ID F7NRC3_9GAMM Unreviewed; 497 AA.
AC F7NRC3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:EGM79719.1};
GN ORFNames=Rhein_0179 {ECO:0000313|EMBL:EGM79719.1};
OS Rheinheimera sp. A13L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM79719.1, ECO:0000313|Proteomes:UP000004282};
RN [1] {ECO:0000313|EMBL:EGM79719.1, ECO:0000313|Proteomes:UP000004282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A13L {ECO:0000313|EMBL:EGM79719.1,
RC ECO:0000313|Proteomes:UP000004282};
RX PubMed=21742876; DOI=10.1128/JB.05636-11;
RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT Lake, India.";
RL J. Bacteriol. 193:5873-5874(2011).
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:EGM79719.1}.
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DR EMBL; AFHI01000001; EGM79719.1; -; Genomic_DNA.
DR RefSeq; WP_008897081.1; NZ_AFHI01000001.1.
DR AlphaFoldDB; F7NRC3; -.
DR STRING; 506534.Rhein_0179; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 5751025at2; -.
DR Proteomes; UP000004282; 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}.
FT ACT_SITE 81
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 81
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 338
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 342
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 497 AA; 56409 MW; EDF01EC37920568D CRC64;
MNNEQNRIKK VVIAGGGTAG WMTAAGLTKL LGKNLEVVLV ESDDIGTVGV GEATIPTMHI
FHRLLNIKES EVMAATNATF KLGIQFENWK TQGENYIHSF GFLGKDCWAC GFQHFWVKGK
QKGIASEIGD YCVEHLGARQ GRFAVTPNQD LNHAYHMDAS LYAKFLRRLS EQHGIKRIEG
KISEVQQHMD GSISALLLES GELIEGDLFI DCTGFRALLI EQTLNTGFED WSHWLPCDSA
YAVQTKTTQE PVAYTRAIAR DAGWQWKIPL QSRVGNGLVF CSKFITEAEA KQTLIDNVEG
EMLFEPRLIK FKTGTRRQHW NKNCVAIGLS SGFLEPLEST SIHLIQRSII RLLQAFPSDG
ILAAEVAEFN RQTKIEMDNI RDFIILHYKA TERTDTKFWR YCKAMDIPET LSHRMELFKQ
SGKVYKFAQE LFGESSWLQV LIGQGLMPQQ YHPIVDLMPD SELNDFLMSI KHNVKRTVSQ
FPTHHEFIQH YCKSSLV
//
