ID A0A2S8KE35_9MYCO Unreviewed; 499 AA.
AC A0A2S8KE35;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:PQP37534.1};
GN ORFNames=C6A82_24720 {ECO:0000313|EMBL:PQP37534.1};
OS Mycobacterium sp. ITM-2016-00318.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2099693 {ECO:0000313|EMBL:PQP37534.1};
RN [1] {ECO:0000313|EMBL:PQP37534.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITM-2016-00318 {ECO:0000313|EMBL:PQP37534.1};
RA Meehan C.J., Cogneau S., Rigouts L., Shojaei H., Azadi D.;
RT "Bioremediation-capable novel species from Iranian environmental samples:
RT Mycobacterium khaydaluicum sp. nov., Mycobacterium meyganicum sp. nov.,
RT Mycobacterium omidicum sp. nov., Mycobacterium seymaricum sp. nov.,
RT Mycobacterium austroafricanum subspecies dezhpoolicum subsp. nov.";
RL Submitted (FEB-2018) 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:PQP37534.1}.
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DR EMBL; PUTV01001454; PQP37534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8KE35; -.
DR OrthoDB; 5168853at2; -.
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; 1.
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 PRINTS; PR00411; PNDRDTASEI.
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 499 AA; 55795 MW; 952F764663D30261 CRC64;
MADERLRTGA EAEYSDVLII GAGISGIGAA YRIHEKNPTL SYTVLERRAR IGGTWDINRY
PGIRSDSDIF TLSFPYEPWT RPEYVAEGAD IREYLTQTAS KHGIDEHIRF KTRVLSADWD
SSTDTWTVAT EIDGEPRTYR GRFLFFGTGY YNYDEPYRPD FPGLQDFSGP VVHPQHWPES
LDYTGKKVLV IGSGATAVSM IPTLTEKAAH VTMLQRSPSY LMSMPRVNPL LSVIRKVLPL
RAGNAAARLY GKIVTVLIYA IARKAPKASR KYIRSTAKKA LPEGYPVDVH FKPRYDPWDQ
RLCLILGNDF YEAIGDGRLD VVTDQIDHID ATGVVLRSGE RIDADLLITA TGIQLQALGG
VALSIDGAEV KPQDRFVYKE HLLEDVPNAA WCVGYVNASW TLRADLTARA FAKLLSYMDS
HGYTHAYPHL GDVPMAEKPA WNINAGYVQR AAHALPKSGT QRPWNVRHNY VLDAIDHRFD
RIEESMVFGR ADAESAQSA
//