ID A0A0Q8Q7Y9_9ACTN Unreviewed; 516 AA.
AC A0A0Q8Q7Y9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=4-hydroxyacetophenone monooxygenase {ECO:0000313|EMBL:KRB78009.1};
GN ORFNames=ASE01_07495 {ECO:0000313|EMBL:KRB78009.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB78009.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB78009.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78009.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB78009.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78009.1,
RC ECO:0000313|Proteomes:UP000050886};
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 -!- 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:KRB78009.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMIA01000008; KRB78009.1; -; Genomic_DNA.
DR RefSeq; WP_056749734.1; NZ_LMIA01000008.1.
DR AlphaFoldDB; A0A0Q8Q7Y9; -.
DR STRING; 1736488.ASE01_07495; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000050886; 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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00469; PNDRDTASEII.
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:KRB78009.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050886}.
SQ SEQUENCE 516 AA; 57268 MW; A3E1AF995769B117 CRC64;
MTATPSRTNV DHLIVGAGFA GLAAAIKLDE AAERDFVVIE KDSDVGGTWH INTYPGAECD
VPSQLYSFSF ALNPDWSRVY SPQQEIWEYT RKVAERSGTL DRFVFNTAVL DAQWDEQAQR
WNVRTEGPDG VREYAARTVI SGSGGLSEPR LPEVEGIDDF RGEIFHSARW NHDVDLTGKR
VAVIGTGASA VQLVPELQKV VGHMDVYQRT PNWIIPRNER SFTSFEKAVF KKVPGAQRAL
RSVVYGALEA RVPAFARFPQ AMRAVDLQGR RNIAKGITDP ELRKKVTPSY RAGCKRILIS
NKWYPALDAD NVDLVTDPIV RITENAIVTA DGVERPIDVL VVATGFYVTE PPIAQHITGR
EGRTLADVWD EGGMAAYKGT TIHGFPNLFQ IVGPNTALGH SSMIFIIESQ VRYVVEAARA
MRREGLAVVE PTRAAQDAWT ADIRRKMKPT VWQTGGCASW YLDKFGNNTT LWPGQTFTLR
QHLSSFDLDK YDVEAVTPQH SAPALQPPQS KKKVTS
//