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Database: UniProt
Entry: Q0B8D0_BURCM
LinkDB: Q0B8D0_BURCM
Original site: Q0B8D0_BURCM 
ID   Q0B8D0_BURCM            Unreviewed;       404 AA.
AC   Q0B8D0;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=Salicylate 1-monooxygenase {ECO:0000313|EMBL:ABI89593.1};
DE            EC=1.14.13.1 {ECO:0000313|EMBL:ABI89593.1};
GN   OrderedLocusNames=Bamb_4040 {ECO:0000313|EMBL:ABI89593.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI89593.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000441; ABI89593.1; -; Genomic_DNA.
DR   RefSeq; WP_011659038.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0B8D0; -.
DR   GeneID; 69546834; -.
DR   KEGG; bam:Bamb_4040; -.
DR   PATRIC; fig|339670.21.peg.4324; -.
DR   eggNOG; COG0654; Bacteria.
DR   OMA; RWMLGYD; -.
DR   Proteomes; UP000000662; Chromosome 2.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0018658; F:salicylate 1-monooxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789:SF318; GERANYLGERANYL DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:ABI89593.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ABI89593.1}.
FT   DOMAIN          6..327
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   404 AA;  44664 MW;  D3904288FBB60F6E CRC64;
     MQTNLRIAIV GAGIGGLTLA LALREQGIDA QLYEQTDVLR EVGAAVALSA NATRFYERMG
     LRPAFDAVCA EIPGLVYRDG RSGAVIGHHR GEPDYRRQFG GSYWGVHRAD LQAILSKAVG
     VEQIHLGHRL VELAQDPERV TLTFENGERV DADLVIGADG ARSLTRRWML GYDDVLYSGC
     SGFRGVVPAE RMNLLPDPET IQFWVGPHGH LLHYPIGDNG DQNFLLVERH PSPWPSRDWV
     MPAQEGEQLR LFGDWHPAVV QMITAVPISQ RWGLFHRPPL GRWSRGRVTL IGDAAHALVP
     HHGQGANQSI EDAMVLAAQL AKAGPGNWRE AQGAYERLRR GRTRKVQYAS ISAADVLHLP
     DGPAAQARNA RLGERDSVLH HLDWIHDFDA LADEPDERQG GTWL
//
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