ID M4SKF6_9SPHN Unreviewed; 512 AA.
AC M4SKF6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:AGH51042.1};
GN ORFNames=G432_16620 {ECO:0000313|EMBL:AGH51042.1};
OS Sphingomonas sp. MM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH51042.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH51042.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH51042.1};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(2013).
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DR EMBL; CP004036; AGH51042.1; -; Genomic_DNA.
DR RefSeq; WP_015460010.1; NC_020561.1.
DR AlphaFoldDB; M4SKF6; -.
DR STRING; 745310.G432_16620; -.
DR KEGG; sphm:G432_16620; -.
DR PATRIC; fig|745310.14.peg.3468; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_022247_0_0_5; -.
DR Proteomes; UP000011816; Chromosome.
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:UP000011816}.
FT ACT_SITE 76
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 10..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 76
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 348
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 512 AA; 55940 MW; 5E1C45BB724D2865 CRC64;
MAKRIIIVGG GTAGWLTAAY LIRSLGRSGW SITLVESPDI GIIGVGEGTF PTIRETLSAI
GVDEREFLRE ADGSFKQGVR FSGWTGGPTP GNDTDDYFHP FNLPYGGDEG LLPYWIKAAG
EARRPSYADA VTVQGHVIRA GCAPKRASDP GFDGPMNYAY HFDAARFADY LRKVATANGV
ERIEATINEV RQAEDGRIAA VVPGDGREAI EGDFFIDCSG FRALLIGKAL GSPFRHVGDV
LFNDRALAMQ VPHGDADTPI RPYTLATAHE AGWTWDIGLG ARRGIGYVYS SRHSDDEAAE
RVLRAYVGKA ADGLSPRQLR FESGYRSVQW IGNCAAVGLS AGFFEPLEST GIMLIEVAAR
MISDFLGSPA IDEAAMAAAA RQYNRLMLAR FDAIVEFLKL HYCISGRRDT AYWRDNSDAA
SIPEGLRDKL AQWRHRPPSR FDFVVDHETF LPASWQFILY GMGFRTDPAA VSSSHRDDEQ
AGAAFVRVFQ AARQAVAELP PHRALLEQLR AA
//
