ID   THAL_CHOCO              Reviewed;         522 AA.
AC   Q0VZ69;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Tryptophan 2-halogenase {ECO:0000303|PubMed:16793524};
DE            EC=1.14.14.-;
GN   Name=cmdE {ECO:0000312|EMBL:CAJ46693.1};
OS   Chondromyces crocatus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Chondromyces.
OX   NCBI_TaxID=52;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAJ46693.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Cm c5 {ECO:0000269|PubMed:16793524};
RX   PubMed=16793524; DOI=10.1016/j.chembiol.2006.06.002;
RA   Rachid S., Krug D., Kunze B., Kochems I., Scharfe M., Zabriskie T.M.,
RA   Blocker H., Muller R.;
RT   "Molecular and biochemical studies of chondramide formation-highly
RT   cytotoxic natural products from Chondromyces crocatus Cm c5.";
RL   Chem. Biol. 13:667-681(2006).
CC   -!- FUNCTION: Involved in the incorporation of a chlorinated tryptophan
CC       residue into halogenated forms of the secondary metabolites called
CC       chondramides. {ECO:0000269|PubMed:16793524}.
CC   -!- MISCELLANEOUS: Chondramides are secondary metabolites with antifungal
CC       and cytotoxic activity. They are non-ribosomally produced depsipeptides
CC       consisting of a polyketide chain and 3 amino acids (alanine, N-
CC       methyltryptophan and beta-tyrosine or alpha-methoxy-beta-tyrosine).
CC   -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM179409; CAJ46693.1; -; Genomic_DNA.
DR   RefSeq; WP_050432504.1; NZ_CP012159.1.
DR   AlphaFoldDB; Q0VZ69; -.
DR   SMR; Q0VZ69; -.
DR   PRIDE; Q0VZ69; -.
DR   OrthoDB; 1770293at2; -.
DR   GO; GO:0004497; F:monooxygenase activity; IMP:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009403; P:toxin biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR006905; Flavin_halogenase.
DR   Pfam; PF04820; Trp_halogenase; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Chloride; FAD; Flavoprotein; Monooxygenase; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN           1..522
FT                   /note="Tryptophan 2-halogenase"
FT                   /id="PRO_0000407917"
FT   BINDING         16..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         42..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         296
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         307..308
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
FT   BINDING         309
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KCZ0"
SQ   SEQUENCE   522 AA;  57896 MW;  96067FEA0A4F46A4 CRC64;
     MQLPSSTKIL VVGGGPAGST AATLLAREGF EVTLVEKAIF PRYHIGESLL ISVQPIIDLL
     GAREAVEAHG FQRKKGVLWE WGGERWLFDW KKLRYDYTFH VKREEFDEIL LRNAQKNGVK
     VFEGIDISRL EFDGERPVAA KWSKSSTGES GTIQFEFLLD ASGRAGLMAT QYLRSRMFMK
     AFQNVATWGY WKGATIPEVE VEGPITVGSI PYGWIWGIPL RDQTMSVGLV IHQELFKEKR
     ATQSVEEIYH EGLKASPLFQ DVVLKGATLE PQIRTETDYS YISRTLAGPG FFLVGDSGAF
     IDPLLSSGVH LAMHSALLAA ASVKSIIAGE VDMASATEFY QRCYQGHFLR WALIVASFYE
     VNARKETYFW TAQQLAHEEL GVFNMSQADM KDVFATMVSG VVDLGDAQNA GRLQKGAERV
     HQYLDDDGRE EDVTALLQKS KQRIFEYLDR VKNRDSRAAM QRYKAGGTET FSMGLDADGA
     VGGLYVTTEP RLGLLRKVVE ERAEAATEAP APAAPPPAVA EV