ID A0A370IDC1_9NOCA Unreviewed; 489 AA.
AC A0A370IDC1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cation diffusion facilitator CzcD-associated flavoprotein CzcO {ECO:0000313|EMBL:RDI67394.1};
GN ORFNames=DFR76_103465 {ECO:0000313|EMBL:RDI67394.1};
OS Nocardia pseudobrasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=45979 {ECO:0000313|EMBL:RDI67394.1, ECO:0000313|Proteomes:UP000254869};
RN [1] {ECO:0000313|EMBL:RDI67394.1, ECO:0000313|Proteomes:UP000254869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44290 {ECO:0000313|EMBL:RDI67394.1,
RC ECO:0000313|Proteomes:UP000254869};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RDI67394.1}.
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DR EMBL; QQBC01000003; RDI67394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370IDC1; -.
DR STRING; 1210086.GCA_001613105_04375; -.
DR Proteomes; UP000254869; 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; 2.
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:SF226; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000254869}.
SQ SEQUENCE 489 AA; 54420 MW; F97CAD5D6B44C6E0 CRC64;
MSVEFGRVVI VGAGISGLVT ARILRDDGFD VTVIEKEPMI GGVWAESRAY PGLRTNNSQQ
TYVYTDHLWD PSADQFPTAE QVRDYLGSYV ARFELGDLLR LSTEVLRVER NDTGFEVEAR
GPDGAIRLDC DYVVVCAGTY SVPVMPEFEG GESFTGAVMH SSTVTDPALL EDKRVVVVGA
GKSALDAATW AAKYGRRSTL VFRRPHWMVP RYLPGGIPTD HFTLGRISEM FVPYYRLNRV
ERFLHGPGAV LPWLFWRFIG RLFRTLLRMP AAMVPDEPFD RGRDNLGFVS EFYSLARAGR
VDMLRDRVAA LDGDEVVLAS GKRVTADIVV CATGFRQDLR FLAPELREAV APGGRFALYR
HILSPTEPRL ACIGFASSTA CTLTAEMSAH WLAQVFAGEL VLPTTAEMTA EIQQAQDWLA
AEFPARPQGY YIGQHLTRHI DALLTDMGLP TRRTRNIFTE YFGTFGPARY RDVAAQRRAT
KTVARSVLS
//