ID A0A1R3H9Y0_COCAP Unreviewed; 509 AA.
AC A0A1R3H9Y0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN ORFNames=CCACVL1_20821 {ECO:0000313|EMBL:OMO67066.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO67066.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO67066.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO67066.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU361177};
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC 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:OMO67066.1}.
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DR EMBL; AWWV01012455; OMO67066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3H9Y0; -.
DR STRING; 210143.A0A1R3H9Y0; -.
DR EnsemblPlants; OMO67066; OMO67066; CCACVL1_20821.
DR Gramene; OMO67066; OMO67066; CCACVL1_20821.
DR OMA; TVPSYWI; -.
DR OrthoDB; 5487623at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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; 3.
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:SF297; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU361177};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
SQ SEQUENCE 509 AA; 58107 MW; CBDDFA39EE1A0333 CRC64;
MASEQGYLKS SKVGIIGAGI SGIAAAKQLS NHNPIVFEAT DSIGGVWKHC SFASTKLQTP
RCDFEFSDYP WPQRDNSNFP SYLEILDYLH GYATHFDVLK YIKFNSRVVE IRYIGDKSEE
FGPKIDHDVV SPGEFGPLLN GHPVWEVTVE THPSKTLEKY TFELLVVCIG KYGDIPRMPI
FPPNKGQEVF GGKVMHTLEY SKLDKEAARE LLKGKKVAVV GYKKSAIDLA TECAEANQAY
WIWGLPFFLF YSTRSSQFLH QTPKQGLLRN LLCPLLSPLR KAVSKFIESY LVWKLPLVKY
GLKPDHPFEE DYASCQMAIL PENFFSEADK GKIQFKRASK WWFWNGGIEF DDNTKLQADV
VLLASGYEGK KKIQTLLPEP FSSLVLDSSG IMPLYRGTIH PLIPNMAFVG YIESVSNLHT
AELRCKWLSR LADGFFKLPS IEKMLEQNSK ELEIMKKTTR FYKRHCISTF SINHSDEICE
EMGWKSWRKN NWLLEAFAPY NSQDYGQDN
//
