ICCG_TALVA
ID ICCG_TALVA Reviewed; 406 AA.
AC A0A482NAR8;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=NADH-dependent flavin oxidoreductase iccG {ECO:0000305|PubMed:30905148};
DE EC=1.-.-.- {ECO:0000305|PubMed:30905148};
DE AltName: Full=Ilicicolin H biosynthesis cluster protein G {ECO:0000303|PubMed:30905148};
GN Name=iccG {ECO:0000303|PubMed:30905148};
OS Talaromyces variabilis (Penicillium variabile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX NCBI_TaxID=28576;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=HXQ-H-1;
RX PubMed=30905148; DOI=10.1021/jacs.9b02204;
RA Zhang Z., Jamieson C.S., Zhao Y.L., Li D., Ohashi M., Houk K.N., Tang Y.;
RT "Enzyme-catalyzed inverse-electron demand Diels-Alder reaction in the
RT biosynthesis of antifungal ilicicolin H.";
RL J. Am. Chem. Soc. 141:5659-5663(2019).
CC -!- FUNCTION: NADH-dependent flavin oxidoreductase; part of the gene
CC cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-
CC pyridonealkaloid that has potent and broad antifungal activities by
CC inhibiting the mitochondrial respiration chain (PubMed:30905148). IccA
CC to iccE are sufficient for ilicicolin H biosynthesis and the roles of
CC the remaining enzymes, iccF, iccG and iccH within the pathway have
CC still to be determined (PubMed:30905148). The biosynthesis of
CC ilicicolin H starts with formation of the tetramic acid by the hybrid
CC PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB
CC since iccA lacks a designated enoylreductase (ER) domain. The
CC cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of
CC the tetramate to the acyclic 2-pyridone. The pericyclase iccD further
CC converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the
CC epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via
CC epimerizationd (PubMed:30905148) (Probable).
CC {ECO:0000269|PubMed:30905148, ECO:0000305|PubMed:30905148}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30905148}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; MK539848; QBQ83711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482NAR8; -.
DR SMR; A0A482NAR8; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; NADP; Oxidoreductase.
FT CHAIN 1..406
FT /note="NADH-dependent flavin oxidoreductase iccG"
FT /id="PRO_0000449010"
FT BINDING 24..27
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 180..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 338..339
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
SQ SEQUENCE 406 AA; 44044 MW; 979B847AD30C3102 CRC64;
MDLNLAKPIT LRCGITLPNR LWKAAMTEEF ADKRRLPGSE ACLATYRVWA NGGWGLVMTG
NVDVDPAYLG SPGNIAVDSS IPREKTLAAW RAWAEACSQN GAKAIVQINH PGRQASFTKS
IAPSAVPLNL GPGILPWMLR SLIYGTPREM TVDEIHDVIM KFAETARLAA DAGFAGVEIH
AAHGYLLAQF LSAASNKRTD AYGGSAKARA KIVIDIIHAI RSDVPKTFCV GIKFNSTDHQ
SETEMKDCLE QLHLISDAGV DFLEISGGTF ENPTFNLGVS DQKAKVSTQT REAFFVDFAK
SIRSELSGLP LMVTGGFRTR QGMETALVED SCDVVGIARP AVLSPYLPRN IIFNRDVVDA
EAIAHAEKID TPTIAKWMGI KAIGVGAETI WYIKKIQNLG SIETEL
