ID A0A0H4CCF1_9ACTN Unreviewed; 499 AA.
AC A0A0H4CCF1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:AKN72331.1};
GN ORFNames=QR97_23410 {ECO:0000313|EMBL:AKN72331.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN72331.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN72331.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN72331.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011799; AKN72331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4CCF1; -.
DR STRING; 1577075.QR97_23410; -.
DR PATRIC; fig|1577075.3.peg.4849; -.
DR Proteomes; UP000036399; 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; 1.
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:UP000036399}.
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 60
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 342
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 499 AA; 57093 MW; 5E4C917BD901423B CRC64;
MTAAYLRRAL GDKVSVTLVE SKRIKTIGVG EATFSTVRHF FDYLGMAEHE WMPRCNATYK
LGIRFENWRE KGHYFYHPFE RLPVVDGFPL TDWWLAKKPG PRFDQDVFLM SSIVDNERSP
RFLDGTLFEQ EFVERAGDQA RTTLSEQSTQ FPYAYQFDAS LLADYLCEYA TERGARHIED
DVLDVVRDER GWISHVVTKE HGDLTGDLFI DCTGFRGLLI NQALEEPFVS YQDTLPNDSA
VALRVPVDME KRGLRPCTTA TAQDAGWIWT IPLYGRIGTG YVYASDYCGP EEAERTLREF
VGPEAADLEA NHIRMRIGRT RQSWVNNCVA IGLSSGFVEP LESTGIFFIQ HGIEQLVKHF
PDAGWDPGLR NSYNTAVARV MDGVREFLVL HYHCAARADN AYWRDAKTRA LPDGLAERLE
QWRSKLPSMD TIYPHYHGFE PYSYLSMLLG LGGLELKPAN AVSLMDDSRA ADEFRRIKDL
SHDLVKRLPS QYEYLSQMR
//
