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Database: UniProt
Entry: A0A0N7A007_9MICO
LinkDB: A0A0N7A007_9MICO
Original site: A0A0N7A007_9MICO 
ID   A0A0N7A007_9MICO        Unreviewed;       401 AA.
AC   A0A0N7A007;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=FAD-binding monooxygenase {ECO:0000313|EMBL:AIV40406.1};
GN   ORFNames=NI26_09895 {ECO:0000313|EMBL:AIV40406.1};
OS   Curtobacterium sp. MR_MD2014.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV40406.1, ECO:0000313|Proteomes:UP000069933};
RN   [1] {ECO:0000313|Proteomes:UP000069933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA   Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA   Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA   Newman D.K.;
RT   "Isolation and characterization of species affiliated with family
RT   Actinomycetaceae.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AIV40406.1, ECO:0000313|Proteomes:UP000069933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV40406.1,
RC   ECO:0000313|Proteomes:UP000069933};
RX   PubMed=26722011;
RA   Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA   Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA   Newman D.K., Dawson S.C.;
RT   "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT   from Topsoil in Woods Hole, Massachusetts.";
RL   Genome Announc. 3:0-0(2015).
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DR   EMBL; CP009755; AIV40406.1; -; Genomic_DNA.
DR   RefSeq; WP_066654881.1; NZ_CP009755.1.
DR   AlphaFoldDB; A0A0N7A007; -.
DR   STRING; 1561023.NI26_09895; -.
DR   KEGG; cum:NI26_09895; -.
DR   PATRIC; fig|1561023.3.peg.2054; -.
DR   OrthoDB; 3356051at2; -.
DR   Proteomes; UP000069933; 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:AIV40406.1};
KW   Oxidoreductase {ECO:0000313|EMBL:AIV40406.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069933}.
FT   DOMAIN          7..313
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   401 AA;  43088 MW;  AF6ABD37E5FFD36B CRC64;
     MSAPHAVISG ASIAGLSAAW WLRHTGWDVT VVERAPAFRD GGQNVDVRGV AKQVLERMGL
     TDAVRAANTT ETGTVLVDTE GRVTATLPEG PDGATAELEV LRGDLARTVR DALPDEVPFV
     FGERITDVDD TAPGHVAVTT TSGRTLRADL LVVAEGVRST TRALVFDHPG DVAERDLGVT
     MAFGTIPRTD SDDRRWRWYN AVGGRQVHLR PDPYDTTRAI LAWAGDDDGV TGAERTGVQA
     GLEERFADAG WQSRRVLDGF ATSDDVYVDR LTQVRMPVWR RGRVALVGDA AWCVTPMGGG
     GASLALTSGY VLAASVTGRS SDRADLDRAL AAFDDWMRPL VDDVQGIPRG IVRFAYPRTR
     LGLALRHVAD RVLLEGPLQG LAAKATRVAE TDRELPPVPV V
//
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