ID   A0A3R8N7S5_9CAUL        Unreviewed;       515 AA.
AC   A0A3R8N7S5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RRN63274.1};
GN   ORFNames=EIK80_15640 {ECO:0000313|EMBL:RRN63274.1};
OS   Caulobacter sp. 602-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN63274.1, ECO:0000313|Proteomes:UP000268773};
RN   [1] {ECO:0000313|EMBL:RRN63274.1, ECO:0000313|Proteomes:UP000268773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=602-1 {ECO:0000313|EMBL:RRN63274.1,
RC   ECO:0000313|Proteomes:UP000268773};
RA   Gao J., Sun J.;
RT   "The genome of Caulobacter sp 602-1.";
RL   Submitted (NOV-2018) 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:RRN63274.1}.
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DR   EMBL; RRYI01000005; RRN63274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R8N7S5; -.
DR   OrthoDB; 7178350at2; -.
DR   Proteomes; UP000268773; 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        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         12..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         81
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         340
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         349
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   515 AA;  56612 MW;  1539E7BA125CE5AF CRC64;
     MRRRRSILIV GGGTAGWLTA AYLAKALRVA DQGDLTITLL ESPDIGIVGV GEATFPTIRN
     TLRFLGVDEA RFIRETSATF KQGIRFVDWA ETPADGRHHS FFHPFEAPFS TEGASLAPYW
     LLQDEAGRAP FAEAVTIQAR VADAARAPKR PHESDFAGPL NYAYHFDAAK LAQVLAERAR
     ELGVRHLRGA LSETVLDETG AIARVVSPEH GDLTADLYID CSGFRAELIG KALGSPFKSA
     RPILFADRAL ACHTPYDRPD APIQSYTVAT AHEAGWTWDI GLAGARGVGC VYSSDHMDDA
     RAEAVLRDYL GGVEAETRRI RFDAGYRPKQ WIGNCVAVGL SAGFLEPLES TGVVLIEAAV
     AMIAELLPHN GPVSAPARRF NELMAARYDN IIVFLKLHYA LSRRQEPFWR QNADPASIPE
     RLAELLEQWR YRPPARFDFI LDLETFAFFN YQYILYGMGF KTDLAAGAGE FADVAGAARL
     FAKIRGFADR ATQDLPSHRD LIARINASGF ETEPA
//