ID A0A5P1E5N3_ASPOF Unreviewed; 924 AA.
AC A0A5P1E5N3;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN ORFNames=A4U43_C10F18580 {ECO:0000313|EMBL:ONK57293.1};
OS Asparagus officinalis (Garden asparagus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Asparagoideae; Asparagus.
OX NCBI_TaxID=4686 {ECO:0000313|EMBL:ONK57293.1, ECO:0000313|Proteomes:UP000243459};
RN [1] {ECO:0000313|Proteomes:UP000243459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH0086 {ECO:0000313|Proteomes:UP000243459};
RX PubMed=29093472; DOI=10.1038/s41467-017-01064-8;
RA Harkess A., Zhou J., Xu C., Bowers J.E., Van der Hulst R., Ayyampalayam S.,
RA Mercati F., Riccardi P., McKain M.R., Kakrana A., Tang H., Ray J.,
RA Groenendijk J., Arikit S., Mathioni S.M., Nakano M., Shan H.,
RA Telgmann-Rauber A., Kanno A., Yue Z., Chen H., Li W., Chen Y., Xu X.,
RA Zhang Y., Luo S., Chen H., Gao J., Mao Z., Pires J.C., Luo M., Kudrna D.,
RA Wing R.A., Meyers B.C., Yi K., Kong H., Lavrijsen P., Sunseri F.,
RA Falavigna A., Ye Y., Leebens-Mack J.H., Chen G.;
RT "The asparagus genome sheds light on the origin and evolution of a young Y
RT chromosome.";
RL Nat. Commun. 8:1279-1279(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.168;
CC Evidence={ECO:0000256|ARBA:ARBA00035920};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361177};
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|RuleBase:RU361177}.
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DR EMBL; CM007390; ONK57293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5P1E5N3; -.
DR EnsemblPlants; ONK57293; ONK57293; A4U43_C10F18580.
DR Gramene; ONK57293; ONK57293; A4U43_C10F18580.
DR Proteomes; UP000243459; Chromosome 10.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:RHEA.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR PANTHER; PTHR43539:SF11; INDOLE-3-PYRUVATE MONOOXYGENASE YUCCA8-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF13456; RVT_3; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 3.
DR PROSITE; PS50879; RNASE_H_1; 1.
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|RuleBase:RU361177};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Reference proteome {ECO:0000313|Proteomes:UP000243459}.
FT DOMAIN 713..839
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 507..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..685
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 102556 MW; 18F65D8E3686FC6C CRC64;
MGPFVPDNYD FLSRRCMWVN GPIVIGAGPS GLAVAASLKE RGVPYVILER SDCIASLWQK
RTYDRLKLHL PKQFCQLPGL PFPESYPEYP CKKQFIDYLE SYVKHFEISP KFNQSVQSAR
YDEISNLWRV KTVGKNHEEI EYIGKWLVVA TGENAESVVP EMDGLGSFGS QITHVCDYKS
GEAYRGKKVL VVGCGNSGME VCLDLCDNEA FPSMVVRDSV HVLPREVYGK SMFELAVFLM
KWLPLWLVDK IMLVLAWLVL GNIENYGLKR PSVGPLELKN THGRTPVLDY GALSKIKSGE
IEVVPAVKRF LPGGVEFADG RVDDFDAVVM ATGYRSNVPY WLQGGTDFFS KNGLPKAQFP
NSWKGKSGLY AVGFTKRGLA GASADAIKVA KDLGKAWKEE TKQAKRLVSC HRRFVTYFRS
FRLNENTTCT RYFHKASEEL QITTPKGSER DVFLKKNPKL PSFRDHLLDV DFFSLFKKGD
MTIVFSAQYV LGNECNSGFS GLKPRVLSSR SNDRSKGCTP TANHTTTTTT GTTTATATAT
AMSTMTAGGH AGSDDGCETR SGTRMLRWMS TLIKGKMETV VLIMLNWMIQ RLSWIRLGFD
LVWLESLYSM QMAELCMGSN WDSEEDNGNP DDYHYDLAGN DSGLRDFATL HGGNQVHDSY
DSEDTEQDSE NDYGYHEDDN SDSGDDDASN SYVVTLHGED HGHNSYHAED REQRGKIYLE
FDGASKGNPG RAGGGAVLKS EDGTVITRMR QGLGTATNND AEYESLKSGL KIARDMGYDK
IHVKGDSKLV YKQEYQDYEE TDSYQSEEDI EEVYLEFDGA SRGNPGRAGA GAVLKFEDGA
VVYLEFDGAS RGNPGRAGAI AALKSKDGAV VVNQRLGIGM DNNAQYRALI RGLKTALNMG
YDGTCVRGHL KLVCKQISYI NHDK
//
