ID A0A3N5Y0N1_9ALTE Unreviewed; 521 AA.
AC A0A3N5Y0N1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RPJ67032.1};
GN ORFNames=DRW07_05665 {ECO:0000313|EMBL:RPJ67032.1};
OS Alteromonas sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=2259342 {ECO:0000313|EMBL:RPJ67032.1, ECO:0000313|Proteomes:UP000275281};
RN [1] {ECO:0000313|EMBL:RPJ67032.1, ECO:0000313|Proteomes:UP000275281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0105 {ECO:0000313|EMBL:RPJ67032.1,
RC ECO:0000313|Proteomes:UP000275281};
RA Ye M.-Q., Du Z.-J.;
RL Submitted (NOV-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:RPJ67032.1}.
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DR EMBL; RPOK01000002; RPJ67032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5Y0N1; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000275281; 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:UP000275281}.
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 16..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 82
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 348
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 521 AA; 58781 MW; DF11358B335627D9 CRC64;
MTSQIHPFRH LVIVGGGTAG WMAASLFQHA WARFGVEITV VESEKIGIIG VGEGSTPSLR
HFFRTLGIAE TEWMAQCHAT YKCGIHFPNW SSHLSQNAYF HPFYSELDWK SGSAFIYNAN
LRRKGYDVEA HPDYFWLQTK LAQGKRSPVS KQASGKELDY GYHFDSAKLG AYLKCRAIKL
GIRHINDTVV AVKRAKEGHV TQIQLARTGA LCGDMYLDCT GFQGLLIRQA LNADYVDFSS
QLLNDKAIAI PSSVPLKDKV ASQTTSTAMS NGWAWSIPLS NRVGNGYVYS SQHISDDSAE
AELRRHIGSN VSQGEARLIN MQLGRVEQHW YHNVLAVGLS QGFIEPLEAT AISCIQYTIE
RFIDIVDEAR TSGKEIASTH LQDKYNADIN RIFDAVKDYI TAHYRLNTRT DSQYWIDNRE
NQDHSSTLQA LLSGWDDPDT HFEKLVHDLD AQTMYLAPSW YCLFAGKGRF PRTLRSVPLD
TNYANAIDAS KYCQHQSTFF NDHKKQLLKT YGQHYPEPVT F
//