ID L5LMT2_MYODS Unreviewed; 969 AA.
AC L5LMT2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|ARBA:ARBA00012850, ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN ORFNames=MDA_GLEAN10014782 {ECO:0000313|EMBL:ELK27769.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK27769.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361177};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004111}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|RuleBase:RU361177}.
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DR EMBL; KB109864; ELK27769.1; -; Genomic_DNA.
DR eggNOG; KOG1399; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
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; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002255; Flavin_mOase_3.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF84; FLAVIN-CONTAINING MONOOXYGENASE 2; 1.
DR Pfam; PF00743; FMO-like; 3.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01123; FMOXYGENASE3.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177}; Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 969 AA; 109846 MW; 0DD501F2649215AA CRC64;
MAKKVAVIGA GVSGLASIRC CLEEGLEPTC FERSNDVGGL WKFSEHAEED RASIYPSVFT
NSSKEMMCFP DFPYPEDYPN FMHHGKLQEY IRTFAEKKNL LRYIQFETLV SSVKKCPSFL
VTGQWEVVSE KNGKQESTIF DAVMVCSGHH VYPNLPNDSL PGLDQFQGHY LHSREYKGPE
AFKGKRVLVI GLGNSGCDIA VELSRLATQV MISTRSGSWV MSRVWEDGYP WDMVYITRFA
SFLQNVLPSF LSDWLYVKKM NTCFKHENYG LMPLNGALRK EPVFNDELPS RILCGTLSIK
PGVKEFTETS AVFEDGTVFE AVDFVIFATG YAYAYPFLDD SIIKSRNNEV TLFKGIFPPM
MEKPTLAVIG FVQSLGAAIP TADQQARWAA KVFANSCTLP TTKEMMDDID MKMGKKLKWF
GQSQTLQTDY ITYMDELGSF IGAKPNIPWL FLTDPQLALQ VFFGPCSPYQ FRLMGPGKWE
GARKAILTQW DRTVKPIRTR RETMAKKVAV IGAGVSGLIS LKCCVDEGLE PTCFERTEDI
GGLWRFKENV EDGRASIYQS VITNTSKEMS CFSDFPMPED FPNFLHNSKL LEYFRIFAKK
FDLLKYIQFQ TTVLSVKRCP DFSSSGQWEV VTESKGNEQS AIFDAIMVCS GHHILPRIPL
ESFPGIENFK GQYFHSRQYK NPDGFEGKRV LVIGIGNSAS DIAVELSKKA SQVFISTRQG
SWVLSRISDC GYPWDMVFHT RFRSMLRNVL PRTVQKWMSE RQMNQWFHHE NYGLEPQNKY
LMKEPVLNDD LPSRILYGAI KVKSRVTELT ETSAIFEDGT VEEDIDVIVF GLLSFGESQS
QILQTNYIDY LDELAEEIGA KPDLLSLLFQ DPKLAVKLYF GPCNSYQYRL VGPGRWEGAK
SAILSQKQRM LRPLKTRTLE PASNFPVSLL LXXXXXXXXX XXXXXXXXXF SNFRVLTHQL
LALLSVSTS
//
