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Database: UniProt
Entry: A0A0Q6VK46_9ACTN
LinkDB: A0A0Q6VK46_9ACTN
Original site: A0A0Q6VK46_9ACTN 
ID   A0A0Q6VK46_9ACTN        Unreviewed;       492 AA.
AC   A0A0Q6VK46;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=FAD-containing monooxygenase EthA {ECO:0000313|EMBL:KQV75868.1};
GN   ORFNames=ASC61_13100 {ECO:0000313|EMBL:KQV75868.1};
OS   Aeromicrobium sp. Root344.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV75868.1, ECO:0000313|Proteomes:UP000051702};
RN   [1] {ECO:0000313|EMBL:KQV75868.1, ECO:0000313|Proteomes:UP000051702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root344 {ECO:0000313|EMBL:KQV75868.1,
RC   ECO:0000313|Proteomes:UP000051702};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV75868.1, ECO:0000313|Proteomes:UP000051702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root344 {ECO:0000313|EMBL:KQV75868.1,
RC   ECO:0000313|Proteomes:UP000051702};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQV75868.1}.
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DR   EMBL; LMDH01000001; KQV75868.1; -; Genomic_DNA.
DR   RefSeq; WP_056212587.1; NZ_LMDH01000001.1.
DR   AlphaFoldDB; A0A0Q6VK46; -.
DR   STRING; 1736521.ASC61_13100; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000051702; 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   Monooxygenase {ECO:0000313|EMBL:KQV75868.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051702}.
SQ   SEQUENCE   492 AA;  54691 MW;  C57A1294E0627D84 CRC64;
     MSADTTTPEH VDVIIVGAGL SGIGAAYRLQ EQCPGKSYAI LEAREAVGGT WDLFRYPGIR
     SDSDMYTLSF PFRPWTNRKS IADGEHIRDY ISDAADEFGI AEHIQFGHRV VSASWSSEDA
     RWTVTSQVGD ARIVQTASFL YLCSGYYNYD KGFQPEFPGL DSFDGQVVHP QFWPEDLDYA
     GKKVVVIGSG ATAVTLIPSM AEDVEHITML QRSPTYITTL PAEDKLAQVM RKVLPANLAH
     RAVRRKNAIV TIGFYQFCRR FPAAATKLLL GRVKRQLPEG ADMTHFTPRY KPWDQRLCIV
     PNGDLFRVIR RGKASIVTDT IKTFTPTGIE LDSGQHLDAD VVVTATGLQV VAFGQLEIEV
     DGQRVDPHEV YVYKGLMFSG VPNLAWCVGY TNASWTLRAD LSSQYVCQYL NHLDAKGYAF
     GMPDPKGAAG QARPILDLTS GYVMRVADLL PQQGTSSPWT IRQNWLLDSY DMKRTDLEQD
     MVFEKATVSV SA
//
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