SNO1_TYRJA
ID SNO1_TYRJA Reviewed; 456 AA.
AC Q8MP06;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Senecionine N-oxygenase;
DE Short=SNO;
DE EC=1.14.13.101;
DE Flags: Precursor;
GN Name=sno1;
OS Tyria jacobaeae (Cinnabar moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Erebidae; Arctiinae; Callimorphini; Tyria.
OX NCBI_TaxID=179666;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-60; 70-85 AND 365-374,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Larva;
RX PubMed=11972041; DOI=10.1073/pnas.082674499;
RA Naumann C., Hartmann T., Ober D.;
RT "Evolutionary recruitment of a flavin-dependent monooxygenase for the
RT detoxification of host plant-acquired pyrrolizidine alkaloids in the
RT alkaloid-defended arctiid moth Tyria jacobaeae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6085-6090(2002).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9182998; DOI=10.1111/j.1432-1033.1997.00626.x;
RA Lindigkeit R., Biller A., Buch M., Schiebel H.M., Boppre M., Hartmann T.;
RT "The two facies of pyrrolizidine alkaloids: the role of the tertiary amine
RT and its N-oxide in chemical defense of insects with acquired plant
RT alkaloids.";
RL Eur. J. Biochem. 245:626-636(1997).
CC -!- FUNCTION: NADPH-dependent monooxygenase that detoxifies senecionine and
CC similar plant alkaloids that are ingested by the larvae. Is active
CC towards a narrow range of related substrates with highest activity
CC towards senecionine, followed by seneciphylline, retrorsine,
CC monocrotaline, senecivernine, axillarine and axillaridine.
CC {ECO:0000269|PubMed:9182998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + O2 + senecionine = H2O + NADP(+) + senecionine N-
CC oxide; Xref=Rhea:RHEA:11420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:52070, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:77617; EC=1.14.13.101;
CC Evidence={ECO:0000269|PubMed:11972041, ECO:0000269|PubMed:9182998};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11972041, ECO:0000269|PubMed:9182998};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=456 nm {ECO:0000269|PubMed:9182998};
CC Kinetic parameters:
CC KM=1.4 uM for senecionine {ECO:0000269|PubMed:9182998};
CC KM=1.3 uM for NADPH {ECO:0000269|PubMed:9182998};
CC KM=12.5 uM for monocrotaline {ECO:0000269|PubMed:9182998};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:9182998};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:9182998};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9182998}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:9182998}.
CC -!- MISCELLANEOUS: Larvae store pyrrolizidine alkaloids from their host
CC plant S.jacobaeae as non-toxic N-oxides. This serves as protection
CC against insectivores; after ingestion of the larvae, the N-oxides are
CC reduced in the gut of the insectivores to form toxic alkaloids
CC (PubMed:11972041). {ECO:0000305|PubMed:11972041}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AJ420233; CAD12369.1; -; mRNA.
DR AlphaFoldDB; Q8MP06; -.
DR SMR; Q8MP06; -.
DR PRIDE; Q8MP06; -.
DR KEGG; ag:CAD12369; -.
DR BioCyc; MetaCyc:MON-16767; -.
DR BRENDA; 1.14.13.101; 6769.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0033784; F:senecionine N-oxygenase activity; IDA:UniProtKB.
DR GO; GO:0009820; P:alkaloid metabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 2.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:11972041"
FT CHAIN 23..456
FT /note="Senecionine N-oxygenase"
FT /id="PRO_5000068127"
FT BINDING 32..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 215..220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 52232 MW; 3AE4ADD925D96932 CRC64;
MFRKFVIMLV LSLLVAAGIS QASSASRVCI IGAGYSGLAT ARYLQDYGLN YTIFEATPNI
GGTWRYDPRV GTDEDGIPIY SSNYKNLRVN SPVDLMTYHG YEFQEGTRSF ISGNCFYKYM
KSFVRHFGLM ENIQVRSLVT WVQRTEDKWN LTYMKTDTRK NYTEECDFVV VASGEFSTPK
IPHIKGQEEY KGKTMHSHDY KEAESFRGQR VLVIGAGPSG LDVVMQLSNI TSKLVHSQHI
LKSWHIFNQP DFPGNFISKP NVKHFTANGA VFEDDTVEEF DMVIYCTGFY YNHPFLSTLS
SGITATENYV MPLYQQVVNI NQPTMTFVGI CKPFFAKLLD QQAHYSAKLA AGHFKLPSQD
KMLRHWLEHV QMLREAQFKI TDVNSVGPNV DEYFKALHKE AGVPLLPPVY ASVFVFSGKT
LLEDLQNYRE YDYRIISDTQ FKKKYNPREE VCPYDD
