IMQE_ASPFN
ID IMQE_ASPFN Reviewed; 364 AA.
AC B8NI22;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase imqE {ECO:0000303|PubMed:29182847};
DE EC=1.14.-.- {ECO:0000305|PubMed:29182847};
DE AltName: Full=Imizoquin biosynthesis cluster protein E {ECO:0000303|PubMed:29182847};
GN Name=imqE {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064270;
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: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC cluster that mediates the biosynthesis of imizoquins A to D,
CC tripeptide-derived alkaloids that serve a protective role against
CC oxidative stress that are essential for normal germination
CC (PubMed:29182847). ImqB is a canonical three-module NRPS that assembles
CC the tripeptide backbone of the imizoquins via condensation of Trp, Tyr,
CC and Leu-derived precursors (PubMed:29182847). N-methylation by imqF and
CC phenol oxidation by imqC, followed by cyclization via the FAD-dependent
CC oxidase imqH carry out the three-step transformation of L-tyrosine into
CC tetrahydroisoquinoline (PubMed:29182847). Importantly, this sequence
CC requires the presence of a free amine in the tyrosine moiety,
CC indicating that isoquinoline formation occurs prior to peptide bond
CC formation (PubMed:29182847). The imidazolidin-4-one ring of imizoquins
CC could form following additional oxidation of the methyl-derived
CC bridgehead carbon by imqH (PubMed:29182847). Lastly, O-methylation by
CC imqG and leucine hydroxylation by imqE complete biosynthesis of the
CC imizoquins (PubMed:29182847). {ECO:0000269|PubMed:29182847}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ963479; EED49606.1; -; Genomic_DNA.
DR RefSeq; XP_002379987.1; XM_002379946.1.
DR AlphaFoldDB; B8NI22; -.
DR SMR; B8NI22; -.
DR STRING; 5059.CADAFLAP00007852; -.
DR EnsemblFungi; EED49606; EED49606; AFLA_064270.
DR VEuPathDB; FungiDB:AFLA_064270; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_1_1; -.
DR OMA; IWPHTDF; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..364
FT /note="2-oxoglutarate-dependent dioxygenase imqE"
FT /id="PRO_0000444552"
FT DOMAIN 199..315
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 306
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 364 AA; 41194 MW; 9543168F484A9821 CRC64;
MTMLSDLPKI PTLDWADFAE GDTDQRLKLA QGLVQGFKRF GFVKLVNHGL SDELIQQLFA
EVKRFYRLPD ELKQKAAHPP GPNPQRGWSG IGVESTSKLY GEQTERPSGK LKDAKVGTDF
SSSKLSRELT HMKEHYDIGP PTDTQFPTRW PDEQDIPGWR AFMESYYARG QSFCLDLMEA
LEIGLELPKN TLRSMCIPDG SELRLLHYPE IPAAELRTGD TARIWPHTDF GLITLLFQDG
VGGLEVEDPL QQGHYIEVAR EQPYEMIVNV SATFERWMNG VIKAAVHRVN ITPEGKHVED
AVVPERWSAA YFFKAHKMAH AGPLPAFVTP ERPALYDNIT ALEFQKRRTD LVYTGQQLKV
EEAA
