ID   A0A2D6EBP6_9SPHN        Unreviewed;       501 AA.
AC   A0A2D6EBP6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:MAL27511.1};
GN   ORFNames=CL820_16795 {ECO:0000313|EMBL:MAL27511.1};
OS   Croceicoccus sp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=1927144 {ECO:0000313|EMBL:MAL27511.1, ECO:0000313|Proteomes:UP000231504};
RN   [1] {ECO:0000313|Proteomes:UP000231504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-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:MAL27511.1}.
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DR   EMBL; NZMY01000050; MAL27511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D6EBP6; -.
DR   Proteomes; UP000231504; 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        78
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         78
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         330
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         339
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         343
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   501 AA;  55557 MW;  29ACF79CCD150EBB CRC64;
     MDDTQQPTIL IAGGGTAGWM AAAALSRFAA GHRIVLVESD AIGTVGVGEA TIPQIHLFNS
     AIGLDEAEFL RETRGSFKLG IEFDGWLRDG HSYMHAFGQI GRGIGLLPFQ HYWLRARQLG
     FAKPLQRYSL NELAARTMRM QRGRTSAGAE MPYAYHFDAG LYAALLRRHA EARGVERHEG
     TMASVDRDGG SGDIASITLD DGRVLAADFF IDCTGFRGLL IEGALETGFD DWSNYLPCDR
     AMAVPCEGGG DFTPYTKSIA RKAGWQWRIP LQHRIGNGLV YSSAHLPDDE AAEMLLANLD
     GATQADPRPI RFTTGKRRKH WNRNCLALGL AAGFMEPLES TSIHLIQSAI SRFLALLPDG
     RPSEAAISHF NAQADFEWTR IRDFLILHYT ANERHGEPFW DAVRTMPLPS TLTDKIALWR
     DTGFIHREHE ELFTEVAWFQ VFAGQGVEAQ GHNPIADTLD EAQLRDLMQG TEAALVEQVR
     AMPRHIDFLQ DFINGRAKEP A
//