ID G8PMH5_PSEUV Unreviewed; 438 AA.
AC G8PMH5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Dimethylaniline monooxygenase {ECO:0000313|EMBL:AEV38166.1};
GN OrderedLocusNames=PSE_3662 {ECO:0000313|EMBL:AEV38166.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38166.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV38166.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38166.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; CP003147; AEV38166.1; -; Genomic_DNA.
DR RefSeq; WP_014286132.1; NC_016642.1.
DR AlphaFoldDB; G8PMH5; -.
DR STRING; 911045.PSE_3662; -.
DR KEGG; psf:PSE_3662; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006909_8_3_5; -.
DR Proteomes; UP000005634; Chromosome.
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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:AEV38166.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 438 AA; 48812 MW; DCEAD06581F5B44C CRC64;
MNISKESYAL IGAGPMGLAT AKTLIEQGID FQGFELHSDV GGLWDIDGPK STMYESAHLI
SSKKMTEFTD FPMGDHIAEY PGHRELKTYF QDFAEQFDLK RRYHFGAEVT RIMPLGGDGE
GWTVSWRDQG GDHSAEFAGV LIANGTLSEP NMPAFEGEFA GDLIHSCKYK SAQQFAGKRV
LIVGAGNSGC DIAVDAIHHG VHCDISMRRG YYFVPKYVFG KPADTMGGAV KLPLWLKRRV
DQTLLKWFVG DPQAYGFPKP DYALYESHPV VNSLILYHAG HGDIGIRADI KELDGNTVRF
RDGEEAEYDL IVAATGYKLH YPFIDKELLN WQGDAPHLFL NCMHPERNDL FVMGMIEATG
LGWQGRHDQA ELVARYLRGL KDGSAAAEAI KAEKAKGFAR ETGGMNYLKL ARMAYYVDKQ
SYRSALNKRT QALKREMA
//
