ID   VERI_CLORO              Reviewed;         428 AA.
AC   A0A1U9YHZ6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Aminotransferase verI {ECO:0000250|UniProtKB:Q4WMJ9};
DE            EC=2.6.1.- {ECO:0000250|UniProtKB:Q4WMJ9};
DE   AltName: Full=Verticillin biosynthesis cluster protein I {ECO:0000303|PubMed:28376389};
GN   Name=verI {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: Aminotransferase; part of the gene cluster that mediates the
CC       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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P00509};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28376389}.
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-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; KY359203; AQZ42161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YHZ6; -.
DR   SMR; A0A1U9YHZ6; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..428
FT                   /note="Aminotransferase verI"
FT                   /id="PRO_0000450164"
FT   MOD_RES         254
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00509"
SQ   SEQUENCE   428 AA;  47334 MW;  79647C300BE27CA7 CRC64;
     MLSRRARESN AWFLERFKRP LGRQGSKSNT NIDLATAENW LIRPEILSAL KRNLQADFQS
     SHLSYAPGLG GTPELLSAIS TFFNHFFSPT IPVAPEHIVT GAGCSSVLDT LINDICDDGD
     GLLVAAPYWG SFEVSSVLRN GVTLIPVQIK FHESHSAQGI VDAYRKAMEN TSCKVRGLLF
     CNPHNPWGHI LSVEVIDALL LFCEQADIHF VSDEIYALST FGRMELPSGN LEHGEKFLSP
     ATSFVSVLSR DLIKLGGCLI TQANKELRMS QAILNNAKLC NAASAMVAPI LGSTSQLSTL
     VNLNVQRMRK AARTAIQFAQ FHGLTFCEPV AGVYIWLRLS EDCHTRDDEE EIVQRCTKHG
     ALVGSGSDYS ESQPGWFRLT FAIPDNEFLE GLNRIETAMG YKERFNGEMV QSSLGGFVSQ
     LWKRFVLV