ILIC_HYPJQ
ID ILIC_HYPJQ Reviewed; 449 AA.
AC G0REX9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Cytochrome P450 monooxygenase iliC {ECO:0000303|PubMed:34947016};
DE EC=1.-.-.- {ECO:0000269|PubMed:34947016};
DE AltName: Full=Ilicicolin H biosynthesis cluster protein C {ECO:0000303|PubMed:34947016};
GN Name=iliC {ECO:0000303|PubMed:34947016}; ORFNames=TRIREDRAFT_58953;
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC 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). IliC
CC catalyzes the ring expansion of the tetramate intermediate to the
CC acyclic 2-pyridone intermediate that contains the trans bis-diene chain
CC (PubMed:34947016). The biosynthesis of ilicicolin H starts with
CC formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA
CC with the partnering trans-enoyl reductase iliB since iliA lacks a
CC designated enoylreductase (ER) domain. The cytochrome P450
CC monooxygenase iliC then catalyzes the ring expansion of the tetramate
CC to the acyclic 2-pyridone. The pericyclase iliD further converts the
CC acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might
CC then spontaneously convert to ilicicolin H since ilicicolin H is
CC produced in the absence of the epimerase iliE, in contrast to what was
CC observed for the Talaromyces variabilis ilicolin H biosynthetic pathway
CC (PubMed:34947016) (Probable). {ECO:0000269|PubMed:34947016,
CC ECO:0000305|PubMed:34947016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5S)-3-[(2E,4E,8S,10E,12Z)-1-hydroxy-4,8-dimethyltetradeca-
CC 2,4,10,12-tetraen-1-ylidene]-5-[(4-hydroxyphenyl)methyl]pyrrolidine-
CC 2,4-dione + O2 + reduced [NADPH--hemoprotein reductase] = 3-
CC [(2E,4E,8S,10E,12Z)-4,8-dimethyltetradeca-2,4,10,12-tetraenoyl]-4-
CC hydroxy-5-(4-hydroxyphenyl)-1,2-dihydropyridin-2-one + 2 H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:64552,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:155889, ChEBI:CHEBI:155890;
CC Evidence={ECO:0000269|PubMed:34947016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64553;
CC Evidence={ECO:0000269|PubMed:34947016};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:34947016}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; GL985060; EGR50064.1; -; Genomic_DNA.
DR RefSeq; XP_006963602.1; XM_006963540.1.
DR STRING; 51453.EGR50064; -.
DR EnsemblFungi; EGR50064; EGR50064; TRIREDRAFT_58953.
DR GeneID; 18486391; -.
DR KEGG; tre:TRIREDRAFT_58953; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_58953; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_27_0_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002974; Cyt_P450_E_CYP52.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR01239; EP450IICYP52.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..449
FT /note="Cytochrome P450 monooxygenase iliC"
FT /id="PRO_0000455713"
FT TRANSMEM 28..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 397
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 449 AA; 52419 MW; A714A39D23063B03 CRC64;
MVYSQLQALK RNYYLDWLRN LHKGKPKTFA ITFMGVKQIC TIEGENLKAI QATNFKDFGL
EPMRRKTKGA MPFADKGIST TDGKNWEFAR FLVKPFFYRE VYASIDRVDP YVRKLFGLLP
EEDGVTFDIQ PLIQRWFLDL TSEFIFGKTM DSMTYPDRAN ITWTMLDVLR GGRLRIQMYK
FLWAFNWNWW LKAVYEVHDF VNVHIRSTYK ELAAREQRIR DGLPVGPERV DLLWYMATHV
RDEEELRSQL CLVFVPNNDT TSIFISNCIW HLARDHEAWQ KLRKEVLDYG DQPITFESLR
SMPYLNGVLN ETHRLTPNNI VQVRACLNDS VLPLGGGPDG KSPLYVNKGD LVSVTKTVMY
RDPDIWGPDV DVFRPERFFG VRGNWNFLPF GGGPRRCPAQ MMVQTESAYM LFQLAKRYSR
LECRDPEPYT AVMRIGPSNI NGVKIAFYK
