ID K0JZZ6_SACES Unreviewed; 520 AA.
AC K0JZZ6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:CCH30882.1};
GN OrderedLocusNames=BN6_35860 {ECO:0000313|EMBL:CCH30882.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH30882.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH30882.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC Bacterial tryptophan halogenase subfamily.
CC {ECO:0000256|ARBA:ARBA00038396}.
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DR EMBL; HE804045; CCH30882.1; -; Genomic_DNA.
DR AlphaFoldDB; K0JZZ6; -.
DR STRING; 1179773.BN6_35860; -.
DR KEGG; sesp:BN6_35860; -.
DR PATRIC; fig|1179773.3.peg.3586; -.
DR eggNOG; COG0644; Bacteria.
DR HOGENOM; CLU_022247_0_0_11; -.
DR OrthoDB; 8868802at2; -.
DR BioCyc; SESP1179773:BN6_RS17375-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
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; 2.
DR PIRSF; PIRSF011396; Trp_halogenase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
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:UP000006281}.
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 203
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 363
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 367
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 520 AA; 58898 MW; CF915A0605AB63A0 CRC64;
MNTRNPQNVV VVGGGTAGWM TASYLKAAFG DRISVTLVES GRIGTIGVGE ATFSDIRHFF
QFLDLKEEDW MPACNATYKL AVRFEDWREP GHHFYHPFEQ MRSVGGFPLT DWWLQNGLTD
RFDKDCFVIA SLCDAGRSPR HLDGRLFEQD YVEGGEEPVG LTMSEHQGKT QFPYAYHFEA
ALLAKYLTKY SVDRGVRHIV DEVQDVRLDE RGWIDHVVTK EHGELHGDLF VDCTGFRGLL
INKALGVPFQ SYQDTLPNDS AVALQVPLDM QARGLRPCTT ATAQEAGWIW TIPLFGRIGT
GYVYAKDYCS PEEAERTLRE FVGPGAEDVE ANHIRMRIGR SRESWANNCV AIGLSSGFVE
PLESTGIFFI HHAIEQLVKF FPAADWHPKL RDMYNSAIAN VMDGVREFLV LHYIGAKRDD
TQYWKDTKTR AIPDGLAERL ERWKVQLPDS ENIFPYYHGL PPYSYMCILL GGGAIPLRPS
PSLALSDDTA ARKEFAAIRD KARHLVERLP AQYEYHARLH
//
