IFGC_PENRF
ID IFGC_PENRF Reviewed; 629 AA.
AC W6R4D7;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=FAD-linked oxidoreductase ifgC {ECO:0000303|PubMed:28620689};
DE EC=1.-.-.- {ECO:0000305|PubMed:28620689};
DE AltName: Full=Isofumigaclavine biosynthesis cluster A protein C {ECO:0000303|PubMed:28620689};
DE Flags: Precursor;
GN Name=ifgC {ECO:0000303|PubMed:28620689}; ORFNames=PROQFM164_S05g000510;
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: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids
CC (PubMed:28620689). The tryptophan dimethylallyltransferase ifgA
CC catalyzes the first step of ergot alkaloid biosynthesis by condensing
CC 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:28620689}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; HG792019; CDM36677.1; -; Genomic_DNA.
DR AlphaFoldDB; W6R4D7; -.
DR SMR; W6R4D7; -.
DR STRING; 1365484.W6R4D7; -.
DR EnsemblFungi; CDM36677; CDM36677; PROQFM164_S05g000510.
DR OrthoDB; 827142at2759; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000030686; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD 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; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..629
FT /note="FAD-linked oxidoreductase ifgC"
FT /id="PRO_5004880373"
FT DOMAIN 122..325
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 629 AA; 69862 MW; 5613AF72421E3E36 CRC64;
MMFHFLGTAG LGIALSWLVF THFLQSSCRC QPWEPCWPSD EQWELLNRSM EFTLVRLQPI
ASVCYNHSLD HTLCEDVMRM SRDSGWRASQ PGALQDWVWE SGQSPGDACP LGSQMNGHTQ
CHQGRIPLYS AMVNSTKHVQ EAVMFAKRHD LRLIIRNTGH DLAGRSSSPN ALQIHTHRLQ
DIKFHDNVQL HGFEKSFGPA VSVGAGVMMG DLYARSAQNG YIVVGGDCPT VGVVGGFLQG
GGISDFLSLH HGLAVDNVLE FEVVTASVSL PEPDAIQYCG FLTLRQGDIV LANAIRNPDL
FWALRGGGGG TFGIVTRATM RVFPDVPAIA AELGVQTSQS HGEYSRSLAA FFTVLQSLNR
ENVGGQLIIT VISEHSIEAK LKMFFLNQTN TADVDQRMQP FVEDMRRIET HVTYESTSLP
KLSMNYRQVP DIHTDNDYGV LGSTVAISND LFNASKGPAY VADGLAQLPT RPGDLLFTSN
LGGQVMRNGD LMETSMHPAW RNATQLINFV RPVEPTIEGK AGALQNLTNI HMPLLYAIDP
RFRLSYRNVG DPNEKDFQQV YWGQSYARLL QLKRRWDREG LLISKLGVGS EEWDSEGMCR
TGRRSLENLA IDTLSSLAHL IHVTYRCIW
