ILIB_HYPJQ
ID ILIB_HYPJQ Reviewed; 350 AA.
AC G0REX7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Trans-enoyl reductase iliB {ECO:0000303|PubMed:34947016};
DE EC=1.-.-.- {ECO:0000269|PubMed:34947016};
DE AltName: Full=Ilicicolin H biosynthesis cluster protein B {ECO:0000303|PubMed:34947016};
GN Name=iliB {ECO:0000303|PubMed:34947016}; ORFNames=TRIREDRAFT_58289;
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, CATALYTIC ACTIVITY, AND PATHWAY.
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: 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:34947016). IliB collaborates
CC with the hybrid PKS-NRPS synthetase iliA to assemble the backbone of
CC ilicicolin H (PubMed:34947016). 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:34947016). 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: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 -!- 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:34947016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64549;
CC Evidence={ECO:0000269|PubMed:34947016};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:34947016}.
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 EMBL; GL985060; EGR50063.1; -; Genomic_DNA.
DR RefSeq; XP_006963601.1; XM_006963539.1.
DR STRING; 51453.EGR50063; -.
DR EnsemblFungi; EGR50063; EGR50063; TRIREDRAFT_58289.
DR GeneID; 18486266; -.
DR KEGG; tre:TRIREDRAFT_58289; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_58289; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_1_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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; Reference proteome.
FT CHAIN 1..350
FT /note="Trans-enoyl reductase iliB"
FT /id="PRO_0000455712"
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 177..180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 242..243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 262..266
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 331..332
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 350 AA; 37205 MW; 9B95FD6B31D6BCC2 CRC64;
MTVIDVLPQT QRALKIVGPN AVSVNAAAPL PDIEPTDVLV RVVCVSINPV DGKAADMSPQ
LGATSGTDFS GVVVALGADV EADNWREANT MKPVRIGDRV FGGIFGNDPL RPHNGAFADY
VAVPARLVWH IPTGTDFATA ATMGAAIATV GLSLFNYLGL PLPSKSKAGL PVVTTCSAAS
STNVLQLGAE AWFDYKSPTC GADIREHTND SLAFALDCIT DTASMGICYE ALGSAGGRYV
ALDAFPVRGH TRRSVVPEWV CTPTQFGKAI RWTPPYDLEP RPYDLKCAEL WYVVAQRLID
EGLIASHPLE KRNGGLSAVP EGMEEVRRGQ IKGKKLVYTI LDSEPIAVSA
