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
//