ID   FMO_STAAM               Reviewed;         368 AA.
AC   Q99R54;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative flavoprotein monooxygenase {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   AltName: Full=Baeyer-Villiger flavin-containing monooxygenase {ECO:0000303|PubMed:30338968};
DE            Short=BVFMO {ECO:0000303|PubMed:30338968};
DE   AltName: Full=Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:30338968};
DE            Short=BVMO {ECO:0000303|PubMed:30338968};
DE   AltName: Full=Flavin-containing monooxygenase {ECO:0000303|PubMed:30338968};
DE            Short=FMO {ECO:0000303|PubMed:30338968};
DE   AltName: Full=SAFMO {ECO:0000303|PubMed:30338968};
GN   OrderedLocusNames=SAV2584 {ECO:0000312|EMBL:BAB58746.1};
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP   RETRACTED PAPER.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=30338968; DOI=10.1002/prot.24661;
RA   Hwang W.C., Xu Q., Wu B., Godzik A.;
RT   "Crystal structure of a Baeyer-Villiger flavin-containing monooxygenase
RT   from Staphylococcus aureus MRSA strain Mu50.";
RL   Proteins 86:269-269(2018).
RN   [3]
RP   RETRACTION NOTICE OF PUBMED:30338968.
RA   Hwang W.C., Xu Q., Wu B., Godzik A.;
RL   Proteins 86:0-0(2018).
CC   -!- FUNCTION: FAD-binding protein that may have monooxygenase activity
CC       using NADPH and/or NADH as an electron donor. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000305, ECO:0007744|PDB:3D1C};
CC   -!- CAUTION: The crystal structure article has been retracted because
CC       submission was made without agreement from the last author. The protein
CC       was predicted in that paper to be a Baeyer-Villiger monooxygenase, but
CC       such activity was never experimentally shown. However, the protein
CC       binds to FAD in the crystal structure, and is probably an
CC       oxidoreductase. {ECO:0000305|PubMed:30338968}.
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DR   EMBL; BA000017; BAB58746.1; -; Genomic_DNA.
DR   PIR; A99964; A99964.
DR   RefSeq; WP_001163746.1; NC_002758.2.
DR   PDB; 3D1C; X-ray; 2.40 A; A=1-368.
DR   PDBsum; 3D1C; -.
DR   AlphaFoldDB; Q99R54; -.
DR   SMR; Q99R54; -.
DR   PaxDb; Q99R54; -.
DR   DNASU; 1122609; -.
DR   EnsemblBacteria; BAB58746; BAB58746; SAV2584.
DR   KEGG; sav:SAV2584; -.
DR   HOGENOM; CLU_037483_0_0_9; -.
DR   OMA; NTIFCYI; -.
DR   BioCyc; SAUR158878:SAV_RS14090-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   3D-structure; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..368
FT                   /note="Putative flavoprotein monooxygenase"
FT                   /id="PRO_0000431622"
FT   BINDING         14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
FT   BINDING         34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
FT   BINDING         41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
FT   BINDING         52..53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
FT   BINDING         110
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
FT   BINDING         307
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
FT   BINDING         319
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:3D1C"
SQ   SEQUENCE   368 AA;  41167 MW;  D99DD66AE56BBAB4 CRC64;
     MQHHKVAIIG AGAAGIGMAI TLKDFGITDV IILEKGTVGH SFKHWPKSTR TITPSFTSNG
     FGMPDMNAIS MDTSPAFTFN EEHISGETYA EYLQVVANHY ELNIFENTVV TNISADDAYY
     TIATTTETYH ADYIFVATGD YNFPKKPFKY GIHYSEIEDF DNFNKGQYVV IGGNESGFDA
     AYQLAKNGSD IALYTSTTGL NDPDADPSVR LSPYTRQRLG NVIKQGARIE MNVHYTVKDI
     DFNNGQYHIS FDSGQSVHTP HEPILATGFD ATKNPIVQQL FVTTNQDIKL TTHDESTRYP
     NIFMIGATVE NDNAKLCYIY KFRARFAVLA HLLTQREGLP AKQEVIENYQ KNQMYLDDYS
     CCEVSCTC