ID   A0A1Z9XF51_9ALTE        Unreviewed;       501 AA.
AC   A0A1Z9XF51;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:OUX88621.1};
GN   ORFNames=CBB95_07045 {ECO:0000313|EMBL:OUX88621.1};
OS   Alteromonas sp. TMED35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1986603 {ECO:0000313|EMBL:OUX88621.1, ECO:0000313|Proteomes:UP000196497};
RN   [1] {ECO:0000313|EMBL:OUX88621.1, ECO:0000313|Proteomes:UP000196497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED35 {ECO:0000313|EMBL:OUX88621.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) 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:OUX88621.1}.
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DR   EMBL; NHCO01000050; OUX88621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9XF51; -.
DR   Proteomes; UP000196497; 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}.
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         23..26
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         337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         346
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         350
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   501 AA;  56136 MW;  C5BD636B864145DB CRC64;
     MTALGLDSSN NQTPVKNVVI AGGGTAGWMA ATALSRLLGK SVSVTLVESK DIGIVGVGEA
     TIPPIRTFHK LLGIDEKAFM RATQATFKLG IEFENWREVN HSYIHSFGIT GRECWAGEFH
     HFWLRAQDYG FGGDFGDYCP ELIAAKQNKF ATSDAMPLNF AYHFDAVAYG RFLKSLACDA
     GVTHREGDIE KVTVCPNTGN IQALHLTNGE SIGGDFFIDC TGFKGLLIEQ ALHTGYDDWS
     HYLFCDRAVA MQTELTSPPV PYTKSVAHKA GWRWQIPLQE RMGNGLVYCS RFMSDQEAID
     TLKSQVSSTP INEPRVIRFT PGKRRRGWNK NCVALGLSSG FIEPLESTSI HLIMTGLIRL
     MRLFPFDGIT QSAVDEYNNK FDSEMSAILD FIVMHYKVTQ REDSPFWQQC QRMEIPASLT
     HKLDLFAQSG RVFLDDGDIF RVDSWTQVLM GQGMKPQQYH RVVDEMSEQS LKQFMAGLKL
     QVDNHVAKLP SHNAFLAQYL R
//