ID E0TBD0_PARBH Unreviewed; 525 AA.
AC E0TBD0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative monooxygenase {ECO:0000313|EMBL:ADM08334.1};
GN OrderedLocusNames=PB2503_01272 {ECO:0000313|EMBL:ADM08334.1};
OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM08334.1, ECO:0000313|Proteomes:UP000001302};
RN [1] {ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RA Kang D.-M., Oh H.-M., Cho J.-C.;
RT "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM08334.1, ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RX PubMed=21037002; DOI=10.1128/JB.01205-10;
RA Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT the type species of the order "Parvularculales" in the class
RT Alphaproteobacteria.";
RL J. Bacteriol. 193:305-306(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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DR EMBL; CP002156; ADM08334.1; -; Genomic_DNA.
DR RefSeq; WP_013299308.1; NC_014414.1.
DR AlphaFoldDB; E0TBD0; -.
DR STRING; 314260.PB2503_01272; -.
DR KEGG; pbr:PB2503_01272; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_032067_2_0_5; -.
DR OrthoDB; 312624at2; -.
DR Proteomes; UP000001302; 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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43872; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR PANTHER; PTHR43872:SF1; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:ADM08334.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001302}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 57990 MW; 2129D357B91E69D4 CRC64;
MDGSAFPSPQ EPGGGRPEGD EGQYDVVIVG AGISGINAAY RLTESDPTLT YKIFEGRERL
GGTWDLFKYP GIRCDSEMST LAFPFRPWEE KSLIGSGYEI RDYLEDTARE NGIYPRIEFQ
TYVKSAAWSS EENLWTVKIV NAAGTERTVK GRYIYLGTGY YDYGSGYTPD FPGLESFGGQ
MIHPQHWPED LPLKDKKAVI IGSGATAITL VPAMADEGAE VTMLQRSPTY VIAMPSSAAP
ARALRAVFGR NLGNKIERWR SHFLGDTFYK ASKAFPGLIR NILQRRAQSL LGKNVSVDPH
FTPKYNPWDQ RLCLDPDAKL FKTLRKGKAK VVTDHIERFD ETGIQLKSGD HLDADIVVSA
TGLNVKMFGD IDLSVDGRPI DPADHFVYRG MMLDGVPNFF LAIGYVNASW TLKVDLTAQL
AASVIGRAKA GGHQRVAAIP LSDMGKESPL LDLTSGYVQR ALERLPRQGA EEPWVVHQDF
KKDIKSTREG MKGDEAVKFD PSPDQLKPFQ PRTPSATAPE LQAAE
//
