ID   IMQC_ASPFN              Reviewed;         223 AA.
AC   B8NI20;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=FAD-dependent monooxygenase imqC {ECO:0000303|PubMed:29182847};
DE            EC=1.-.-.- {ECO:0000305|PubMed:29182847};
DE   AltName: Full=Imizoquin biosynthesis cluster protein C {ECO:0000303|PubMed:29182847};
GN   Name=imqC {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064250;
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: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of imizoquins A to D, tripeptide-derived
CC       alkaloids that serve a protective role against oxidative stress that
CC       are essential for normal germination (PubMed:29182847). ImqB is a
CC       canonical three-module NRPS that assembles the tripeptide backbone of
CC       the 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   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29182847}.
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 PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963479; EED49604.1; -; Genomic_DNA.
DR   RefSeq; XP_002379985.1; XM_002379944.1.
DR   AlphaFoldDB; B8NI20; -.
DR   SMR; B8NI20; -.
DR   STRING; 5059.CADAFLAP00007850; -.
DR   EnsemblFungi; EED49604; EED49604; AFLA_064250.
DR   VEuPathDB; FungiDB:AFLA_064250; -.
DR   eggNOG; KOG3855; Eukaryota.
DR   HOGENOM; CLU_1239882_0_0_1; -.
DR   OMA; CLEVIRC; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..223
FT                   /note="FAD-dependent monooxygenase imqC"
FT                   /id="PRO_0000444551"
FT   BINDING         139..141
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
FT   BINDING         189
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
FT   BINDING         210
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
SQ   SEQUENCE   223 AA;  25367 MW;  E5634B522C36BE5B CRC64;
     MIENLRKRST IEVEWRKQPV HMDIDLDQVD NPEAYPITVS VETSKDGSDP GLLWQPMHAE
     RDSIVKETIH AKYVLGCDGA RSWIRQRLGV SFIGDLTDST WGVMDIVPKT SFPDIRKVAV
     IHSSKGTVMS VPREDKLVRF YIQIDAVNPN AASGLARRDL KVEDLLDAAR AIMFPYTMEA
     AECAWWSAYR VGQRVANEFA RHDRIFLAGD SVREYCLEVI RCQ