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Database: UniProt
Entry: A0A1H7MAD6_9SPHN
LinkDB: A0A1H7MAD6_9SPHN
Original site: A0A1H7MAD6_9SPHN 
ID   A0A1H7MAD6_9SPHN        Unreviewed;       496 AA.
AC   A0A1H7MAD6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:SEL07695.1};
GN   ORFNames=SAMN05216382_1420 {ECO:0000313|EMBL:SEL07695.1};
OS   Sphingomonas palmae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1855283 {ECO:0000313|EMBL:SEL07695.1, ECO:0000313|Proteomes:UP000199214};
RN   [1] {ECO:0000313|Proteomes:UP000199214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS21-1 {ECO:0000313|Proteomes:UP000199214};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNZZ01000002; SEL07695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7MAD6; -.
DR   STRING; 1855283.SAMN05216382_1420; -.
DR   OrthoDB; 462203at2; -.
DR   Proteomes; UP000199214; 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:UP000199214}.
FT   ACT_SITE        82
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         17..20
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         330
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         339
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         343
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   496 AA;  54392 MW;  236A5E0ED7F05E65 CRC64;
     MTDTDKPKPT RVVIAGGGTA GWIAAAALTR QLGKLIELTL VESDEIGTVG VGESTIPTAR
     GFHAFIGVDE AAFMRETQAT FKLGISFENW RRQGDAYFHP FGQVGRSVAI ADFQHFWLQA
     RAHGIAGGYG DYSLEQQAAA AGRFGLDAQG SLAYAYHLNA TDYARFLRGV AEGAGATRVE
     GRIERVELGE NGDIDALVLA SGTRIEGDLF IDCTGFRALL IEGALKTGYD DWSEWLATDR
     ALAVQTETVR APVPYTRAVA HGAGWRWQIP LQSRVGNGIV YSSAHMSDDE ARATLLAGLD
     GAPLFEPRPL RFTAGMRRRS WNRNCVALGL AGGFIEPLES TSIHLIMNAA TRLIQLFPFR
     GDDRSALAAR FNAQSRHEWE HVRDFIILHY VVTERDDTPF WRERRAMNIP DTLAERIALF
     TESAGAWQGQ DDLFRIDSWI AVMLGQGITP TAHHRVASLL GAEALKGSLS DLTRLIAATV
     QMLPTHARFL QHYCPA
//
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