ID V6KQ37_STRNV Unreviewed; 458 AA.
AC V6KQ37;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:EST31114.1};
GN ORFNames=M877_08345 {ECO:0000313|EMBL:EST31114.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST31114.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST31114.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST31114.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:EST31114.1}.
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DR EMBL; AWQW01000057; EST31114.1; -; Genomic_DNA.
DR RefSeq; WP_023537961.1; NZ_CM002280.1.
DR AlphaFoldDB; V6KQ37; -.
DR PATRIC; fig|1352941.4.peg.1709; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006909_8_3_11; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000017971; Chromosome.
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; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:EST31114.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 458 AA; 49767 MW; CEA63373E04D882D CRC64;
MRRTCVIGAG PSGLAASKVL ASRNVPFDCF EAGSGVGGLW RYGNDNGMSG VYASLHTNIS
KQSMAFSSLA LPDTCPVFPH HSLMLAYLED YAASFGLHRH IEFSTRVTSV RPLDDGGWEV
VCRRRGGPAE ETRRYTEVVV ANGHHWDPRL PSPAVPGAEE FAGTAIHSHD YRTPDPYAGQ
RVLVIGMGNS ACEIAAEISR TAARTFLSAR DAAHLFPKVL LGRPADHLAW SPLSDLPRLL
KDPALRLLLR LTRGSTARYG LPEPVRGPLA GHPSTSDELL SQLARGAVTP KPGVSSFGRE
TAVFSDGGRE PVDAVVYATG YRISFPFLAP SLFAAPDGRT ELYLRTIPPR LPGLYFMGLA
QPSGAAFPLL EPQAEWIAEL IEGTVAPPSP ADMTRMIARE WRRHRKTYVP TYRHGIEIDF
RSYRRALRRE RRAGRRRARG AVPALPAVAG PAPAADAV
//
