ID A0A369VYP3_9SPHN Unreviewed; 521 AA.
AC A0A369VYP3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Tryptophan 7-halogenase {ECO:0000313|EMBL:RDE07263.1};
GN ORFNames=DVW87_06445 {ECO:0000313|EMBL:RDE07263.1};
OS Sphingomonas aracearum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2283317 {ECO:0000313|EMBL:RDE07263.1, ECO:0000313|Proteomes:UP000253918};
RN [1] {ECO:0000313|EMBL:RDE07263.1, ECO:0000313|Proteomes:UP000253918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZY 27 {ECO:0000313|EMBL:RDE07263.1,
RC ECO:0000313|Proteomes:UP000253918};
RA Zhiyong W., Qinglan Z., Zhiwei F., Ding X., Gejiao W., Shixue Z.;
RT "a novel species of Sphingomonas isolated from the rhizosphere soil of
RT Araceae plant.";
RL Submitted (JUL-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:RDE07263.1}.
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DR EMBL; QQNB01000001; RDE07263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369VYP3; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000253918; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000253918}.
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 13..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 82
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 352
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 521 AA; 56498 MW; E5A9B61FF1D71D6F CRC64;
MEQPVSRIVI VGGGTAGWLA ACLLAARGDR TARPPLSVTL IESPDVATVG VGEGTWPTMR
RTLERIGLSE ADFLRRCEAS FKQGSRFDGW RTGAEGEQYF HPFTPPVDGQ AADLVAAWAD
DPLARPFAET VSAQPGICAQ DLAPRQRGMP DYAGALNYAY HLDAGKLAAL LAEHGTQVLG
VRHLRDHVTR VVPGEGGDIA AVELRGAGEI AGDLFLDCTG HAALLIGGHH GVPFVDWSDV
LFNDRALAVQ VPVAPGSAIA SQTNATAHAA GWLWDIGLPT RRGVGCVYAS AFLSDAAAEE
TLAAYLARTA PDVDRSALSF RKLAFRSGHR ERFWQGNCLA IGLAAGFLEP LEASAIVLIE
LSLNALLDGF PRTRGAMERH ARRFNDLFRY RWDRIVEFLK LHYVPSVRSE PYWQAHRDPA
SIPARLQELL ALWRDQPPSR ADLPMVDEIF PAASYQYVLY GMGWPAPPPS RIAGETQAQV
AQQLAAAAQR ARVLAASLPT NRAYLDAVRA DALPRQMETV R
//
