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Entry: A0A0G9HH59_9GAMM
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Original site: A0A0G9HH59_9GAMM 
ID   A0A0G9HH59_9GAMM        Unreviewed;       524 AA.
AC   A0A0G9HH59;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:APG05632.1};
GN   ORFNames=BJI69_18130 {ECO:0000313|EMBL:APG05632.1}, Y883_10435
GN   {ECO:0000313|EMBL:KLD66987.1};
OS   Luteibacter rhizovicinus DSM 16549.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG05632.1, ECO:0000313|Proteomes:UP000182987};
RN   [1] {ECO:0000313|EMBL:KLD66987.1, ECO:0000313|Proteomes:UP000035585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD66987.1,
RC   ECO:0000313|Proteomes:UP000035585};
RX   PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA   Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT   "A phylogenomic and molecular marker based taxonomic framework for the
RT   order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT   Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT   within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT   containing the genus Rhodanobacter and its closest relatives.";
RL   Antonie Van Leeuwenhoek 107:467-485(2015).
RN   [2] {ECO:0000313|EMBL:APG05632.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LJ96 {ECO:0000313|EMBL:APG05632.1};
RX   PubMed=28123952;
RA   Aamot H.U., Hofgaard I.S., Lysoe E.;
RT   "Complete genome sequence of Luteibacter rhizovicinus strain LJ96T,
RT   isolated from the rhizosphere of barley (Hordeum vulgare L.) in Denmark.";
RL   Genom Data 11:104-105(2016).
RN   [3] {ECO:0000313|Proteomes:UP000182987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017480; APG05632.1; -; Genomic_DNA.
DR   EMBL; JPLB01000030; KLD66987.1; -; Genomic_DNA.
DR   RefSeq; WP_046967682.1; NZ_JPLB01000030.1.
DR   AlphaFoldDB; A0A0G9HH59; -.
DR   STRING; 1440763.BJI69_18130; -.
DR   KEGG; lrz:BJI69_18130; -.
DR   PATRIC; fig|1440763.5.peg.1976; -.
DR   OrthoDB; 462203at2; -.
DR   Proteomes; UP000035585; Unassembled WGS sequence.
DR   Proteomes; UP000182987; Chromosome.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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         12..15
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         193
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         353
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         357
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   524 AA;  58644 MW;  784027A6AE8489B5 CRC64;
     MARLKKVLIV GGGTAGWLAA CYLAKAVNAV DPRSVQVHLV ESPDIGLLGV GEATFPSIRG
     TLAAIGLDER RFLVGATATY KQGIHYRHWV RPPGTPGPDH FFHPFNAPSQ RPGGPDLLPY
     WLLGAAPEGT SFADAVSMQS FLVDHSRAPK RPKDADYQGP MNHAFHFDAA CFARVLAEHG
     QETLGVVRHV ATVERTELDE HGAIARVVTK EEGELTADLY VDCTGLRGML IGNAMQSPFR
     SRADVLFADR AVAIQVPYET PDAPIPSYTI STAQEAGWVW DIGLQKRRGS GYVYSSRHTT
     DDRAEEVFRR YLGKAGEGLK AFHIKFETGY RPEHWRKNCV AVGLAGGFVE PLESTGIALI
     ELATYLLTHL LPGDTDDMES AARHFNEMMV ARYDRIIDFI KMHYCLSQRR DSPFWIDNTD
     PASIPQTLQE KLEKWKLRPP HRLDFVSDLE MFMTSSWQYV LYGMEFRTDL EPMRSAYPDM
     DVARKEFAVI RQAGSLALDD LPDHRAFVEQ MCREHRQRSE AVGV
//
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