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Database: UniProt
Entry: A0A1G4RY14_9CAUL
LinkDB: A0A1G4RY14_9CAUL
Original site: A0A1G4RY14_9CAUL 
ID   A0A1G4RY14_9CAUL        Unreviewed;       506 AA.
AC   A0A1G4RY14;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:SCW61617.1};
GN   ORFNames=SAMN02927928_2237 {ECO:0000313|EMBL:SCW61617.1};
OS   Asticcacaulis taihuensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=260084 {ECO:0000313|EMBL:SCW61617.1, ECO:0000313|Proteomes:UP000199150};
RN   [1] {ECO:0000313|EMBL:SCW61617.1, ECO:0000313|Proteomes:UP000199150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3431 {ECO:0000313|EMBL:SCW61617.1,
RC   ECO:0000313|Proteomes:UP000199150};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMTS01000003; SCW61617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4RY14; -.
DR   STRING; 260084.SAMN02927928_2237; -.
DR   OrthoDB; 5695497at2; -.
DR   Proteomes; UP000199150; 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        79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         14..17
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         338
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         347
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         351
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   506 AA;  56763 MW;  C3C6EAE8C057212D CRC64;
     MTNPPIKTIT IVGGGTAGWM TAALLSKLLM GRYDITLIES EEIGTIGVGE ATIPAIKVFN
     EMLEVNEAEF LKATQGTFKL GIEFVGWRDG PHDPADSYIH GFGKIGIDRL WLHTHQFWLK
     MREKGAVKHF DHYAICCAAA RKGRFTPPDP RRGPPVSDLD YAYHFDASLY ARYLRTLSEG
     RGVKRIEGRI TQVNLRPEDG FIDTLTLQNG HSIGGDLFID CSGMRGLLIG EALGIDYEDW
     NEWLLCDRAY AVPSVNPAQI TPYVTCTTRD AGWQWRIPLQ HRTGNGYVHS SGYTDDQTAV
     DTLMSTLGGP ALAEPRLVKF RPGKRHKSWE KNCVAIGLSG GFLEPLESTS IHLIQTGILR
     LLSLFPGQGF NAADISEYNT YTDDEYRDIR DFIIAHYKVT NREDTPFWKY LKHMPVPESL
     ARKLDLFRSS ARFFKRGAFE LFREESWVQV LLGQGMTAGY DPNVDLLSEA EMIGFLRDIE
     AVIDGNVNAM PTHDAYIARY CPAPKV
//
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