ID A0A395JL93_9GAMM Unreviewed; 500 AA.
AC A0A395JL93;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:RBP49738.1};
GN ORFNames=DFR28_103163 {ECO:0000313|EMBL:RBP49738.1};
OS Arenicella xantha.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Arenicellales;
OC Arenicellaceae; Arenicella.
OX NCBI_TaxID=644221 {ECO:0000313|EMBL:RBP49738.1, ECO:0000313|Proteomes:UP000253083};
RN [1] {ECO:0000313|EMBL:RBP49738.1, ECO:0000313|Proteomes:UP000253083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24032 {ECO:0000313|EMBL:RBP49738.1,
RC ECO:0000313|Proteomes:UP000253083};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-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:RBP49738.1}.
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DR EMBL; QNRT01000003; RBP49738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395JL93; -.
DR InParanoid; A0A395JL93; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000253083; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000253083}.
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 14..17
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"
FT BINDING 347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 500 AA; 56074 MW; A749D5744753CB4F CRC64;
MTDKIINNVV IVGGGTAGWI SAALLVRMLG KTLNVTLVES DQIGTVGVGE ATIPPILTLN
QALGIDQADF MAKTNATIKL GIEFENWRKP GHKYMHAFGK LGKDFPFCGF EQLWLRGLKA
GYSSDFWDYS LNYQAAKQGK FALLDNIPKT DMQGLVYAFH FDAGLYANYL RELSERAGVT
RIEGKVKQVD RHTASGDITS LVLDDGRTVD GDLFIDCSGF RALLIGETLG VEYEDWRHWL
PCDSALAVQS EASLPVPPYT QSIAHSAGWR WRIPLTKRTG NGIVFSSQHM HEEEARQYLL
DSLDGAAITE PRLLRFTAGR RASQWHKNCV AIGLSSGFLE PLESTSIHLI QTAVIRLLKL
FPHAGIKATE VAEYNRQAAE EIEHVRDFII LHYHATERED SEFWRACRSM DIPDGLRHKI
ELFRQSGKVY NPTEALFSDV AWQQVMLGQG IVPNDYHPLA DAMSEAQLAE YHRNVKSIIK
QVVEKLPLHQ DFLDVVHRKS
//
