ID A0A0Q0FAF2_9GAMM Unreviewed; 497 AA.
AC A0A0Q0FAF2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Flavin-dependent tryptophan halogenase RebH {ECO:0000313|EMBL:KPZ55566.1};
DE EC=1.14.19.9 {ECO:0000313|EMBL:KPZ55566.1};
GN Name=rebH_2 {ECO:0000313|EMBL:KPZ55566.1};
GN ORFNames=AN393_01668 {ECO:0000313|EMBL:KPZ55566.1};
OS Pseudoalteromonas sp. P1-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1723758 {ECO:0000313|EMBL:KPZ55566.1, ECO:0000313|Proteomes:UP000050552};
RN [1] {ECO:0000313|EMBL:KPZ55566.1, ECO:0000313|Proteomes:UP000050552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-25 {ECO:0000313|EMBL:KPZ55566.1,
RC ECO:0000313|Proteomes:UP000050552};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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:KPZ55566.1}.
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DR EMBL; LKDW01000010; KPZ55566.1; -; Genomic_DNA.
DR RefSeq; WP_055017811.1; NZ_LKDW01000010.1.
DR AlphaFoldDB; A0A0Q0FAF2; -.
DR SMR; A0A0Q0FAF2; -.
DR PATRIC; fig|1723758.3.peg.1700; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000050552; 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 Oxidoreductase {ECO:0000313|EMBL:KPZ55566.1}.
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 12..15
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 332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 341
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 497 AA; 55600 MW; 6B79ADC287BEC8FA CRC64;
MKPIKHVVIA GGGTAGWITA ALLNKVLGKV IKITLIESST IGTIGVGEAT IPPIIQLNNA
LGINEQDFIN TTHASIKLGI EFENWKNTSH SYMHAFGSFG KDFPFCDFYN FWIKGKITGS
ENSLWDFSLN YQAAKKHKFA PLNTIPNTQL PGLSYAYHFD ATLYAEFLKN LAVARGVEHV
DAKIEQVEQC PLSGNIKSLT LDNSQQINGD LFIDATGQRA LLIEQTLNTG FVDWAHYLPC
DSAVAVQSKG TDELKPYTRS IAHSAGWQWQ IPLQSRIGNG LVYCSRYLSD DAATQLLLNN
LSAELITAPR VIKFKTGRRL KQWHRNVVSV GLASGFLEPL ESTSIHLIQS AVTRLIKLFP
HNGISDALVT EFNRQSVTEI EHIRDFIILH YKLTEREDSP FWRQCKQMDI PDSLAHKLEL
FKETGKVVRE NDELFAEVAW QQVFIGQGLI PEDYNSIVDS LSSEQLNDLF STLNTLITST
VEQLPTHKEF LAKIKKA
//
