., Liu G.;
RT   "Identification and characterization of the verticillin biosynthetic gene
RT   cluster in Clonostachys rogersoniana.";
RL   Fungal Genet. Biol. 103:25-33(2017).
RN   [2]
RP   INDUCTION.
RX   PubMed=29058652; DOI=10.1099/mic.0.000557;
RA   Guo Z., Hao T., Wang Y., Pan Y., Ren F., Liu X., Che Y., Liu G.;
RT   "VerZ, a Zn(II)2Cys6 DNA-binding protein, regulates the biosynthesis of
RT   verticillin in Clonostachys rogersoniana.";
RL   Microbiology 163:1654-1663(2017).
CC   -!- FUNCTION: Thioredoxin reductase; part of the gene cluster that mediates
CC       the biosynthesis of 11'-deoxyverticillin A, one of the dimeric
CC       epipolythiodioxopiperazines (ETPs) from the verticillin family that act
CC       as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is required for
CC       normal conidiation (PubMed:28376389). The nonribosomal peptide
CC       synthetase verP is speculated to be responsible for condensation of
CC       amino acids to form the carbon skeleton of verticillin, whereas the
CC       cluster-specific tailoring enzymes are involved in further
CC       modifications leading to the production of 11'-deoxyverticillin A
CC       (Probable). {ECO:0000269|PubMed:28376389, ECO:0000305|PubMed:28376389}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:E9RAH5};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:E9RAH5};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28376389}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:E9RAH5}.
CC   -!- INDUCTION: Expression is regulated by the cluster-specific regulator
CC       verZ. {ECO:0000269|PubMed:29058652}.
CC   -!- DISRUPTION PHENOTYPE: Completely abolishes the 11'-deoxyverticillin A
CC       production. {ECO:0000269|PubMed:28376389}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; KY359203; AQZ42157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YHZ1; -.
DR   SMR; A0A1U9YHZ1; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..327
FT                   /note="Thioredoxin reductase verT"
FT                   /id="PRO_0000450170"
FT   BINDING         14..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   BINDING         36..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   BINDING         49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   BINDING         84
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   BINDING         287
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   BINDING         294..295
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT   DISULFID        142..145
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:E9RAH5"
SQ   SEQUENCE   327 AA;  35527 MW;  C43F3089C72F5B97 CRC64;
     MATPMIYDAL IIGGGPAGLA ASLALARVCR TSMLFDSGEY RNEGAKEMHT FLSRDGIPPH
     DFRATCLQQL EKYKDYAYVT NTKITDIANT DVAPGLKGFK AVDFTKKEFF GRKLVLATGT
     EDVLPTHIEG YKENWPVHIY QCPFCDGFER KSYPIGLLTF PNPSYSHLAL MLRPLNKDIT
     IYSNGPVPTD EPTQTALKMV LAAGVKLDER PVRRLINNGD GPENGISIEF TSGATVKLGM
     LYHRPPTRSR AANLILQLGL ETNAIGDVIT DTMMLKTNVP GCVSAGDTQE NMKQASVAAA
     TGTRAAASIV FQLADEDGKK ALAEAHL