STOX_BERWI
ID STOX_BERWI Reviewed; 530 AA.
AC F1BVB6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Tetrahydroberberine oxidase {ECO:0000303|PubMed:3402447};
DE Short=THB oxidase {ECO:0000305};
DE EC=1.3.3.8 {ECO:0000269|PubMed:21327819, ECO:0000269|PubMed:3402447};
DE AltName: Full=(S)-tetrahydroprotoberberine oxidase {ECO:0000303|PubMed:21327819};
DE Short=BwSTOX {ECO:0000303|PubMed:21327819};
DE Flags: Precursor;
OS Berberis wilsoniae (Mrs Wilson's barberry).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Berberidoideae;
OC Berberis.
OX NCBI_TaxID=258211;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3402447; DOI=10.1111/j.1432-1033.1988.tb14160.x;
RA Amann M., Nagakura N., Zenk M.H.;
RT "Purification and properties of (S)-tetrahydroprotoberberine oxidase from
RT suspension-cultured cells of Berberis wilsoniae.";
RL Eur. J. Biochem. 175:17-25(1988).
CC -!- FUNCTION: Catalyzes the oxidation of different
CC tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and
CC (S)-corypalmine (PubMed:3402447). Catalyzes the oxidation of (S)-
CC coreximine and (S)-tetrahydropalmatine (PubMed:3402447,
CC PubMed:21327819). Catalyzes the oxidation of different 1-
CC benzylisoquinoline alkaloids, such as (S)-norreticuline, (S)-
CC nororientaline, (S)-coclaurine and (S)-norisoorientaline
CC (PubMed:3402447). Exhibits strict specificity for the (S)-enantiomer of
CC tetrahydroprotoberbirines and 1-benzylisoquinoline alkaloids
CC (PubMed:3402447). {ECO:0000269|PubMed:21327819,
CC ECO:0000269|PubMed:3402447}.
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, ECO:0000269|PubMed:3402447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13490;
CC Evidence={ECO:0000269|PubMed:21327819, ECO:0000269|PubMed:3402447};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21327819, ECO:0000269|PubMed:3402447};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000250|UniProtKB:O64743};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.3 uM for (S)-canadine {ECO:0000269|PubMed:3402447};
CC KM=25 uM for (S)-scoulerine {ECO:0000269|PubMed:3402447};
CC KM=4.3 uM for (S)-tetrahydropalmatine {ECO:0000269|PubMed:3402447};
CC KM=0.7 uM for (S)-corypalmine {ECO:0000269|PubMed:3402447};
CC pH dependence:
CC Optimum pH is 8.9. {ECO:0000269|PubMed:3402447};
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}.
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DR EMBL; HQ116697; ADY15026.1; -; mRNA.
DR SMR; F1BVB6; -.
DR KEGG; ag:ADY15026; -.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..530
FT /note="Tetrahydroberberine oxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5003263162"
FT DOMAIN 72..246
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..94
FT /evidence="ECO:0000250|UniProtKB:P30986"
FT CROSSLNK 109..171
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 530 AA; 58990 MW; FE7B47FA37E5D892 CRC64;
MSKMASSIFA TFSLLSSLLP TSLASSDANY EDFLQCLDLY SQNSIPVYTR NTSSYTSILE
STIKNLVFLS PTTPKPNFIV TPMQESHVQT SVICCRMHGL QMRIRSGGHD FEGLSYVSNV
PFVVLDLIHL KTINVDIEEN SAWVQTGATI GELYYRIAEK VGVHAFPAGL CPTVGVGGHI
SGAGYGVLMR KYGVSADHVI DARIVNVDGE ILDRESMGED LFWAIRGGGG ASFGVILAWK
IRLVPVPPTV TIFIVPKTLE EGATALLHKW QFIGDNVHED LFIGLSMRSV IISPKGDKTI
LVSFIGLFLG GSDKLVQHME QSFPELGVKP HDCIEMSWIK STVVFGVFSN DASLSVLLDR
KNPFPPKSYH KVKSDYVTEP LPISVLEGIC HRFLKNGVNK AEIIMSPYGG RMNEISESEI
AFPHRKGNLY KINYIAEWEE AGSMENHLSW IRELYRYMTP YVSKSPRSSY LNFKDIDLGQ
TKNGTATYSQ AKAWGSKYFK NNFKRLMQVK TKVDPNNFFC NEQGIPPFSS
