ID A0A0M2LS34_9SPHN Unreviewed; 517 AA.
AC A0A0M2LS34;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KKI18668.1};
GN ORFNames=XM50_12310 {ECO:0000313|EMBL:KKI18668.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI18668.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI18668.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18668.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-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:KKI18668.1}.
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DR EMBL; LAZX01000093; KKI18668.1; -; Genomic_DNA.
DR RefSeq; WP_046410014.1; NZ_LAZX01000093.1.
DR AlphaFoldDB; A0A0M2LS34; -.
DR STRING; 1642949.XM50_12310; -.
DR PATRIC; fig|1642949.3.peg.1622; -.
DR Proteomes; UP000033997; 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}.
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 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 342
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 351
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 517 AA; 55907 MW; 4A91326FF2699629 CRC64;
MKRQVANIVI VGGGTAGWLA AATIAACADP TAQPPVQVTL IESPDVPTIG VGEGTWPTIR
RTLARIGISE AEFLLACDAS FKQGSRFDSW RNGAPDDSYL HPFSAPVEAD PRALVAAWQA
GEEEGFAAAV TPQARACALD LAPRQRAMPD YAGALNYAYH LDAVKLAALL RRHATQRLGV
RHVRDHVLSV DRRHDGDIAA VRCRDHGAME GDLFIDCTGH AALLIGGALG VHFIDRGHEL
FNDRALAVQV PVAAGSAIAS TTNATAHEAG WIWDIGLPTR RGVGCVYSSA HLTDDAAEGI
LRAYLGRTTP AANLDALAPR KLTFRSGHRT RFWERNCLAI GLSSGFLEPL EASAIVTIEL
ALDALVANFP ATRASMDAHA DRFNALFRYR WDRIVDFLKL HYVLSDRGQP YWRDNRDRSS
IPHSLAGLLA IWREQPPSGH DLGMVDEVFP AASYQYVLYG MGMAPPPPGP MRIEGVPPAS
AALRQAAQRA RALAASLPTN RAYLDVLRAD RQNEIIA
//
