ID   IMQH_ASPFN              Reviewed;         478 AA.
AC   B8NI25;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Amino acid oxidase imqH {ECO:0000303|PubMed:29182847};
DE            EC=1.5.3.- {ECO:0000305|PubMed:29182847};
DE   AltName: Full=Imizoquin biosynthesis cluster protein H {ECO:0000303|PubMed:29182847};
DE   Flags: Precursor;
GN   Name=imqH {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064300;
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: Nonribosomal peptide synthetase; part of the gene cluster
CC       that 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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O43029};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29182847}.
CC   -!- SUBUNIT: Dimer. {ECO:0000250|UniProtKB:O43029}.
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 MSOX/MTOX family. {ECO:0000305}.
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DR   EMBL; EQ963479; EED49609.1; -; Genomic_DNA.
DR   RefSeq; XP_002379990.1; XM_002379949.1.
DR   AlphaFoldDB; B8NI25; -.
DR   SMR; B8NI25; -.
DR   STRING; 5059.CADAFLAP00007855; -.
DR   EnsemblFungi; EED49609; EED49609; AFLA_064300.
DR   VEuPathDB; FungiDB:AFLA_064300; -.
DR   eggNOG; KOG2820; Eukaryota.
DR   HOGENOM; CLU_007884_0_1_1; -.
DR   OMA; CDHAFKF; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961; PTHR10961; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Oxidoreductase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..478
FT                   /note="Amino acid oxidase imqH"
FT                   /id="PRO_0000444554"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   478 AA;  52382 MW;  309C38837B8E5530 CRC64;
     MPAPKSIIIV GSGVFGLSTA HAMSQNNEFA SSKITLIDSW NFEPSGPSAS APNPSAANFD
     TSRIIRSDYS HRTYATLARE AQQKWKADWG ADGRYRNQSI VMIGEGHSMK QPMKALESIN
     YVKHAYAQSY ERAGRNSDIV HILDSESAVW EALGLGTPDE ASKAGPNASE LRGYRNHNCG
     WAESGATMAW LRQKTIHSDR IDIHIGQVVG LRVCSDSPSE SHVNAEPRVC GVILDDGSQL
     TADLTVLAAG AMTPRLLGSP TLCDVYSETV AYVQLTEMER RELVRREFPL IVNVARKIFA
     IGPDNQGFLK LARFSWSGYR DVQKFAGVDV GPRSQAAPQE EDGYGACGDL DQTKLSPDVE
     STLQDYRGFL RELFRSGDGG DLGGLRNIAT RPFAQVRRCW YADTVSTDFI VDYHPAYGKS
     LFIATGGSDH AFKFLPVLGE RICELILQSD NGKAGPSESI QELQRLWKFP GGDSHAKL