ID A0A3N1NRU6_9GAMM Unreviewed; 496 AA.
AC A0A3N1NRU6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:ROQ21572.1};
GN ORFNames=EDC38_2198 {ECO:0000313|EMBL:ROQ21572.1};
OS Marinimicrobium koreense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Marinimicrobium.
OX NCBI_TaxID=306545 {ECO:0000313|EMBL:ROQ21572.1, ECO:0000313|Proteomes:UP000273643};
RN [1] {ECO:0000313|EMBL:ROQ21572.1, ECO:0000313|Proteomes:UP000273643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16974 {ECO:0000313|EMBL:ROQ21572.1,
RC ECO:0000313|Proteomes:UP000273643};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
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:ROQ21572.1}.
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DR EMBL; RJUK01000001; ROQ21572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1NRU6; -.
DR OrthoDB; 6278312at2; -.
DR Proteomes; UP000273643; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000273643}.
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 78
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
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"
SQ SEQUENCE 496 AA; 56135 MW; 35F3B69D2B960F6D CRC64;
MNHSIKNVLI VGGGSSGWMA AAVLARFFSK QIQIQLVESS EIGTVGVGEA TIPPIRTFND
VLGIKEADFL KQTMGTIKLG IQFENWSQPG DSYMHAFGEI GRNLGIAGFH HYWLKARQAG
VAEDFWRYSL NEQAARHNRF APMETIPGTQ FPGLTHAYHL DAGLYAQMLR AYSEKLGVKR
IDGKIQTVDK DSESGDIAAV QLESGERLEA DLFIDCSGFR ALLIGEALDV DFEDWSHWLP
CDRALAVPSE AAETITPYTR AIAHEGGWQW RIPLQHRTGN GLVYSHRHLS DDEATHTLLS
NLDTPALADP RPIRFKTGRR VQQWCQNVVS LGLSSGFLEP LESTSLHLVQ QGLTRLIKLF
PRNGIQPSDI EEYNRQSQIE FEKIRDFIIL HYHLNSKTDS PFWRMCREAP KPESLLRRID
LFAGSGRVFR EQDELFSETA WEQVMIGQGI TPQDYHPLVD NLEDHQLREF MNSWQRIVDK
TVAQMPSHND FIASLK
//