ID A0A3N5DKM4_9SPHN Unreviewed; 504 AA.
AC A0A3N5DKM4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RPF72262.1};
GN ORFNames=EG799_11980 {ECO:0000313|EMBL:RPF72262.1};
OS Aurantiacibacter spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2488860 {ECO:0000313|EMBL:RPF72262.1, ECO:0000313|Proteomes:UP000275232};
RN [1] {ECO:0000313|EMBL:RPF72262.1, ECO:0000313|Proteomes:UP000275232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E23 {ECO:0000313|EMBL:RPF72262.1,
RC ECO:0000313|Proteomes:UP000275232};
RA Zhuang L., Luo L.;
RT "Erythrobacter spongiae sp. nov., isolated from a marine sponge.";
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:RPF72262.1}.
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DR EMBL; RPFZ01000001; RPF72262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5DKM4; -.
DR OrthoDB; 462203at2; -.
DR Proteomes; UP000275232; 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:UP000275232}.
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 331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 340
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 504 AA; 56538 MW; DE64AC5C293DE95D CRC64;
MTDRPITRYC IAGGGTAGWM AAAALARFLP GGHTVELVES EAIGTVGVGE ATIPQIHLFN
GALGLDEAEF LRETKGSIKL GIEFDGWLRE GAAYMHAFGN IGRSAGLLPF QHYWLRAHAL
GFAKPLQRYS LNELAGRTMR MQRGKTAGGQ EMPYAYHFDA ALYARYLRRF AEERGVTRYE
GRIEQVERAG QSGDISALLL DGDRRIEADF FIDCTGFRGL LIEGALETGF EDWSDWLPCD
RALAVACEGG GDFTPYTRSI ARPAGWQWRI PLQHRLGNGL VYCSAQWSDD EAAETLLANL
DGAPQTDPRP IRFTTGTRRR HWNRNCLALG LAAGFMEPLE STSIHLVQSA ISRFLAVLPH
AAPDPAIVGW FNQQARFEWE RIRDFLILHY TANDRVGQPF WDQVRTMIPP DTLTAKLDQW
RATGFIHREH EELFTDVGWF QVLVGQGVAA RGYNRLADAM PEDDLRRFLG ETERALIEQV
KPMPRHLDFL RDCIARSERQ GVDA
//