ID   ILIE_HYPJQ              Reviewed;         401 AA.
AC   G0REX8;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=NADH-dependent flavin oxidoreductase iliE {ECO:0000303|PubMed:34947016};
DE            EC=1.-.-.- {ECO:0000269|PubMed:34947016};
DE   AltName: Full=Epimerase iliE {ECO:0000303|PubMed:34947016};
DE   AltName: Full=Ilicicolin H biosynthesis cluster protein E {ECO:0000303|PubMed:34947016};
GN   Name=iliE {ECO:0000303|PubMed:34947016}; ORFNames=TRIREDRAFT_76204;
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a;
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=34947016; DOI=10.3390/jof7121034;
RA   Shenouda M.L., Ambilika M., Cox R.J.;
RT   "Trichoderma reesei Contains a Biosynthetic Gene Cluster That Encodes the
RT   Antifungal Agent Ilicicolin H.";
RL   J. Fungi 7:0-0(2021).
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:34947016). The
CC       biosynthesis of ilicicolin H starts with formation of the tetramic acid
CC       by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl
CC       reductase iliB since iliA lacks a designated enoylreductase (ER)
CC       domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring
CC       expansion of the tetramate to the acyclic 2-pyridone. The pericyclase
CC       iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H.
CC       8-epi-ilicicolin H might then spontaneously convert to ilicicolin H
CC       since ilicicolin H is produced in the absence of the epimerase iliE, in
CC       contrast to what was observed for the Talaromyces variabilis ilicolin H
CC       biosynthetic pathway (PubMed:34947016) (Probable).
CC       {ECO:0000269|PubMed:34947016, ECO:0000305|PubMed:34947016}.
CC   -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC       family. {ECO:0000305}.
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DR   EMBL; GL985060; EGR50287.1; -; Genomic_DNA.
DR   RefSeq; XP_006963789.1; XM_006963727.1.
DR   EnsemblFungi; EGR50287; EGR50287; TRIREDRAFT_76204.
DR   GeneID; 18488589; -.
DR   KEGG; tre:TRIREDRAFT_76204; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_76204; -.
DR   eggNOG; KOG0134; Eukaryota.
DR   HOGENOM; CLU_012153_6_2_1; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; Reference proteome.
FT   CHAIN           1..401
FT                   /note="NADH-dependent flavin oxidoreductase iliE"
FT                   /id="PRO_0000455715"
FT   BINDING         25..28
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         188..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P54550"
FT   BINDING         346..347
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P54550"
SQ   SEQUENCE   401 AA;  43473 MW;  0F69775C09474282 CRC64;
     MAELHASLPI TLRCGLTLPN RLVKASMSEG ISAAGSLPDM KIRNIYQRWA KGGWGMVITG
     NVQVDDRYLG TANDLAVDSR ASDDTIVASW SRWAKVCRQH GTPTLVQLNH PGRQCPIGAG
     THGYLSKNVA PTSIGLHMGD GLIPKAVSAI AFGKPRELEI AEIRTITQQF ARAARLAYRS
     GFAGVEIHAA HGYLIDEFLT ERTNRRSDAY GGSTERRAKF LIDIISAVRS EVPSSFCVGV
     TINSVDSVFP EILVDRVRQL ELVTSAGVDF IEISGGTFED PLMFLGPPKP SSSANMEHSE
     AYFVDFAKVV ASKFPDVPLL LTGGFRCRES IEKAVTNGAC SMVGIARPAA VNPLLPKTVM
     FNHEVKDSDA TLYSPKIEAP WLIRQMGITA LSVHMDNVSS F