ID   NCS2_COPJA              Reviewed;         196 AA.
AC   A2A1A1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=S-norcoclaurine synthase 2;
DE            EC=4.2.1.78 {ECO:0000250|UniProtKB:Q67A25};
DE   AltName: Full=Pathogenesis related protein 10A;
DE            Short=CjPR10A;
DE   Flags: Precursor;
GN   Name=PR10A;
OS   Coptis japonica (Japanese goldthread).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC   Coptis.
OX   NCBI_TaxID=3442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INHIBITION.
RC   STRAIN=cv. dissecta;
RX   PubMed=17204481; DOI=10.1074/jbc.m608933200;
RA   Minami H., Dubouzet E., Iwasa K., Sato F.;
RT   "Functional analysis of norcoclaurine synthase in Coptis japonica.";
RL   J. Biol. Chem. 282:6274-6282(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of the common precursor of all
CC       benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or
CC       berberine. Condenses dopamine and pyruvic acid or 4-
CC       hydroxyphenylpyruvate. {ECO:0000269|PubMed:17204481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine +
CC         H2O; Xref=Rhea:RHEA:16173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15621,
CC         ChEBI:CHEBI:58253, ChEBI:CHEBI:59905; EC=4.2.1.78;
CC         Evidence={ECO:0000250|UniProtKB:Q67A25};
CC   -!- ACTIVITY REGULATION: Not inhibited by O-phenanthroline or EDTA.
CC   -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR   EMBL; AB267399; BAF45338.2; -; mRNA.
DR   AlphaFoldDB; A2A1A1; -.
DR   SMR; A2A1A1; -.
DR   BRENDA; 4.2.1.78; 1610.
DR   GO; GO:0050474; F:(S)-norcoclaurine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR000916; Bet_v_I/MLP.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   Pfam; PF00407; Bet_v_1; 1.
PE   2: Evidence at transcript level;
KW   Alkaloid metabolism; Lyase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..196
FT                   /note="S-norcoclaurine synthase 2"
FT                   /id="PRO_0000358942"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q67A25"
FT   BINDING         104..106
FT                   /ligand="dopamine"
FT                   /ligand_id="ChEBI:CHEBI:59905"
FT                   /evidence="ECO:0000250|UniProtKB:Q67A25"
FT   BINDING         137
FT                   /ligand="(4-hydroxyphenyl)acetaldehyde"
FT                   /ligand_id="ChEBI:CHEBI:15621"
FT                   /evidence="ECO:0000250|UniProtKB:Q67A25"
SQ   SEQUENCE   196 AA;  22160 MW;  52EA8EA013A8D9A8 CRC64;
     MRMEVVLVVF LMFIGTINCE RLIFNGRPLL HRVTKEETVM LYHELEVAAS ADEVWSVEGS
     PELGLHLPDL LPAGIFAKFE ITGDGGEGSI LDMTFPPGQF PHHYREKFVF FDHKNRYKLV
     EQIDGDFFDL GVTYYMDTIR VVATGPDSCV IKSTTEYHVK PEFAKIVKPL IDTVPLAIMS
     EAIAKVVLEN KHKSSE