ID   EFUL_HORCR              Reviewed;         312 AA.
AC   A0A2Z4HPZ5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Reductase efuL {ECO:0000303|PubMed:30051576};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30051576};
DE   AltName: Full=Enfumafungin biosynthesis cluster protein L {ECO:0000303|PubMed:30051576};
GN   Name=efuL {ECO:0000303|PubMed:30051576};
OS   Hormonema carpetanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Dothioraceae; Hormonema.
OX   NCBI_TaxID=284138;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=30051576; DOI=10.1111/1462-2920.14333;
RA   Kuhnert E., Li Y., Lan N., Yue Q., Chen L., Cox R.J., An Z., Yokoyama K.,
RA   Bills G.F.;
RT   "Enfumafungin synthase represents a novel lineage of fungal triterpene
RT   cyclases.";
RL   Environ. Microbiol. 20:3325-3342(2018).
CC   -!- FUNCTION: Reductase; part of the gene cluster that mediates the
CC       biosynthesis of enfumafungin, a glycosylated fernene-type triterpenoid
CC       with potent antifungal activity, mediated by its interaction with beta-
CC       1,3-glucan synthase and the fungal cell wall (PubMed:30051576). The
CC       pathway begins with the terpene cyclase-glycosyl transferase fusion
CC       protein that most likely uses 2,3-oxidosqualene as substrate and
CC       catalyzes glycosylation immediately after cyclization (Probable). The
CC       fernene glycoside then could be processed by the desaturase efuI which
CC       catalyzes isomerization of a double bond established by efuA to form
CC       the core structure (Probable). The latter would then undergo a series
CC       of hydroxylations in unknown order at C-2, C-19, C-23 and C-25, which
CC       would be catalyzed by two of the three cytochrome P450 monooxygenases
CC       efuB, efuG or efuH (Probable). The hydroxy-group at C-25 becomes
CC       oxidized by the dehydrogenase efuE to enable a spontaneous, non-
CC       enzymatic hemiacetal formation with C-23 (Probable). After
CC       hydroxylation at C-2, acetylation by the acetyltransferase efuC takes
CC       place (Probable). The final steps in enfumafungin biosynthesis require
CC       expansion of the 5-membered ring by lactonization via a Baeyer-Villiger
CC       reaction mediated by one of the BGC's cytochrome P450 monooxygenases
CC       (efuB, efuG or efuH) followed by ring cleavage (Probable). This type of
CC       reaction would establish a double bond between C-20 and C-21 which
CC       could be reduced by the reductase efuL to form the final product
CC       (Probable). {ECO:0000269|PubMed:30051576, ECO:0000305|PubMed:30051576}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:30051576}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; MF611894; AWW17222.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05259; PCBER_SDR_a; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   InterPro; IPR045312; PCBER-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; NADP; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..312
FT                   /note="Reductase efuL"
FT                   /id="PRO_0000454466"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         11..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O81355"
FT   BINDING         47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         138
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   312 AA;  34665 MW;  AC84BEAAA49FCB89 CRC64;
     MSQTKNIIIF GGTGVIGKYI TSAILASKES FDRVALFTSA STVSNKKEQL EEWKHQGLDI
     IVGDLTKDDD VLSAYRSFDT VVSAVGRNVI AEQINLIRLA EATPNITRFF PSEYGTDIEY
     NPQTSPHEKP HQLKLKVRKY IREEVRRLDV TYLVTGPYAD LYLGNSNNAE YGSFDTKAKK
     ATLLGSGEDP VSFTTMKDVG KLLVAALKHP EESKNKALKV NSFTATPNEI LAEFEKQTGG
     QKWDVEYTSL AKLTELEKKA WEEGNPAATV YTLRRIWTEG GTLYKKRDNA LIDAEETDSL
     AQAIAQVVDS QA