IFGE_PENRF
ID IFGE_PENRF Reviewed; 261 AA.
AC W6QIM3;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Chanoclavine-I dehydrogenase ifgE {ECO:0000303|PubMed:28620689};
DE EC=1.1.1.- {ECO:0000269|PubMed:28902217};
DE AltName: Full=Isofumigaclavine biosynthesis cluster A protein E {ECO:0000303|PubMed:28620689};
DE AltName: Full=Short-chain dehydrogenase/reductase ifgE {ECO:0000303|PubMed:28620689};
DE Flags: Precursor;
GN Name=ifgE {ECO:0000303|PubMed:28620689};
GN Synonyms=FgaDH {ECO:0000303|PubMed:28902217};
GN ORFNames=PROQFM164_S05g000506;
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.
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
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 dehydrogenase; part of the gene cluster that
CC mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids
CC (PubMed:28620689, PubMed:28902217). The tryptophan
CC dimethylallyltransferase ifgA catalyzes the first step of ergot
CC alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP)
CC and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:28620689).
CC The second step is catalyzed by the methyltransferase ifgB that
CC methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-
CC L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-
CC tryptophan (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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=573 uM for chanoclavine-I (in absence of chanoclavine-I aldehyde
CC reductase fgaOx3) {ECO:0000269|PubMed:28902217};
CC KM=168 uM for chanoclavine-I (in presence of chanoclavine-I aldehyde
CC reductase fgaOx3) {ECO:0000269|PubMed:28902217};
CC KM=82 uM for NAD(+) (in absence of chanoclavine-I aldehyde reductase
CC fgaOx3) {ECO:0000269|PubMed:28902217};
CC KM=154 uM for NAD(+) (in presence of chanoclavine-I aldehyde
CC reductase fgaOx3) {ECO:0000269|PubMed:28902217};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000269|PubMed:28902217}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; HG792019; CDM36673.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QIM3; -.
DR SMR; W6QIM3; -.
DR STRING; 1365484.W6QIM3; -.
DR EnsemblFungi; CDM36673; CDM36673; PROQFM164_S05g000506.
DR OrthoDB; 1226147at2759; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000030686; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; NAD; Oxidoreductase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..261
FT /note="Chanoclavine-I dehydrogenase ifgE"
FT /id="PRO_0000444540"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 16..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
SQ SEQUENCE 261 AA; 27594 MW; 67F0AA382E74E620 CRC64;
MASVKSRVFA ITGGASGIGA ATSRLLAERG ATAVCVGDIS CKNFDELKES MKKINPATEV
HCSLLDVTSP TEVEKWVKSI VAKFGNLHGA ANIAGIAQGA GLRNSPTILE EGDEEWSKVL
KVNLDGVFYC TRAEVRAMKS LPSDDRSIVN VGSIAALSHI PDVYAYGTSK GASTYFTTCV
AADTFPFGIR VNSVSPGITD TPLLPQFIPK AKTSDEVKEV YRKEGFSVVK AGDVARTIVW
LLSEDSSPVY GANINVGASM P
