ID A0A1M2V4W8_TRAPU Unreviewed; 574 AA.
AC A0A1M2V4W8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tryptophan 2-halogenase {ECO:0000313|EMBL:OJT02644.1};
GN ORFNames=TRAPUB_6825 {ECO:0000313|EMBL:OJT02644.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT02644.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT02644.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT02644.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJT02644.1}.
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DR EMBL; MNAD01001654; OJT02644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2V4W8; -.
DR OMA; RVIHSEH; -.
DR OrthoDB; 1599601at2759; -.
DR Proteomes; UP000184267; Unassembled WGS sequence.
DR GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR PANTHER; PTHR43747:SF1; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR Pfam; PF04820; Trp_halogenase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000184267}.
FT REGION 42..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 62029 MW; 9F7C668AFE963B71 CRC64;
MVLLVNAWNV VRSEFDHLLL QHAAACGAHV YEQTRVTDIH FEETPPSSPI HSHFDSPLSR
QCQDEHTSRP LPRRRTSAVE FALNDGPNAD GLGRPKSVSY ETAFGGTGEI TFDYLVDASG
RAGLMSTKYL KNRKFNASLK NVAVWGYWKN TGMYGQGTDR ENAPFFEALS DESGWAWFIP
LHKGLTSVGI VMDQKQLGIR SRASSSASGS PSLGSSVRRD TLSARTSSTL AERYLSFLEL
APGVLDLIGD GELVSLKTDE DQDDDADIPV ARSASDYSYS ASHYAGPGWR LVGDAGSFID
PFFSSGVHLA MTGALSAAAS IAASIRGDCP EADAAAWYSS RVSVSYTRFL IVVLSAYKQI
RCQSEGILAD VDEDNFDAAF AFLRPGQCGV ARFSAGLTNP HPAVIQGGAD MGARLSEDEV
QRALDFCVHL FDPTTPEQHE SARRKIELAS GLVGAAHDAA VPDADPLRLL DVRAPVVDPV
HLEQLLRRQL HLQENLPTSP SGTHGGLPRP PDIATQELSM VLNKVNARRV IHSEHGNGLN
SLEEEELAGY ALRLHCGELG LRRVGGEKGT GVQP
//
