IFGG_PENRF
ID IFGG_PENRF Reviewed; 375 AA.
AC W6Q2D7;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Chanoclavine-I aldehyde reductase ifgG {ECO:0000303|PubMed:28620689};
DE EC=1.3.1.100 {ECO:0000250|UniProtKB:Q4WZ70};
DE AltName: Full=Isofumigaclavine biosynthesis cluster B protein G {ECO:0000303|PubMed:28620689};
DE AltName: Full=Old yellow enzyme homolog ifgG {ECO:0000303|PubMed:28620689};
DE Short=OYE ifgG {ECO:0000303|PubMed:28620689};
GN Name=ifgGI {ECO:0000303|PubMed:28620689}; ORFNames=PROQFM164_S02g000300;
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164;
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=28620689; DOI=10.1007/s00253-017-8366-6;
RA Fernandez-Bodega A., Alvarez-Alvarez R., Liras P., Martin J.F.;
RT "Silencing of a second dimethylallyltryptophan synthase of Penicillium
RT roqueforti reveals a novel clavine alkaloid gene cluster.";
RL Appl. Microbiol. Biotechnol. 101:6111-6121(2017).
RN [3]
RP FUNCTION.
RX PubMed=28902217; DOI=10.1039/c7ob02095c;
RA Gerhards N., Li S.M.;
RT "A bifunctional old yellow enzyme from Penicillium roqueforti is involved
RT in ergot alkaloid biosynthesis.";
RL Org. Biomol. Chem. 15:8059-8071(2017).
CC -!- FUNCTION: Chanoclavine-I aldehyde reductase; part of the gene cluster
CC that mediates the biosynthesis of isofumigaclavines, fungal ergot
CC alkaloids (PubMed:28620689). The tryptophan dimethylallyltransferase
CC ifgA catalyzes the first step of ergot alkaloid biosynthesis by
CC condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-
CC dimethylallyl-L-tryptophan (PubMed:28620689). The second step is
CC catalyzed by the methyltransferase ifgB that methylates 4-
CC dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine,
CC resulting in the formation of N-methyl-dimethylallyl-L-tryptophan
CC (PubMed:28620689). The catalase ifgD and the FAD-dependent
CC oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan
CC to chanoclavine-I which is further oxidized by ifgE in the presence of
CC NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC (PubMed:28902217). The chanoclavine-I aldehyde reductases ifgG and/or
CC fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde
CC that spontaneously dehydrates to form 6,8-dimethyl-6,7-
CC didehydroergoline (PubMed:28620689, PubMed:28902217). The festuclavine
CC dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-
CC dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689).
CC Hydrolysis of festuclavine by a yet undetermined cytochrome P450
CC monooxygenase (called ifgH) then leads to the formation of
CC isofumigaclavine B which is in turn acetylated by ifgI to
CC isofumigaclavine A (PubMed:28620689). Penicillium roqueforti has
CC interestingly at least two sets of genes for the consumption of
CC chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3
CC and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689,
CC PubMed:28902217). The reason for the duplication of these genes is
CC unclear, probably to ensure the conversion of chanoclavine-I aldehyde
CC by differential gene expression under various environmental conditions
CC (PubMed:28902217). {ECO:0000269|PubMed:28620689,
CC ECO:0000269|PubMed:28902217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydrochanoclavine-I aldehyde + NADP(+) = chanoclavine-I
CC aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:35947, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65032,
CC ChEBI:CHEBI:71487; EC=1.3.1.100;
CC Evidence={ECO:0000250|UniProtKB:Q4WZ70};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q4WZ70};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:28620689}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; HG792016; CDM30151.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q2D7; -.
DR SMR; W6Q2D7; -.
DR STRING; 1365484.W6Q2D7; -.
DR EnsemblFungi; CDM30151; CDM30151; PROQFM164_S02g000300.
DR OrthoDB; 978998at2759; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000030686; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; Flavoprotein; FMN; NADP; Oxidoreductase.
FT CHAIN 1..375
FT /note="Chanoclavine-I aldehyde reductase ifgG"
FT /id="PRO_0000444541"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:W6Q9S9"
FT BINDING 31..33
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 66
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 176
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 228
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 325..326
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 326
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
SQ SEQUENCE 375 AA; 41775 MW; 49DE340BBAF92B4F CRC64;
MTIIPKHPSP TLFKPLALGK CQLQHRIVMS PTTRYRADEA AVPLPFVKEY YAQRASDPGA
LLITEATNIC PNSVGEAHIP GIWSKTQCEA WREVVSQVHA KECYIFCQIY ATGRSADPEL
LASRGFEQVS SSAVAAEPGC QPPRALDEEE IQKYISDYAQ AARNAIEVGF DGVEIHGANG
YLIDQFTQAS CNQRTDEWGG DIPNRARFAL QVTMAVINAI GPDRVGMKLS PWSQYSGMGI
MGDLVPQFEY LILQLRQLGI AYLHLANSRW LDQMTTHPDP NHLTFVKVWG RSLPVILAGG
YDATSAPEVI EMVYADYDNV AIGFGRYFTS TPDLPFRMKN GIALQKYDRS SFYTCLTKTG
YLDYPYSPEY LCRSS
