ID A0A0W1LG49_9GAMM Unreviewed; 499 AA.
AC A0A0W1LG49;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KTF18498.1};
GN ORFNames=ATS75_03580 {ECO:0000313|EMBL:KTF18498.1};
OS Pseudoalteromonas sp. H105.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348393 {ECO:0000313|EMBL:KTF18498.1, ECO:0000313|Proteomes:UP000054685};
RN [1] {ECO:0000313|EMBL:KTF18498.1, ECO:0000313|Proteomes:UP000054685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H105 {ECO:0000313|EMBL:KTF18498.1,
RC ECO:0000313|Proteomes:UP000054685};
RA Duhaime M.B., Sullivan M.B., Wichels A.;
RT "Six Pseudoalteromonas strains isolated from surface waters of Kabeltonne
RT offshore Helgoland, North Sea.";
RL Submitted (DEC-2015) 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:KTF18498.1}.
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DR EMBL; LOFH01000001; KTF18498.1; -; Genomic_DNA.
DR RefSeq; WP_058559034.1; NZ_LOFH01000001.1.
DR AlphaFoldDB; A0A0W1LG49; -.
DR STRING; 1348393.ATS75_03580; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000054685; 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 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 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 343
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 499 AA; 56093 MW; 9B39B5677AD5DFB9 CRC64;
MQNKQIKQVV IAGGGTAGWI TAALLNKVLG KVVNITLVES EQIGTVGVGE ASIPPILHLN
AALGIRESEF IKATQATIKL GIEFENWRAQ DHTYMHAFGD IGKDFPFCEF YHFWLRAKQQ
GTTADFWDFS LNYQAAKQHK FTHLQHIPNT QLTGLNYAYH FDATLYGEYL KSLAISRGVN
RIEGKIANVE QCENTGFITA LALEDGQTIS GDLFIDCTGL RALLIEQTLN TGFEDWSHWL
PCDSAIAVQT QSANDPVPYT RSIAHDAGWQ WQIPLQHRVG NGLVFSSRHI TDEQAKQQLL
ANLPGEPITE PRVIRFKTGR RRKQWHKNVV SVGLSSGFLE PLESTSIHLI QTAAIRLIKL
FPHNGIDDSL VETFNQQSQT EIECIRDFII LHYKLTDRTD SAFWRQCKQM SIPDSLQKKI
DLFKATGKII RQDDELFAEI AWQQVMIGQG LEANDYSVLA GALTDDQLND LFSSLKTLIN
GTVEQLPSHS EFLARMKNN
//