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Database: UniProt
Entry: A0A285QZT1_9SPHN
LinkDB: A0A285QZT1_9SPHN
Original site: A0A285QZT1_9SPHN 
ID   A0A285QZT1_9SPHN        Unreviewed;       504 AA.
AC   A0A285QZT1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:SOB87403.1};
GN   ORFNames=SAMN06297144_2535 {ECO:0000313|EMBL:SOB87403.1};
OS   Sphingomonas guangdongensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1141890 {ECO:0000313|EMBL:SOB87403.1, ECO:0000313|Proteomes:UP000219494};
RN   [1] {ECO:0000313|EMBL:SOB87403.1, ECO:0000313|Proteomes:UP000219494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12672 {ECO:0000313|EMBL:SOB87403.1,
RC   ECO:0000313|Proteomes:UP000219494};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OBMI01000003; SOB87403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285QZT1; -.
DR   OrthoDB; 462203at2; -.
DR   Proteomes; UP000219494; 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:UP000219494}.
FT   ACT_SITE        79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         13..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         79
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         334
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         343
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         347
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   504 AA;  54624 MW;  C70550F3F85D6F4F CRC64;
     MSEPIRDVVI VGGGTAGWMM AAAAARFLAD GQRRITLVES EAIGTVGVGE ATIPPIREFL
     GLLGIPEAEF VAATGATMKL GIEFHGWGAP GERYIHPFGQ QGRDFDGIDF HMAWLKHRAA
     DGIGPLEDYW LSAVAARASR FAPPSADGRS PLSQLAYAYH FDASRFAAYL RRRAEDHGVV
     RVEGRITRVA HDGASGHVAQ LHLDGGRIVT GDLFIDCSGF RSLLLGDAMK VPFRDWTHWL
     PCDRAVAVPS ARTEPLLPLT RAIAHDAGWR WRIPLQHRTG NGLVYASGLL SDDAATARLL
     AALDGAAEGE PRTLSFRTGR RDRLWEGNVV ALGLAGAFLE PLESTSIHLI QSGIQKLFAL
     FPDRGFAPIL TQEYNRLMAA QIDAVRDFVI LHYSANGRVG EPFWDALRTM TLPDTLATRL
     ALFREKGRVL RYDDDLFSVA SWVAVLIGQG VMPTGYDPLV DALDDARVIA AMRELRGGYA
     RVAAQLPAHG AVVQELAARG AATG
//
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