ID   STOX_ARGME              Reviewed;         543 AA.
AC   F1BVB7;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Tetrahydroberberine oxidase {ECO:0000305};
DE            Short=THB oxidase {ECO:0000305};
DE            EC=1.3.3.8 {ECO:0000269|PubMed:21327819};
DE   AltName: Full=(S)-tetrahydroprotoberberine oxidase {ECO:0000303|PubMed:21327819};
DE            Short=AmSTOX {ECO:0000303|PubMed:21327819};
DE   Flags: Precursor;
OS   Argemone mexicana (Mexican prickly poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Argemone.
OX   NCBI_TaxID=54796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=21327819; DOI=10.1007/s00425-011-1357-4;
RA   Gesell A., Diaz Chavez M.L., Kramell R., Piotrowski M., Macheroux P.,
RA   Kutchan T.M.;
RT   "Heterologous expression of two FAD-dependent oxidases with (S)-
RT   tetrahydroprotoberberine oxidase activity from Argemone mexicana and
RT   Berberis wilsoniae in insect cells.";
RL   Planta 233:1185-1197(2011).
CC   -!- FUNCTION: Catalyzes the oxidation of different
CC       tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and
CC       (S)-tetrahydropalmatine. {ECO:0000269|PubMed:21327819}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-canadine + H(+) + 2 O2 = berberine + 2 H2O2;
CC         Xref=Rhea:RHEA:13489, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16118, ChEBI:CHEBI:16240, ChEBI:CHEBI:16592; EC=1.3.3.8;
CC         Evidence={ECO:0000269|PubMed:21327819};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13490;
CC         Evidence={ECO:0000269|PubMed:21327819};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:21327819};
CC       Note=Binds 1 FAD per subunit in a bicovalent manner.
CC       {ECO:0000250|UniProtKB:O64743};
CC   -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC       N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:O64743}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ116698; ADY15027.1; -; mRNA.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050328; F:tetrahydroberberine oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Nucleotide-binding;
KW   Oxidoreductase; Signal; Thioether bond.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..543
FT                   /note="Tetrahydroberberine oxidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003264860"
FT   DOMAIN          75..250
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        37..97
FT                   /evidence="ECO:0000250|UniProtKB:P30986"
FT   CROSSLNK        112..175
FT                   /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT                   Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:O64743"
SQ   SEQUENCE   543 AA;  61398 MW;  E10D21B36265163F CRC64;
     MIPNSSSSSI LSLLVLLLFS TSSSWATNSI HEDFLNCLSI YKSSFPIPIY TSKNSSFNTL
     FRSSARNLRF LSPNSTQKPE FIITPTLESH VQTTVVCSKK HGLDLKVRSG GHDVEGLSYV
     SDSPYVMIDL VDFRNITVNV KNATAWIQAG SSLGEVYYKV GNESKNTLGF PAGFCPTVGV
     GGHISGGGFG SLVRKYGLAS DQVIDARIVT VNGEILNKET MGKDLYWAIR GGGANNFGVL
     LSWKVKLVPV TPIVTVATID RTLEQGATNL VHKWQFVADR LHEDVYIGLT MVTANTSRAG
     EKTVVAQFSF LFLGNTDRLL QIMEESFPEL GLKRNDTTEM SWVESHVYFY RRGQPIEFLW
     DRDHLTKSFL KVKSDYVREP ISKLGLEGIW KRYVGGDSPA MLWTPFGGRM NQISEFESPY
     PHRAGNIYNI MYVGNWLNEN ESEKQLNWMR SFYSYMGRYV SKNPRSAYLN YKDLDLGVND
     NNVSEYIRYL KARSWGRKYF KNNFEKLVKV KSMVDPDNFF KNKQSIPPIR SWGKELEAIN
     IVI