ID   A0A0M9Y961_9ACTN        Unreviewed;       501 AA.
AC   A0A0M9Y961;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KOU35942.1};
GN   ORFNames=ADK54_36165 {ECO:0000313|EMBL:KOU35942.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU35942.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC       Bacterial tryptophan halogenase subfamily.
CC       {ECO:0000256|ARBA:ARBA00038396}.
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:KOU35942.1}.
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DR   EMBL; LGDD01000328; KOU35942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9Y961; -.
DR   PATRIC; fig|1415557.3.peg.7973; -.
DR   Proteomes; UP000037774; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   InterPro; IPR033856; Trp_halogen.
DR   PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR   PANTHER; PTHR43747:SF4; FLAVIN-DEPENDENT TRYPTOPHAN HALOGENASE; 1.
DR   Pfam; PF04820; Trp_halogenase; 2.
DR   PIRSF; PIRSF011396; Trp_halogenase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR011396-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR011396-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011396-2}.
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         60
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         344
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         348
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   501 AA;  56658 MW;  CDDD479337C51FC2 CRC64;
     MTASYLKAAF GDRINVTLVE SGHVGAVGVG EATFSDIRHF FEFLGLKEKD WMPACNATYK
     LAVRFENWRE KGHYFYHPFE QMRSVNGFPL TDWWLQQGPT DRFDKDCFVM ASVIDAGLSP
     RRLDGTLIDQ PFDEGADEMQ GLTMSEHQGK TQFPYAYQFE AALLAKYLTK YSVERGVKHI
     IDDVKQVNLD DRGWISGVTT AEHGDISGDL YIDCTGFRAL LINKALDEPF ISYADTLPND
     SAVALQVPMD MEKRGIMPCT TATAQDAGWI WTIPLMGRVG TGYVYAKDYL SPEDAERTLR
     EFVGPAAADV SANHIKMRIG RSRNSWVNNC VAVGLSSGFV EPLESTGIFF IHHAIEQIAK
     NFPNEDWNPN QRVLYNRSIA HVMDGIREFL VLHYVAAKRQ DTQYWRDTKT RAIPDSLAER
     LEMWKTQVPD SESIFPYYHG LPAYSYMCVL LGMGGIEMKP SPALALSDPS AAEREFAAIR
     DKTRRLTETL PKAYEYFAQH H
//