ILIE_NEOS2
ID ILIE_NEOS2 Reviewed; 766 AA.
AC P0DO34;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=NADH-dependent flavin oxidoreductase iliE {ECO:0000303|PubMed:31216742};
DE EC=1.-.-.- {ECO:0000269|PubMed:31216742};
DE AltName: Full=Epimerase iliE {ECO:0000303|PubMed:31216742};
DE AltName: Full=Ilicicolin H biosynthesis cluster protein E {ECO:0000303|PubMed:31216742};
GN Name=iliE {ECO:0000303|PubMed:31216742};
OS Neonectria sp. (strain DH2).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria;
OC unclassified Neonectria.
OX NCBI_TaxID=1735992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RX PubMed=31216742; DOI=10.3390/molecules24122267;
RA Lin X., Yuan S., Chen S., Chen B., Xu H., Liu L., Li H., Gao Z.;
RT "Heterologous expression of ilicicolin H biosynthetic gene cluster and
RT production of a new potent antifungal reagent, ilicicolin J.";
RL Molecules 24:0-0(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:31216742). 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:31216742) (Probable).
CC {ECO:0000269|PubMed:31216742, ECO:0000305|PubMed:31216742}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P0DO34; -.
DR SMR; P0DO34; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Glycoprotein; Membrane; NADP; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..766
FT /note="NADH-dependent flavin oxidoreductase iliE"
FT /id="PRO_0000453071"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 551..622
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..64
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 143
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 224..227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 385..386
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 766 AA; 83902 MW; E94B1E40BFA03673 CRC64;
MSEQLGSHIT TPSSHDDASK DKRPAAEVVN GSGIFIMADL HTGKPITLKC GLTLPNRLVK
AATAESMAPN NTLPDEKFQN LYRHWAEGGW GMVLAGNVQV DANHICTATD LSVDHSLSDS
KIVEAWRPWA AACNGNGTVT VMQLCHPGRQ SPAGAGKRGL FAKSIAPSAV ALQMGSGLVA
KAVTALLFGT PREMSVSDIE TVVSQFARSA RLAAESGFAG VEVHAGHGFL LEQFLSTKSN
RRTDAYGGTP AKRARIVVEV LTAIRAVVPA GFCVGLSLNS VDLQSQTELK DCVEQVKLIT
DAGVDFIEVS GGTFENPTMF LGPEKSRKQA QLGQPLAHEP FFLDFAKAIR PHVPGVPLIV
TGGFRSCQGI EETIAGGDAD LVGLARPAVV NPLLPKTTVL SPKTTEFGPE IEDGDVTLYA
KKTEAPWILK QIGIRAVEVH IDNSVYHNRR HAAKQVRRAS VLLQFPSRPS LSVAAVDIDN
VISRLSTARP FVFIFLAITV EVNIDTDIAA LLLALRPSPE LYHLAAAMPP RRSDGSADHD
VPDWPKTPHP TPYDILAMRK DDPYTKHRFF QLVKIYHPDR HGHTPAVHRL PHATRLERYR
LIVAANDLLS NPSKRSLYDT QGVGWTGDRP PTLNESVRHA EKSWRHQPGN ASRNATWEDW
ERWYDARDGK TRDPMYMSNG VFATLVVMMC MIGAFAQMSR AEQSGTEYLE TRDQSNLAIG
QQISRTTLVS AGRSKDERVD SFLRERENVA YEFTPSKYDD RTRTEA
