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Database: UniProt
Entry: A0A426GM57_9CAUL
LinkDB: A0A426GM57_9CAUL
Original site: A0A426GM57_9CAUL 
ID   A0A426GM57_9CAUL        Unreviewed;       506 AA.
AC   A0A426GM57;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RRN65163.1};
GN   ORFNames=EIK80_06255 {ECO:0000313|EMBL:RRN65163.1};
OS   Caulobacter sp. 602-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN65163.1, ECO:0000313|Proteomes:UP000268773};
RN   [1] {ECO:0000313|EMBL:RRN65163.1, ECO:0000313|Proteomes:UP000268773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=602-1 {ECO:0000313|EMBL:RRN65163.1,
RC   ECO:0000313|Proteomes:UP000268773};
RA   Gao J., Sun J.;
RT   "The genome of Caulobacter sp 602-1.";
RL   Submitted (NOV-2018) 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:RRN65163.1}.
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DR   EMBL; RRYI01000002; RRN65163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A426GM57; -.
DR   OrthoDB; 5695497at2; -.
DR   Proteomes; UP000268773; 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        80
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         80
FT                   /ligand="7-chloro-L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:58713"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         187
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         344
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT   BINDING         348
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ   SEQUENCE   506 AA;  56883 MW;  6EFBC39CDE743224 CRC64;
     MQDNRIRKLV IVGGGTAGWM AAAALRRHFQ GGPLEITLVE SSEIGTIGVG EATIPTIRAF
     YNQLGLTDIE VMRATQATCK LGIRFNGWVR EGQSFIHPFG HFGQDLRGVA FHHYWRKLAQ
     AGEPTDIADY SLGASLARAG KFMAPSRNPA STLSVFDWAL HFDASLFAQL MRRVAEENGV
     RRVDARVTKV NLRPEDGFVA SLDLHTGESV EGDLFIDCSG FRGLLIEEAL QTGYEHWNDM
     LFCDRAWAAQ SEGVGDPMPY TDVTAHTAGW RWRIPLQHRY GNGYVFSSRH IGDEDALAEL
     KAAIPDPLLH EPRLIRFNPG RRKQVWNKNV IALGLASGFL EPLESTSIAL IETGIEKIKA
     LFPDKDFAPE IVDEFNDWSR REMERVRDFI VLHYWANKRG DTAFWRDCND VVLPEALRRK
     VDLFLTRGHF VRYRWEMFAP PSWMAIYAGF ELLPQTVDPS LDGIDPRTLS APLAEMRKAV
     REVVANAPPH AAFLDQYCRS AAMAAE
//
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