IMQG_ASPFN
ID IMQG_ASPFN Reviewed; 247 AA.
AC B8NI24;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=O-methyltransferase imqG {ECO:0000303|PubMed:29182847};
DE EC=2.1.1.- {ECO:0000305|PubMed:29182847};
DE AltName: Full=Imizoquin biosynthesis cluster protein G {ECO:0000303|PubMed:29182847};
GN Name=imqG {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064290;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP INDUCTION, FUNCTION, AND PATHWAY.
RX PubMed=29182847; DOI=10.1021/acschembio.7b00731;
RA Khalid S., Baccile J.A., Spraker J.E., Tannous J., Imran M.,
RA Schroeder F.C., Keller N.P.;
RT "NRPS-derived isoquinolines and lipopetides mediate antagonism between
RT plant pathogenic fungi and bacteria.";
RL ACS Chem. Biol. 13:171-179(2018).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids
CC that serve a protective role against oxidative stress that are
CC essential for normal germination (PubMed:29182847). ImqB is a canonical
CC three-module NRPS that assembles the tripeptide backbone of the
CC imizoquins via condensation of Trp, Tyr, and Leu-derived precursors
CC (PubMed:29182847). N-methylation by imqF and phenol oxidation by imqC,
CC followed by cyclization via the FAD-dependent oxidase imqH carry out
CC the three-step transformation of L-tyrosine into tetrahydroisoquinoline
CC (PubMed:29182847). Importantly, this sequence requires the presence of
CC a free amine in the tyrosine moiety, indicating that isoquinoline
CC formation occurs prior to peptide bond formation (PubMed:29182847). The
CC imidazolidin-4-one ring of imizoquins could form following additional
CC oxidation of the methyl-derived bridgehead carbon by imqH
CC (PubMed:29182847). Lastly, O-methylation by imqG and leucine
CC hydroxylation by imqE complete biosynthesis of the imizoquins
CC (PubMed:29182847). {ECO:0000269|PubMed:29182847}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q40313};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:Q40313};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29182847}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q40313}.
CC -!- INDUCTION: Expression is down-regulated by ralstonins, lipopeptides
CC produced by the plant pathogenic bacteria Ralstonia solanacearum
CC (PubMed:29182847). Expression is positively regulated by the imizoquins
CC cluster-specific transcription regulator imqK (PubMed:29182847).
CC {ECO:0000269|PubMed:29182847}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; EQ963479; EED49608.1; -; Genomic_DNA.
DR RefSeq; XP_002379989.1; XM_002379948.1.
DR AlphaFoldDB; B8NI24; -.
DR SMR; B8NI24; -.
DR STRING; 332952.B8NI24; -.
DR EnsemblFungi; EED49608; EED49608; AFLA_064290.
DR VEuPathDB; FungiDB:AFLA_064290; -.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_8_0_1; -.
DR OMA; NYHNSHL; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..247
FT /note="O-methyltransferase imqG"
FT /id="PRO_0000444553"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 86..87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 190
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
SQ SEQUENCE 247 AA; 27359 MW; 4EAD63306D38DD6F CRC64;
MTATTTTTSQ IFVSEDYNQD PNWYAVDNYT LSHLQPPTRP NHASLHQTLE NSAKRGLEDI
SAFPTQAKFM ALQCQLGGVK HALEVGTLGG YTAIYIASLN PDIRIVSIEI DPKSAEVAKE
NIAAAGYQDR IEVLVGAAID LLPILQAKVE NGEQERFGFT FIDANKDNGW DYFDYAVKMS
RPRASIIVDN VVRAGKLVQE DYIKNDINVR GSRRTVENVG KDDRVDAVVL QTLSEKSYDG
FLMAVVK
