ID A0A061G5C9_THECC Unreviewed; 476 AA.
AC A0A061G5C9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN ORFNames=TCM_016016 {ECO:0000313|EMBL:EOY24407.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY24407.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY24407.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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}.
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DR EMBL; CM001881; EOY24407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061G5C9; -.
DR EnsemblPlants; EOY24407; EOY24407; TCM_016016.
DR Gramene; EOY24407; EOY24407; TCM_016016.
DR HOGENOM; CLU_006909_3_0_1; -.
DR OMA; FMEWEHH; -.
DR Proteomes; UP000026915; Chromosome 3.
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; 2.
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; 2.
DR PIRSF; PIRSF000332; FMO; 2.
DR PRINTS; PR00370; FMOXYGENASE.
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:UP000026915}.
SQ SEQUENCE 476 AA; 54081 MW; 3BDDB18B46B1C13F CRC64;
MNLAMPPAFP SVKSRHVAVV GAGAAGLVAA RELRREGHSV VVFERGNEVG GTWVYTPRVE
PDPLGIDPTR PIVHTSLYSS LRTNLPREVM GFTDFPFITL AGENRDPRRF PGHREVLMYL
KDFAREFEVK EMVRFETEVV KVWILENGKW KVRSKKTIFF NNENNDHYNA DIDNINKSEV
ELDDEIYDAV VVCNGHHTEP RIAEIPGINL WPGKQMHSHN YRVPESFTDQ VVILIGSSSS
AVDICRDVAG VAKEVHVASR SVAHETYTKQ PGYDNLWIHS MIDAAHEDGT VVFQNGKVVL
ADVIMHCTGY KYQFPFLDTN GIVTVDDNRL GPLYKHVFPP ALAPWLSFIG IPWKIAPFPL
FEFQSKWIAG VLSGRITLPS QKEMMEDIKA FYSTLEASGV PKRYTHKMGE SQFEYNNWLA
AQCGCQGIEK WRKQIYLAAS ANKHLRPDTY RDEWEDHDLV LEAHEDFVKY TSKSDS
//
