ID A0A397NR86_9SPHN Unreviewed; 502 AA.
AC A0A397NR86;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:RIA37697.1};
GN ORFNames=DFR49_3584 {ECO:0000313|EMBL:RIA37697.1};
OS Hephaestia caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Hephaestia.
OX NCBI_TaxID=645617 {ECO:0000313|EMBL:RIA37697.1, ECO:0000313|Proteomes:UP000266568};
RN [1] {ECO:0000313|EMBL:RIA37697.1, ECO:0000313|Proteomes:UP000266568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25527 {ECO:0000313|EMBL:RIA37697.1,
RC ECO:0000313|Proteomes:UP000266568};
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 (AUG-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:RIA37697.1}.
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DR EMBL; QXDC01000004; RIA37697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397NR86; -.
DR OrthoDB; 462203at2; -.
DR Proteomes; UP000266568; 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:UP000266568}.
FT ACT_SITE 77
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 77
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 342
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 502 AA; 55250 MW; 6EB825521847E375 CRC64;
MTERATRVVI LGGGTAGWMT AAAIARLLPQ VELRLIESAD IGIVGVGEAT LPHLRAFVET
LGIDEAEFMR TTSATYKLGI AFEGFGRIGA TYTHPFGGFG SDLAGVGFHH YWRRMHAAGR
ARDIGAYSYP VVLAAARKFA RPTPDGDPIT STYGYAYQFD ATRFAPYLRD YAIARGAVRT
EGKVVRVEQH PETGDVTALH LESGEAVTGD LFIDCSGFRS LLLGDTLKTP WEDWSHWLPC
DRAAALPCES PEGDIEPLTR AIAMPFGWRW RIPLQHRVGN GYVYSSAHLS DDDACAAIVG
AVEGKPIASP RVLRFRAGRR RLGWVKNVVA IGLSSGFLEP LESTSLYLAQ AAITQLIELF
PEDGRSTDAD RDEFNRVIDL EHDRIRDFLI LHYHATTRDD SDFWNHVRTM RVPYSLHEKI
AMFRASGRVA RYTKGLFLEP SWVAVYLGQG IIPERWDQRA DLADEAQLDR ALAGLDRALG
AAAARTPGHR EALAAHHAGA PA
//