ILIB_NEOS2
ID ILIB_NEOS2 Reviewed; 381 AA.
AC P0DO31;
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=Trans-enoyl reductase iliB {ECO:0000303|PubMed:31216742};
DE EC=1.-.-.- {ECO:0000269|PubMed:31216742};
DE AltName: Full=Ilicicolin H biosynthesis cluster protein B {ECO:0000303|PubMed:31216742};
GN Name=iliB {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], FUNCTION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
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: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that
CC has potent and broad antifungal activities by inhibiting the
CC mitochondrial respiration chain (PubMed:31216742). IliB collaborates
CC with the hybrid PKS-NRPS synthetase iliA to assemble the backbone of
CC ilicicolin H (PubMed:31216742). The PKS portion of iliA and trans-
CC acting enoyl reductase iliB work together to construct an octaketide,
CC and two methyl groups are introduced by the MT domain of iliA during
CC the chain assembly (PubMed:31216742). The nascent chain is then
CC condensed with tyrosine, catalyzed by the iliA C domain, and the
CC resulting PKS-NRPS hybrid is offloaded by the iliA RED domain to form
CC an advanced tetramic acid intermediate (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 -!- CATALYTIC ACTIVITY:
CC Reaction=N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-
CC tetraenoyl]-L-tyrosyl-[ACP] = (3E,5S)-3-[(2E,4E,8S,10E,12Z)-1-
CC hydroxy-4,8-dimethyltetradeca-2,4,10,12-tetraen-1-ylidene]-5-[(4-
CC hydroxyphenyl)methyl]pyrrolidine-2,4-dione + H(+) + holo-[ACP];
CC Xref=Rhea:RHEA:64548, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16623,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:155890,
CC ChEBI:CHEBI:155893; Evidence={ECO:0000269|PubMed:31216742};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64549;
CC Evidence={ECO:0000269|PubMed:31216742};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31216742}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P0DO31; -.
DR SMR; P0DO31; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..381
FT /note="Trans-enoyl reductase iliB"
FT /id="PRO_0000453068"
FT BINDING 50..53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 145..152
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 213..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 278..279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 298..302
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 367..368
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 381 AA; 40275 MW; B319067A6D60A27D CRC64;
MALATPLPAT QAAVKVTGPS TVDVSAATTL PVLEAFEVLV RVACVSINHV DGKSADMSPT
PGATSGVDFS GLIVALGSKV DSDEFRANNN MRALSIGDRV FGGVFGNNPL RHDNGAFAEY
VAVPARLIWH MPAAMDFSTA ATIGATLATV GLALFQYLQV PMPSTQTISD SKTIPDPQQK
TRMALVYGGG TATGAMAIQV LKLAGFRPIT TCSPGSAARA MHLGAAATFD YRSPTCGADL
REHTANGLEL ALDCITDTAS MSICYEALGS AGGRYVALDA FPLRGHTRRS VAAEWVCTYT
QFGHAVAWVP PYNLDARPRD REIAEAWYVV AQQLVDEGLI EPYPKEDRTG GLAAVGEGMR
AVWKGEISGR KLAYPIAEEC Y
