ID A0A226EP04_FOLCA Unreviewed; 502 AA.
AC A0A226EP04;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN ORFNames=Fcan01_05779 {ECO:0000313|EMBL:OXA59362.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA59362.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA59362.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA59362.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA59362.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000332,
CC ECO:0000256|RuleBase:RU361177};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR000332}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177}.
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:OXA59362.1}.
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DR EMBL; LNIX01000002; OXA59362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226EP04; -.
DR OrthoDB; 3614005at2759; -.
DR Proteomes; UP000198287; 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-UniRule.
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 PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 2.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000332};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000332};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000332}; Membrane {ECO:0000256|PIRNR:PIRNR000332};
KW Monooxygenase {ECO:0000256|PIRNR:PIRNR000332,
KW ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|PIRNR:PIRNR000332};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000332};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287}.
SQ SEQUENCE 502 AA; 57906 MW; E608ECEE81E0920A CRC64;
MKMSPNVIER PVKRHPKVFI IGAGFSGLCA GIKLQSDLEI FDYVIFDENH DVGGTWLTHT
YPGCACDVKS HLYSYSFELN PNWSTTYAPQ PEILAYLKGV AYKYDLYSKV KFHHQVKSAT
WVENSSIWKI VVHDKHVGKT TEYECDIIIS GVGGLRVPSI PEQFSKFTGP TIHSAKWNPS
LDLDDKVVAV IGSGCSAVQI VPTIEPRVKK LLSFQRHPAW IVPLSQFQIF GFIRWLFNKI
PYLMWLYRMF IFFSQEAYFM IFKANSRLRE FAKWAARMFL KWQIPNDPEL RTKLIPNYEF
GCKRISPSNM YYRALAKPKC EVVTEKIASV TQHSIITEDH REYPIDVLIL ATGYRVQDYF
SPLKLYGLNS EDILETWKTG SPSHYLGIMS SSTPNSFALL GPNTAYGHNS VIFSIECQVN
WVMQVIREFM QRNAKAVVVK ENVEKQYMKS IRTRLKDTVW GNYECGSWYV NHEGINTTLY
PGSLISYWKE TRKPVFSNLI FD
//
