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Database: UniProt
Entry: A0A1Y0FV89_9GAMM
LinkDB: A0A1Y0FV89_9GAMM
Original site: A0A1Y0FV89_9GAMM 
ID   A0A1Y0FV89_9GAMM        Unreviewed;       508 AA.
AC   A0A1Y0FV89;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:ARU27301.1};
GN   ORFNames=CBR65_07525 {ECO:0000313|EMBL:ARU27301.1};
OS   Cellvibrio sp. PSBB006.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU27301.1, ECO:0000313|Proteomes:UP000196143};
RN   [1] {ECO:0000313|EMBL:ARU27301.1, ECO:0000313|Proteomes:UP000196143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB006 {ECO:0000313|EMBL:ARU27301.1,
RC   ECO:0000313|Proteomes:UP000196143};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021382; ARU27301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0FV89; -.
DR   KEGG; cell:CBR65_07525; -.
DR   OrthoDB; 6278312at2; -.
DR   Proteomes; UP000196143; 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:UP000196143}.
FT   ACT_SITE        85
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         19..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         85
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"
FT   BINDING         353
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   508 AA;  57211 MW;  882DC8E057900753 CRC64;
     MAEELSEGKS ISDVLIVGGG TAGWMTAAAL ANVFSKTHCR IRLVESDQIG TVGVGEATIP
     VVLKFNQMLG IDEDDFLRST QGTFKLGIQF VNWGSLGNRY IHPFGSYGTP MGSLSFYHYW
     LKYHREGKSR DIGEFSIAVQ AALNGKFMRP ANMPNSPLSQ IAYAYHFDAG LYAQYLRSFS
     EKKGVERIEG EIVDVAIRPD DGFIESVNLK NGEKLSADLY IDCTGFRGLL IEQALNTGFI
     DWSHYLPCDR AVTVPSKNIG PPDSFTRATA HTAGWQWRIP LQHRTGNGHV YSSKYMRDEE
     AKDILLKNIE GDTLAEPKFI QFKTGMRQKF WNKNCVAIGL SSGFLEPLES TSIHLIQSSI
     AKLLALFPTA DFVQPVIDKY NQIMCSEFIG VRDFIILHYK ATDRSDSAFW NYCRHMDIPQ
     NLADKIELYK SSGRLFRDNN ELFDEISLIA VMHGQGIRAQ RYHPMVDDIN EIEFDRLMKE
     IKSVIDHSAQ AMPRHGDFIA KHCAAKFV
//
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