IFGH_PENRF
ID IFGH_PENRF Reviewed; 484 AA.
AC W6Q0S4;
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=Fumigaclavine B O-acetyltransferase ifgI {ECO:0000303|PubMed:28620689};
DE EC=2.3.1.205 {ECO:0000250|UniProtKB:Q4WZ64};
DE AltName: Full=Isofumigaclavine biosynthesis cluster B protein I {ECO:0000303|PubMed:28620689};
GN Name=ifgI {ECO:0000303|PubMed:28620689}; ORFNames=PROQFM164_S02g000302;
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: Fumigaclavine B O-acetyltransferase; 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=acetyl-CoA + fumigaclavine B = CoA + fumigaclavine A;
CC Xref=Rhea:RHEA:34267, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:67145, ChEBI:CHEBI:67146; EC=2.3.1.205;
CC Evidence={ECO:0000250|UniProtKB:Q4WZ64};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:28620689}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4WZ64}.
CC -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HG792016; CDM30153.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q0S4; -.
DR SMR; W6Q0S4; -.
DR EnsemblFungi; CDM30153; CDM30153; PROQFM164_S02g000302.
DR OrthoDB; 1130893at2759; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000030686; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 3: Inferred from homology;
KW Acyltransferase; Alkaloid metabolism; Transferase.
FT CHAIN 1..484
FT /note="Fumigaclavine B O-acetyltransferase ifgI"
FT /id="PRO_0000444547"
SQ SEQUENCE 484 AA; 53739 MW; 0AFC7D093301C8B3 CRC64;
MSTSFDHSVI LSPLDHIAPQ AYVSYLLSFQ TANSTHCLSL LEAGITRLTK VLPLLLGHIV
VNPELDGKYN IQSVQIPCTK EDRTILVHKH HPFPMESALG GVQSGMSMLE TSDSKQHLCP
LPPLIPSTER QPVIRFQANI FTDAIVLAMT FSHIVFDGTG AAKILALLGR CCRDPSVTPL
PLIIDEQDRA QSAIFAGLAD TSPAQDHTAE LGPAPAIHPV PLDAASLRTC RFEFNSERIL
QLKYQCSQVL KNACMFQPNS ASIPVADLPP FLSSNDVLTS ALADAIQRVK SQSKTYDCLD
LCMAVNMRGR IELSAAREFL GNMACNLRLK TPGPEYTGPE QCLSCRKTHD CPIQTDQLRF
LTDLACKVRN KVRNMDRKYF QSCMTYIANQ KDWSQTGMIF TDLAFSSWRH LDIYGLDFGD
SFGIVHNFDL SFGLIEGDVI FLPKRLTCDQ KEAGWDVHIT LPAKDLEALV KDDLIRWLMG
RDGE
