ID   A0A143HRB8_9GAMM        Unreviewed;       497 AA.
AC   A0A143HRB8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:AMX04265.1};
GN   ORFNames=A3224_13675 {ECO:0000313|EMBL:AMX04265.1};
OS   Microbulbifer thermotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX04265.1, ECO:0000313|Proteomes:UP000076077};
RN   [1] {ECO:0000313|Proteomes:UP000076077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA   Lee Y.-S., Choi Y.-L.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP014864; AMX04265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143HRB8; -.
DR   STRING; 252514.A3224_13675; -.
DR   KEGG; mthd:A3224_13675; -.
DR   OrthoDB; 6278312at2; -.
DR   Proteomes; UP000076077; Chromosome.
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:UP000076077}.
FT   ACT_SITE        79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         14..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         79
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         186
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         334
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         343
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         347
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   497 AA;  55904 MW;  2F7450ACC432823B CRC64;
     MRDGSIKKLV ILGGGTAGWM TAALAAKVLG KVIDITLVES DRIGTVGVGE ATIPPIIHFN
     RALGIDEREF LTATKGTIKL GIQFENWLRR GDSYMHAFGS IGKNLAFCDF HHIWNRSRLR
     GDTSSFWDYS LNYQAAINNK FAPLTHIQGT NLPGISYAYH FDAGLYAQFL RRYSEGRGVK
     RIEGMVKEVR VRSDNGFIQG LLLESGLEID GDLFVDCTGM AALLIEKTLG VGYEAWSQWL
     PCDRAMAVPS ASAKPIVPYT RSIAHEAGWQ WRIPLQHRTG NGLVYSSKHW SDDRAREALM
     SNLDGEPLAE PRVIPFRTGR RGEQWCRNVV SIGLSSGFLE PLESTSIHLI QTAATRLMKM
     FPHRGIRAEE VAEFNRQSRV EIEHIRDFII LHYKANQRRD SDFWRDCEAM GVPDTLSEKV
     ELFRRTGKVF RDYDDLFSEA AWQQVMIGQG IVPEDYHPVA DALSEEQLGD LMASLRTMID
     GTVNSLPEHE QYLPNVG
//