ID   A0A136I295_9ALTE        Unreviewed;       522 AA.
AC   A0A136I295;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KXJ62023.1};
GN   ORFNames=AXW14_17575 {ECO:0000313|EMBL:KXJ62023.1};
OS   Alteromonas sp. Nap_26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ62023.1, ECO:0000313|Proteomes:UP000070342};
RN   [1] {ECO:0000313|Proteomes:UP000070342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) 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:KXJ62023.1}.
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DR   EMBL; LSMP01000025; KXJ62023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136I295; -.
DR   Proteomes; UP000070342; 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        87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT   BINDING         18..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         87
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         360
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   522 AA;  58510 MW;  D6961A47A33F54A9 CRC64;
     MKESHFQAPL TSIVVAGGGA AGWLTAAILA AEHNIKNNDR VSVTLVESPD VKILGVGEGT
     WPTMRDTLRK IGISEADFIA SCDASFKQGT RFINWKSTES ENIYDHPFSL PAGFFEGEVG
     AWWLSHGHQH QKSTFSEMFS TQSLLCNFSK APKQVQTPPY AAVANYGYHL DAHKFAELLK
     THCIERLGVN YVNDHIEHIK EDVEGYIASL ECKSQEIRGD LFVDCTGFSA SLIGKHFNSP
     ITDVSQGLKN NSAMAVQAGY VDETVDIASA TLSTAHENGW IWDIGLPHRK GVGCVYSSEF
     ASDEKAAETL KAYLTSCKKT KDVSENDFRK ITFSPGYRKT AWVKNCVAVG TSAGFVEPLE
     ASALVMVEMS ARFISEHLPN HREIMPSVSK RFNSNFTRRW ERIVDFLKLH YVLSERKDSP
     YWRFMTNLDN ASEQLKDWLL EWQYRPISLT DFCYADELFP AASYMYVLYG MKAPEQFAIN
     FSRYSDSVMG QTLNAVKANE KLSHKHVAAL PTNRELIKAI RA
//