ID   A0A1H8L5X6_9BURK        Unreviewed;       517 AA.
AC   A0A1H8L5X6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:SEO00554.1};
GN   ORFNames=SAMN05428959_104141 {ECO:0000313|EMBL:SEO00554.1};
OS   Duganella sp. CF517.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEO00554.1, ECO:0000313|Proteomes:UP000198691};
RN   [1] {ECO:0000313|Proteomes:UP000198691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FODC01000004; SEO00554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8L5X6; -.
DR   STRING; 1881038.SAMN05428959_104141; -.
DR   OrthoDB; 8868802at2; -.
DR   Proteomes; UP000198691; 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; 1.
DR   PIRSF; PIRSF011396; Trp_halogenase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR011396-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR011396-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011396-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198691}.
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         19..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         88
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         353
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         357
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   517 AA;  56744 MW;  2896C5855A5E065E CRC64;
     MGSTDTHGGA IRRIVIVGGG TAGWMAAAPL AQRLARHPTE PCEVTLVESP EIGTIGVGEA
     TLPTIRAYNE ALGLDGADFV AKTQASFKLG IEFKDWGHVG NRFFHAFGDF GPVLAGVGAH
     QHWLRLAQAF NSMPDIENWS VPSVMARHGK FSPPKDDQPG VTDAYSYGFH FDASLYAKYL
     RDYAVARGAR RLEGMIVEVE QHPQSGFVTA VKLQDGRRIE GDLFIDCSGF RGLLIEGALK
     AGYEDWSAYL PCNSAQAVPC ASVAQLTPYT RSTAKQAGWL WRIPLQHRTG NGHVYSDGFT
     SDEQARRVLL DGLDGAALDE PRQLRFTTGR RRKSWVKNVV AIGLSAGFVE PLESTSINLI
     EMAVGKLLEL FPDRDCAPAL ADEFNRFMGI RYESVRDFII LHYKLTKRDD SEFWRYCADM
     AIPDALRHQI ELFRETGRVA IVDRGGFAEP SFVAMMMGLG VMPKRYDPLA DRVDLRAVHG
     HFAGLRDLIA QTVARMPDHG AYVAGQAKSG AASRVAA
//