ID A0A137QID4_9AGAR Unreviewed; 534 AA.
AC A0A137QID4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Tryptophan 2-halogenase {ECO:0000313|EMBL:KXN87001.1};
GN ORFNames=AN958_09344 {ECO:0000313|EMBL:KXN87001.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN87001.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN87001.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN87001.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + FADH2 + melleolide F + O2 = 6'-chloromelleolide F +
CC FAD + H(+) + 2 H2O; Xref=Rhea:RHEA:67160, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:167712,
CC ChEBI:CHEBI:167713; Evidence={ECO:0000256|ARBA:ARBA00036433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67161;
CC Evidence={ECO:0000256|ARBA:ARBA00036433};
CC -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC {ECO:0000256|ARBA:ARBA00005706}.
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DR EMBL; KQ962301; KXN87001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QID4; -.
DR OrthoDB; 1599601at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR PANTHER; PTHR43747:SF1; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04820; Trp_halogenase; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249}.
SQ SEQUENCE 534 AA; 58544 MW; BB63289E4AFD7723 CRC64;
MLPPFATVLV VGGGPAGSYA SAVLAQEGVD VVCCEAAHFP RYHIGESLLA SVKAYLQMVD
VVEKIDQHGF HPKVGSAIKF RPDRPEAYTG FIAVNPNNGA WNVDRSQFDH LLLNHAVEKG
AKVFQGARIS NVQFSNDNCH SAQWTRDDKT GVISFNYIID CSGRQGILST KLFRNRHFNQ
SLKNIATWTY WKGETGVYGR GTRREGAIFI EGLVNGLKGW VWYIPLADKV SVGVVMHESD
NTALRRDSND LKDHYMRALS HSPDVMEMLK GAAICDEIHM ASDYSYSATK YAGPGWRLAG
DAGAFIDPFF SSGVHLALNG GLSSAISVLA SIRKDVSEEA AAAYHDKKVS MAYTRFLLVV
LSAYKQLRHQ DADVLSDVAS GDFDTAFDIM RPVIQGLGDV EASHDRTLTE EALEKTMDFV
ASVLTTPFDE VASARESGYV PAHLFDRNGD LLGPEQIAKL VTDTGADEKT ERALRSINAR
KTLKLYDPKS NFENEEVLGM VAHLQRGSFG LRTVDLKPVV ASISGVWVGH IQNI
//