ID A0A0A3X1L4_9GAMM Unreviewed; 501 AA.
AC A0A0A3X1L4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GW12_21220 {ECO:0000313|EMBL:KGT46818.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT46818.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT46818.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT46818.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KGT46818.1}.
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DR EMBL; JPQO01000189; KGT46818.1; -; Genomic_DNA.
DR RefSeq; WP_034587444.1; NZ_JPQO01000189.1.
DR AlphaFoldDB; A0A0A3X1L4; -.
DR STRING; 1509403.GW12_21220; -.
DR PATRIC; fig|1509403.3.peg.2108; -.
DR eggNOG; COG2072; Bacteria.
DR OrthoDB; 312624at2; -.
DR Proteomes; UP000032870; 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; 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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 501 AA; 56068 MW; 6B5B247A89CA2D37 CRC64;
MEKQVDILIV GAGISGIGLA AHLSKHCPQR SFEIIERRDS IGGTWDLFKY PGIRSDSDMS
TFGFNFKPWK QESVLATGPA IKNYLSEVVD EFKLKSKIHF QHRVLSANYD SSTHKWSVEI
ENDQGQKETW VANFVLGCTG YYNYDQGFQP EFPNQQAFKG TFIHPQHWPE NFDYSGKKVV
IIGSGATAIT LVPAMVKGGA GHVAMLQRSP TYIASVPSID VIYAKMRKFL PEEVAYKLTR
ARNISMQRGI YALAQKYPKL LKTILLNAVK LQLKGKVDMK HFTPNYEPWD QRLCVVPDGD
LFKILREGKA SVETDLIEKF TEKGIQLKSG KHLDADVIVS ATGLNIQILG GIQASIDGKP
INTSNHMLYR GVMVSDIPNM ALLIGYINAS WTLKVDIAAE YICRLLNYMD KKGYDEVVPE
GNASEMLQDT VMGSLTSGYI ARAADVMPKQ GKRGVWRVSN NYLADRKDLK QAGFDDDILQ
FKKKAGQDKP QSKKVKPRLV S
//
