VERK_CLORO
ID VERK_CLORO Reviewed; 179 AA.
AC A0A1U9YI11;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Gamma-glutamyl cyclotransferase verK {ECO:0000250|UniProtKB:E9R9Y3};
DE Short=GGCT verK {ECO:0000250|UniProtKB:E9R9Y3};
DE EC=4.3.2.9 {ECO:0000250|UniProtKB:E9R9Y3};
DE AltName: Full=Verticillin biosynthesis cluster protein K {ECO:0000303|PubMed:28376389};
GN Name=verK {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: Gamma-glutamyl cyclotransferase; part of the gene cluster
CC that mediates the biosynthesis of 11'-deoxyverticillin A, one of the
CC dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family
CC that act as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is
CC required for normal conidiation (PubMed:28376389). The nonribosomal
CC peptide synthetase verP is speculated to be responsible for
CC condensation of amino acids to form the carbon skeleton of verticillin,
CC whereas the 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 -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline +
CC an L-alpha-amino acid; Xref=Rhea:RHEA:20505, ChEBI:CHEBI:58402,
CC ChEBI:CHEBI:59869, ChEBI:CHEBI:71304; EC=4.3.2.9;
CC Evidence={ECO:0000250|UniProtKB:E9R9Y3};
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: Dicreases the production of 11'-deoxyverticillin
CC A. {ECO:0000269|PubMed:28376389}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; KY359203; AQZ42164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9YI11; -.
DR SMR; A0A1U9YI11; -.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06661; GGCT_like; 1.
DR InterPro; IPR017939; G-Glutamylcylcotransferase.
DR InterPro; IPR013024; GGCT-like.
DR PANTHER; PTHR12935; PTHR12935; 1.
PE 2: Evidence at transcript level;
KW Lyase.
FT CHAIN 1..179
FT /note="Gamma-glutamyl cyclotransferase verK"
FT /id="PRO_0000450166"
SQ SEQUENCE 179 AA; 19953 MW; 7889AA475FE5357D CRC64;
MTNTERSSSW KASSIPDQPM WYFGYGSNMK ASSMADRKVT PLSTKIVTVP THFVTFDIFG
IPYSEPSYAS LEQFPDGGTG KLDLVHHISR TQVLPACGVA HLLSPNDFHR LLVTEGSGVV
YNLVEVQAYE MNKDGQPIPA PFTVHTLKAK WPQRPNGTPS ARYMVRFLGL LSSSTYYQY