ID A0A087NAG9_9SPHN Unreviewed; 480 AA.
AC A0A087NAG9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative tryptophan halogenase {ECO:0000313|EMBL:KFL46122.1};
GN ORFNames=IL54_1538 {ECO:0000313|EMBL:KFL46122.1};
OS Sphingobium sp. ba1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL46122.1, ECO:0000313|Proteomes:UP000029094};
RN [1] {ECO:0000313|EMBL:KFL46122.1, ECO:0000313|Proteomes:UP000029094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT Sphingobium species.";
RL Submitted (JUL-2014) 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:KFL46122.1}.
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DR EMBL; JPPQ01000069; KFL46122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087NAG9; -.
DR PATRIC; fig|1522072.3.peg.3366; -.
DR eggNOG; COG0654; Bacteria.
DR Proteomes; UP000029094; 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}.
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 60
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 318
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 480 AA; 53617 MW; 71DE64CE05F827AC CRC64;
MTAAALARTL GPVAQVTLVE SEQIGTIGVG ESTIPPLVAY NRILGINEAD FMRATQATFK
LGINFENWRV PGESYFHSFG GTGKDHWSAG FQHFWMHGQA QGHDAPYGDY CLELKAAEAG
RFAHLPDDRM NYAYQLDSGL YARFLRRMAE ADGAQRIEGR IAKVELDSES GDIAALLLDG
DRRIEGDLFI DCTGFRALLI EGALHVGYDD WTHWLPCDGA VAIQTSSVRP PVPYTCAIAH
EAGWQWRIPL QHRQGNGIVY CSSFLNPDAA LEKLLASVEG DKLVQPNPIR FRTGARRRQW
HRNCVAVGLS GGFMEPLEST SIHLIQRAVL RILRMLPAGT VSPLDIAEFN DQQMTDMEQI
RDFLILHYKA TDRRDTPFWR HCAAMAVPDS LAHRMELFRQ TGRAFRKNEE LFAENSWVQV
MMGQGITPQS HHPIASKLRP DELTHLLASL KDQVSRTVAN LPEHAAYIAR YCSAQEPVAA
//