ID A0A2S1JWW4_9GAMM Unreviewed; 503 AA.
AC A0A2S1JWW4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:AWF82873.1};
GN ORFNames=BTJ40_19755 {ECO:0000313|EMBL:AWF82873.1};
OS Microbulbifer sp. A4B17.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=359370 {ECO:0000313|EMBL:AWF82873.1, ECO:0000313|Proteomes:UP000244764};
RN [1] {ECO:0000313|EMBL:AWF82873.1, ECO:0000313|Proteomes:UP000244764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4B17 {ECO:0000313|EMBL:AWF82873.1,
RC ECO:0000313|Proteomes:UP000244764};
RX PubMed=16885309; DOI=10.1128/AEM.00494-06;
RA Peng X., Adachi K., Chen C., Kasai H., Kanoh K., Shizuri Y., Misawa N.;
RT "Discovery of a marine bacterium producing 4-hydroxybenzoate and its alkyl
RT esters, parabens.";
RL Appl. Environ. Microbiol. 72:5556-5561(2006).
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DR EMBL; CP029064; AWF82873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1JWW4; -.
DR KEGG; mii:BTJ40_19755; -.
DR OrthoDB; 6278312at2; -.
DR Proteomes; UP000244764; 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}.
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 13..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 79
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 343
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 503 AA; 56878 MW; 2C82BE8D1902794C CRC64;
MSSQRKKIII LGGGTAGWIT ANLMANHWQD KGFEITLVES PDIGIIGVGE GSTPPLKGFM
ETIGVSEAEW MPACNATYKV GITFRDWSVK PGFTEYVHPF VGQPDQFTIP AFFHNSFLRR
KGVELEGHPD HFFLATEMIR QKLSPVAPEN FPFEIAYGYH FDSGLLGQFL RRVAETKGVH
YKVATVAGAM LDAQGNIDHL KTTDGEVLKA DLYVDSSGFR GSLIQQSLKV PFISSAESLF
NDSAVVFATD QEKEYAPHTI STAMKYGWAW KIPLTNRNGN GYVYSSRFVD DDKAETEFRA
HLGLLNSDVE ARRLKFKVGR VAQHWAKNCL AVGLSQGFIE PLEATALDMV QETVVRFIEA
YNNGDHTDKF RDDFNNRISA RFDAVRDYIV CHYRISSRTD TDYWIVNGAN EKISPSLRSI
LMSWMAGKNI TDELLDQKLD VYFPNVSWNC LLTGKGIYPD QEQLRPGNEL AHKYKMEEIR
EFNRRCALNF MSHMDQLNQL RMG
//