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Database: UniProt
Entry: A0A1G9CFG0_9MICO
LinkDB: A0A1G9CFG0_9MICO
Original site: A0A1G9CFG0_9MICO 
ID   A0A1G9CFG0_9MICO        Unreviewed;       461 AA.
AC   A0A1G9CFG0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD {ECO:0000313|EMBL:SDK50411.1};
GN   ORFNames=SAMN05216282_10739 {ECO:0000313|EMBL:SDK50411.1};
OS   Cryobacterium psychrotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=386301 {ECO:0000313|EMBL:SDK50411.1, ECO:0000313|Proteomes:UP000198701};
RN   [1] {ECO:0000313|EMBL:SDK50411.1, ECO:0000313|Proteomes:UP000198701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5382 {ECO:0000313|EMBL:SDK50411.1,
RC   ECO:0000313|Proteomes:UP000198701};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNFU01000007; SDK50411.1; -; Genomic_DNA.
DR   STRING; 386301.SAMN05216282_10739; -.
DR   OrthoDB; 9808049at2; -.
DR   Proteomes; UP000198701; 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   Reference proteome {ECO:0000313|Proteomes:UP000198701}.
FT   REGION          113..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  49527 MW;  1334BCA6FCC3C56F CRC64;
     MTGPTRVAVI GAGAAGLAAT KALIDAGVDV VTYEKGDRPG GLWARDNSSG LSPAYVSLHL
     NTSKGRTEFA DYPMPADWPD YPSADHVAGY LADYATAFAL TPHIRFSTGV TSVEREGDGD
     SERGAEPAGA GWIVGADDGS SERYDAVVVA NGHNWDPRWP SPAYLGTFTG TTMHAHDYRT
     AEVFRDKRVL VVGMGNSAMD ITVDASYVSR GPVLLSSRHG VHIVPKYIFG RPSDKMNGIL
     SVLPWRARQT IAQTLLRLAV GSPEDYGLPA PAGGLFQNHP TISDTIMHRL THGEVVARPG
     IARFDGDRVE FTDGSTETVD VIVWATGYRV NIPFLTSAWL GEDAEELPLY QRVFHLQDPS
     LSFIGLIQST GAALPVLEVQ AKLVAAHLSG GYALPGAEDQ QKAVARHLAY SAARWGGDRR
     PRMRIDFDGY VAALPKEIAA GRERLRRGAK PFSIAHEGVT A
//
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