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Database: UniProt
Entry: A0A0M4Q4A7_9PSEU
LinkDB: A0A0M4Q4A7_9PSEU
Original site: A0A0M4Q4A7_9PSEU 
ID   A0A0M4Q4A7_9PSEU        Unreviewed;       490 AA.
AC   A0A0M4Q4A7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=FAD-containing monooxygenase EthA {ECO:0000313|EMBL:ALE85454.1};
GN   ORFNames=XF36_21800 {ECO:0000313|EMBL:ALE85454.1};
OS   Pseudonocardia sp. HH130629-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE85454.1, ECO:0000313|Proteomes:UP000062082};
RN   [1] {ECO:0000313|EMBL:ALE85454.1, ECO:0000313|Proteomes:UP000062082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE85454.1,
RC   ECO:0000313|Proteomes:UP000062082};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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; CP011868; ALE85454.1; -; Genomic_DNA.
DR   RefSeq; WP_060713403.1; NZ_CP011868.1.
DR   AlphaFoldDB; A0A0M4Q4A7; -.
DR   KEGG; pseh:XF36_21800; -.
DR   PATRIC; fig|1641402.3.peg.4668; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000062082; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IEA:UniProtKB-EC.
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; 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:ALE85454.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062082}.
SQ   SEQUENCE   490 AA;  55093 MW;  00B4B492865595C9 CRC64;
     MTATTSEHVD VLIVGAGVSG IGAAHRLREE FPDRSFVLLE AQDAPGGTWW THRFPGARSD
     SDLFTYGYRH KPWTGPSIAA GAEILAYLDE VIAEDDLAGH IRYHHRVTAL SWSSAEYRWT
     AEVTRTDTGE TLSTTASFLW MCQGYYNHDE PYTPQWPGLE QYAGTVVHPQ SWPSDLDVTG
     AKVLVIGSGA TAATVVPATA ATAEHVTMLQ RSPSYWFPAP TVHDLATMLE PLDLPAEWTH
     EILRRTYVQQ LDWLATTGRD DPDALHEFLI ESIRPLLPEG TDIEKHFVPR YRPWQQRIAF
     VPDGDFFAAM REGKASVVTD TIARFTEKGV ELDSGEVIEA DVVVTATGFD LAVFGDIPFT
     VDGEPVDFTR HVTWRGLMIE GIPNMAYAFG YFRHSWTLRI DLVNDLIGRI LARMDERRHQ
     VVVPTVAPQD ADMPRLPWVS EENFNPGYIG RSAHRMFGQG DREPWTHMHE HDVDRVELPK
     ADLDDGLQYR
//
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