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Database: UniProt
Entry: D3Q0W5_STANL
LinkDB: D3Q0W5_STANL
Original site: D3Q0W5_STANL 
ID   D3Q0W5_STANL            Unreviewed;       402 AA.
AC   D3Q0W5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Monooxygenase FAD-binding protein {ECO:0000313|EMBL:ADD43715.1};
GN   OrderedLocusNames=Snas_4063 {ECO:0000313|EMBL:ADD43715.1};
OS   Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS   NBRC 102104 / LLR-40K-21).
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Stackebrandtia.
OX   NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD43715.1, ECO:0000313|Proteomes:UP000000844};
RN   [1] {ECO:0000313|EMBL:ADD43715.1, ECO:0000313|Proteomes:UP000000844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC   LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX   PubMed=21304662; DOI=10.4056/sigs.47643;
RA   Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT   40K-21).";
RL   Stand. Genomic Sci. 1:292-299(2009).
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DR   EMBL; CP001778; ADD43715.1; -; Genomic_DNA.
DR   RefSeq; WP_013019286.1; NC_013947.1.
DR   AlphaFoldDB; D3Q0W5; -.
DR   STRING; 446470.Snas_4063; -.
DR   KEGG; sna:Snas_4063; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_1_0_11; -.
DR   OrthoDB; 3356051at2; -.
DR   Proteomes; UP000000844; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
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; PTHR46865; OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR46865:SF2; POSSIBLE OXIDOREDUCTASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:ADD43715.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ADD43715.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000844}.
FT   DOMAIN          5..321
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   REGION          85..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  43251 MW;  29A90E5B7D80BE08 CRC64;
     MPHERVLISG AGIAGITLAH WLHHHGFSPT VVERAPAPRA GGYKVDIRGA ALSVVERMGL
     TDAIRAACTD IQGGSVVTAS GKRVASMDGD SFGGREHEDS ELPRGELGRL LYEATEKKAD
     FRFGDSITAL DQTGDDVEVT FASGTTERFD LVVGADGLHS ATRALAFGPE DQYVRDLGYY
     VSVYTVPNHL NLDREELTYV GPGRTALMYS TAGDPNARAM FLWSSPSLEY DRGDANAQRE
     LLRSAYADEG WEVPTLLEAA ETTPDFYFDT LSQVHMDHWF TGKVALVGDA AHCASAASGQ
     GTSLALVGGY VLAGELSRAK DPTAAFAAYE QRMRGFAETN QALGPANIKR MVLRGKGQIR
     VAMTMLALMS RMPGKERMMA RVAATIHKAA TAIDLPDYEA AD
//
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