ID   NCS1_COPJA              Reviewed;         352 AA.
AC   A2A1A0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=S-norcoclaurine synthase 1;
DE            Short=CjNCS1;
DE            EC=4.2.1.78;
GN   Name=NCS1;
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, SUBUNIT, AND INHIBITION BY
RP   O-PHENANTHROLINE.
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 phenylacetaldehyde, 3,4-
CC       dihydrophenylacetaldehyde or 4-hydroxyphenylacetaldehyde.
CC       {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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by O-phenanthroline, but not by EDTA.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17204481}.
CC   -!- MISCELLANEOUS: NCS1 is a 2-oxoglutarate-independent dioxygenase-like
CC       protein that catalyzed the cyclase reaction without oxygen.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB267398; BAF45337.1; -; mRNA.
DR   AlphaFoldDB; A2A1A0; -.
DR   SMR; A2A1A0; -.
DR   PRO; PR:A2A1A0; -.
DR   GO; GO:0050474; F:(S)-norcoclaurine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Iron; Lyase; Metal-binding; Oxidoreductase.
FT   CHAIN           1..352
FT                   /note="S-norcoclaurine synthase 1"
FT                   /id="PRO_0000358939"
FT   DOMAIN          200..304
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         228
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         230
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         285
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   352 AA;  39964 MW;  726AB1DB46111732 CRC64;
     MSKNLTGVGG SLPVENVQVL AGKELKNLPN RYVRPELEHD DVVPIDNSLE IPVIDLSRLL
     DQQYACDELA KFHSACLDWG FFQLINHGVR EEVIEKMKVD TEDFFRLPFK EKNAYRQLPN
     GMEGYGQAFV TSEEQKLDWA DMHFLITKPV QERNMRFWPT SPTSFRETME KYSMELQKVA
     MCLTGMMAKN LGLESEILTK PLRTVFNRED ELLPSMSSCG EGLGLSPHSD ATGLTLLIQV
     NEVNGLHIKK DEKWVPIKPI LGAFVVNIGD VIEIMSNGIY KSIEHRAVIN TDKERLSIAA
     FHDPEYGTKI GPLPDLVKEN GVKYKTIDYE DYLIRSSNIK LDGKSLLDQM KL