ID   A0A437JCC2_9SPHN        Unreviewed;       509 AA.
AC   A0A437JCC2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RVT43578.1};
GN   ORFNames=ENE74_02870 {ECO:0000313|EMBL:RVT43578.1};
OS   Sphingobium algorifonticola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=2008318 {ECO:0000313|EMBL:RVT43578.1, ECO:0000313|Proteomes:UP000282977};
RN   [1] {ECO:0000313|EMBL:RVT43578.1, ECO:0000313|Proteomes:UP000282977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TLA-22 {ECO:0000313|EMBL:RVT43578.1,
RC   ECO:0000313|Proteomes:UP000282977};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVT43578.1}.
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DR   EMBL; RZUL01000001; RVT43578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437JCC2; -.
DR   OrthoDB; 7178350at2; -.
DR   Proteomes; UP000282977; 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:UP000282977}.
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         19..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         84
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         339
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         348
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         352
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   509 AA;  55489 MW;  580FA1FAB15E106B CRC64;
     MEAENGRGRR IGQVVILGGG TAGWMTATAL ARTLGRSVAI TLLESEEIGT VGVGEATIPT
     IHWFNDLIGL DEAAFVAATQ ASFKLGIEFV DWARPGHRYF HPFGQYGVAF PGVPFHHRWL
     KAQRDGLDLP LDAFSLASQL AKDNRFAKPV SEARSILSTL GYAYHFDAGL YARHLRGLAE
     AMGVRRVEGK LGAIAQDPQN GFITAITTQA GERLDGDLFI DCSGFRALLI EGVMQAGFED
     WSHWLPCDRA VAVPCARVAD TTPYTRSTAR SAGWQWRIPL QHRTGNGYVY ASAFLSDDEA
     AATLLAGLDG EALADPRFLR FTAGRRRRAW VKNVVAIGLS SGFLEPLEST SIHLIQSGIA
     KLLTLFPDAD CDPGLADRFN LLLDRDMDNI KDFLILHYHA TADKPEPLWQ HCRAMVLPDT
     LVAREAHYRA TGRIMIETDE LFREASWLAV LNGQGILARD YSPIADTLEA PANRTQLEQI
     AALIARAVPT LPRHDAAIAA LTGGGRAAA
//