ID A0A396RQL3_9SPHN Unreviewed; 501 AA.
AC A0A396RQL3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RHW17572.1};
GN ORFNames=D1610_08940 {ECO:0000313|EMBL:RHW17572.1};
OS Sphingomonas gilva.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2305907 {ECO:0000313|EMBL:RHW17572.1, ECO:0000313|Proteomes:UP000266693};
RN [1] {ECO:0000313|EMBL:RHW17572.1, ECO:0000313|Proteomes:UP000266693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZDH117 {ECO:0000313|EMBL:RHW17572.1,
RC ECO:0000313|Proteomes:UP000266693};
RA Zhu D., Zheng S.;
RT "The multiple taxonomic identification of Sphingomonas gilva.";
RL Submitted (AUG-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:RHW17572.1}.
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DR EMBL; QWLV01000003; RHW17572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396RQL3; -.
DR OrthoDB; 462203at2; -.
DR Proteomes; UP000266693; 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:UP000266693}.
FT ACT_SITE 80
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 80
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 344
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 501 AA; 55311 MW; E90BC1FBAEE8FDEA CRC64;
MRQSAIQSVA IIGGGTAGWM TAAALAHKLA GLPISVTLVE SEEIGTVGVG EATVPHIRHF
NASLGFDEAD FMARTNATFK LGIEFRNWGR IGDSYIHPFG AFGRDIDGVP FHHLWARLRR
DGAAPAFDSF SLPVQAARMG RFAHPADDPA SPFSTYSYAY QFDAGLYAAY LRAFAEARGT
RRIEGKVVDT ALDAQTGFIE AVTLDGGKRI AADLFIDCSG FRGLLIEQAL KAGYQEWTHW
LPCDRAIAVP CANAGPIAPL TRSTALDAGW AWRIPLRHRA GNGHVYSSAF IDDDRAEQAV
LAQLEAPPLA DSRRLRFTTG KRRRQWIGNC VAIGLSSGFL EPLESTSIHL IQLAITHLIE
LFPTTDWDPM DAAEFNRVMA LEYERVRDFL ILHYHATERD DTPFWTHCRT MEIPDSLAHK
LALFRERGVV VNYREGMFLE PSWLAVYLGQ RVIPRRGDPL AERGDSAELE ARAVAMAADY
RRAAERLPLH QSLLANVAAA A
//
