ID   A0A0X3UBA0_9GAMM        Unreviewed;       478 AA.
AC   A0A0X3UBA0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KUJ84016.1};
GN   ORFNames=AVO43_07125 {ECO:0000313|EMBL:KUJ84016.1};
OS   Microbulbifer sp. ZGT114.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=1685377 {ECO:0000313|EMBL:KUJ84016.1, ECO:0000313|Proteomes:UP000054457};
RN   [1] {ECO:0000313|EMBL:KUJ84016.1, ECO:0000313|Proteomes:UP000054457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT114 {ECO:0000313|EMBL:KUJ84016.1,
RC   ECO:0000313|Proteomes:UP000054457};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUJ84016.1}.
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DR   EMBL; LQBR01000002; KUJ84016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3UBA0; -.
DR   STRING; 1685377.AVO43_07125; -.
DR   Proteomes; UP000054457; 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:UP000054457}.
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         167
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         315
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         324
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   478 AA;  54143 MW;  B6B86D5FE9E470A8 CRC64;
     MTASLMVKVL GKSLNITLVE SDKIGTVGVG EATIPPIINF NQALGINERD FLKATRGTIK
     LGIQFENWLR QGDSYMHAFG SIGKNFPFCD FHHFWRRSRA SGDESSLWDY SLNYQAAIHN
     KFAHLAQIKG TNLPGISYAY HFDAGLYAQY LRNYSESKGV GRIEGTVKSV QVRPQDGFVE
     SLLLEDGQSV SGDLFVDCTG LAALLIEKTL GVGFEGWSQW LPCDRAMAVP SAGSKPIVPY
     TRSIAHAAGW QWRIPLQHRT GNGIVYSSRH WSDDEAREVL MKNLDGEALA EPRVIPFRTG
     RREKQWDRNV VSIGLSSGFL EPLESTSIHL IQSAATRLIK SFPHQGIKPE EVSEFNRQSQ
     VEIERIRDFI ILHYKLNERR DSEFWRECES MSIPQTLEHK IELFRRTGKV FRDYDDLFTE
     VAWQQVMIGQ GIFPQDHHTI ADNLSEEQLR DLMGSLRTLI DGTVKSLPDH EKFLASLN
//