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Database: UniProt
Entry: N9M767_9GAMM
LinkDB: N9M767_9GAMM
Original site: N9M767_9GAMM 
ID   N9M767_9GAMM            Unreviewed;       496 AA.
AC   N9M767;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=FAD-containing monooxygenase EthA {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F905_01966 {ECO:0000313|EMBL:ENW88965.1};
OS   Acinetobacter sp. CIP 53.82.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144671 {ECO:0000313|EMBL:ENW88965.1, ECO:0000313|Proteomes:UP000018455};
RN   [1] {ECO:0000313|EMBL:ENW88965.1, ECO:0000313|Proteomes:UP000018455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 53.82 {ECO:0000313|EMBL:ENW88965.1,
RC   ECO:0000313|Proteomes:UP000018455};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 53.82.";
RL   Submitted (FEB-2013) 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:ENW88965.1}.
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DR   EMBL; APRK01000011; ENW88965.1; -; Genomic_DNA.
DR   RefSeq; WP_005180241.1; NZ_KB850046.1.
DR   AlphaFoldDB; N9M767; -.
DR   PATRIC; fig|1144671.3.peg.1897; -.
DR   HOGENOM; CLU_032067_2_0_6; -.
DR   Proteomes; UP000018455; 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   Pfam; PF13450; NAD_binding_8; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   496 AA;  55507 MW;  0CFA815062FBDE98 CRC64;
     MDKHVDILIV GAGISGIGLA AHLSKHCPQR TFEIIERRES FGGTWDLFKY PGIRSDSDMS
     TFGFNFKPWT QDSILADGAS IKNYLSEVIA EYQLKSKIHF QHRVLSANYD SQTQKWSVVI
     ENAQGKKQTW IANFVLGCTG YYNYDQGFQP DFPNQSAFKG TFIHPQHWPE NFDYSGKKVV
     IIGSGATAIT LVPAMVKGGA AHVTMLQRSP TYIASIPSVD FIYNNMRKVL PEELAYKLTR
     ARNIGMQRGV YALAQKQPKL LRKFLLKSIE MQLKGKVDMK HFSPSYNPWD QRLCVVPDGD
     LFKVLREGQA SVETDQIEAF TEQGIQLKSG KHLDADVIVS ATGLQIQILG GVKATIDHQP
     LDTSKHMLYQ GVMVSDVPNM AMIIGYINAS WTLKVDIAAD YICRLINHMD QQGYTEVIAE
     GDPSELMEDT VMGSLTSGYI ARAANVMPKQ GKHAPWRVSN NYLKDRKDLK QASFADPVLK
     FRKAVSESAR KPKLVS
//
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