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Database: UniProt
Entry: A0A0M2H4G0_9MICO
LinkDB: A0A0M2H4G0_9MICO
Original site: A0A0M2H4G0_9MICO 
ID   A0A0M2H4G0_9MICO        Unreviewed;       456 AA.
AC   A0A0M2H4G0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Putative oxidoreductase CzcO {ECO:0000313|EMBL:KJL41188.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:KJL41188.1};
GN   Name=czcO_4 {ECO:0000313|EMBL:KJL41188.1};
GN   ORFNames=RS82_03105 {ECO:0000313|EMBL:KJL41188.1};
OS   Microbacterium trichothecenolyticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41188.1, ECO:0000313|Proteomes:UP000034098};
RN   [1] {ECO:0000313|EMBL:KJL41188.1, ECO:0000313|Proteomes:UP000034098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41188.1,
RC   ECO:0000313|Proteomes:UP000034098};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:KJL41188.1}.
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DR   EMBL; JYJA01000038; KJL41188.1; -; Genomic_DNA.
DR   RefSeq; WP_045300974.1; NZ_JYJA01000038.1.
DR   AlphaFoldDB; A0A0M2H4G0; -.
DR   PATRIC; fig|69370.6.peg.3159; -.
DR   OrthoDB; 9808049at2; -.
DR   Proteomes; UP000034098; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KJL41188.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034098}.
FT   REGION          436..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  50271 MW;  06C77F90FFE471FA CRC64;
     MSAHRYAIIG AGPSGLSAAR ALQKTGIEFD GFEASRGVGG LWDIENPRST MYESAHLISS
     RTTTEFTEFP MRTKADYPSH RELIAYFRDF ADHFGLTGRF RFDTKVTSLE PTDDGGWMLR
     AEGPSAGSGN ASVEQRYDGV ILANGTLAEP NVPAFRGEFT GELLHTNAYK SATQLTGKRV
     LIIGAGNSGC DIAVDAVHHA AAVDMSVRRG YYFVPRYLFG RPSDTLNQGK PLPARIKQFV
     DTRVLRAFTG DPVRFGFPKP DYKIYESHPI VNTLILNHLG QGDLRIVPDI DRFDGRTVHF
     RDGSSAEYDT VLLATGYKLD YPFVDRAALD WSGMAPRLFL NTFTPSFNGL YVMGMIEASG
     IGWQGRYEQA ELIAAYLAAI ERHPDRAAAF RARVTGEPWP DLTGGYNYLG LERMSYYVNK
     DAYRGAVRTA TQALRTDAAS GGPRRARGAA RREVTA
//
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