ID   I3I5T8_9GAMM            Unreviewed;       502 AA.
AC   I3I5T8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:EIK43423.1};
GN   ORFNames=O59_003821 {ECO:0000313|EMBL:EIK43423.1};
OS   Cellvibrio sp. BR.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK43423.1, ECO:0000313|Proteomes:UP000003395};
RN   [1] {ECO:0000313|EMBL:EIK43423.1, ECO:0000313|Proteomes:UP000003395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR {ECO:0000313|EMBL:EIK43423.1,
RC   ECO:0000313|Proteomes:UP000003395};
RA   Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL   Submitted (MAY-2012) 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:EIK43423.1}.
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DR   EMBL; AICM01000009; EIK43423.1; -; Genomic_DNA.
DR   RefSeq; WP_007645109.1; NZ_JH668205.1.
DR   AlphaFoldDB; I3I5T8; -.
DR   STRING; 1134474.O59_003821; -.
DR   PATRIC; fig|1134474.3.peg.3641; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_022247_1_0_6; -.
DR   OrthoDB; 6278312at2; -.
DR   Proteomes; UP000003395; 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         78
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         332
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         341
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         345
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   502 AA;  56242 MW;  A3F7501D77AFDC71 CRC64;
     MNSIKKIVIL GGGVSGWIAA SMLAAQVRRD LCEIELIESE DIGSVGVGES TIPPVVRLIT
     SLGIDEEDFI RETQACYKLG IKFVDWRSKN QSYFHPYGAL GQRIGTQDFY QCWLKATMAG
     GDYPLQDFSP CSVMAAQGRF FLPAQAMNTP IGGAGYAIHL DAKLVAAYLR RYAEARGVVR
     SEGNYVAVER RDNGFISALV LADGRKIEGD FFVDCSGFRA LLIDGAMAAG FEDWAQYLPC
     DRAIVVKTGA AGSRMPYTTA TARKAGWSWR IPLRNATGHG YVYSSRFCSD TEAKSTLLGN
     LDAPRINDPR LISFKAGRRL EFWKNNCLAL GLAGGFVEPL ESTAIHLIAR GMDYFLRFFP
     DLECEPSLRR EYNRRMAADY QEVRDFIVLH YCTSERSDSD FWRWCQTMPL PDSLRERIEL
     FKGHGIVREE RDELFRSASW QSVFEGMGIR PAKYSPRVDN IELAQINENL KLARSAILNM
     VKTLPTHDDY LAGRFGVPVV DQ
//