NCS2_PAPSO
ID NCS2_PAPSO Reviewed; 231 AA.
AC Q4QTJ1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=S-norcoclaurine synthase 2 {ECO:0000303|PubMed:15925393};
DE Short=PsNCS2 {ECO:0000303|PubMed:15925393};
DE EC=4.2.1.78 {ECO:0000269|PubMed:15925393};
DE Flags: Precursor;
GN Name=NCS2 {ECO:0000303|PubMed:15925393};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000312|EMBL:AAX56304.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15925393; DOI=10.1016/j.phytochem.2005.04.029;
RA Liscombe D.K., Macleod B.P., Loukanina N., Nandi O.I., Facchini P.J.;
RT "Evidence for the monophyletic evolution of benzylisoquinoline alkaloid
RT biosynthesis in angiosperms.";
RL Phytochemistry 66:1374-1393(2005).
RN [2]
RP TISSUE SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11722126; DOI=10.1007/s004250100581;
RA Samanani N., Facchini P.J.;
RT "Isolation and partial characterization of norcoclaurine synthase, the
RT first committed step in benzylisoquinoline alkaloid biosynthesis, from
RT opium poppy.";
RL Planta 213:898-906(2001).
RN [3]
RP TISSUE SPECIFICITY, INDUCTION BY ELICITOR, AND SUBCELLULAR LOCATION.
RX PubMed=21037103; DOI=10.1105/tpc.110.077958;
RA Lee E.J., Facchini P.;
RT "Norcoclaurine synthase is a member of the pathogenesis-related 10/Bet v1
RT protein family.";
RL Plant Cell 22:3489-3503(2010).
CC -!- FUNCTION: Involved in the biosynthesis of (S)-coclaurine, the common
CC precursor of all benzylisoquinoline alkaloids such as morphine,
CC sanguinarine, codeine or papaverine. Condenses dopamine and 4-
CC hydroxyphenylacetaldehyde. {ECO:0000269|PubMed:15925393}.
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:0000269|PubMed:15925393};
CC -!- ACTIVITY REGULATION: Activity doubles within 5 hours of elicitor
CC treatment and continues to increase for at least 80 hours.
CC {ECO:0000269|PubMed:11722126}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.02 mM for 4-hydroxyphenylacetaldehyde
CC {ECO:0000269|PubMed:11722126};
CC Note=Sigmoidal saturation kinetics suggesting positive cooperativity
CC in the binding of dopamine. {ECO:0000269|PubMed:11722126};
CC pH dependence:
CC Optimum pH is between 6.5 and 7.0. {ECO:0000269|PubMed:11722126};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:11722126};
CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21037103}; Single-pass membrane protein
CC {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:21037103}; Single-
CC pass membrane protein {ECO:0000255}. Note=Initially localized to the
CC endoplasmic reticulum but subsequently sorted to the vacuole.
CC {ECO:0000269|PubMed:21037103}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves
CC (PubMed:11722126, PubMed:21037103). Detected in flower buds and
CC germinating seeds (PubMed:11722126). Low expression in carpels
CC (PubMed:21037103). Restricted to sieve elements of the phloem adjacent
CC or proximal to laticifers (PubMed:21037103).
CC {ECO:0000269|PubMed:11722126, ECO:0000269|PubMed:21037103}.
CC -!- INDUCTION: Up-regulated by elicitor treatment.
CC {ECO:0000269|PubMed:21037103}.
CC -!- MISCELLANEOUS: The 40 amino acid N-terminal extension should included a
CC signal peptide targeting the mature protein to the endoplasmic
CC reticulum. {ECO:0000305|PubMed:21037103}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
CC -!- CAUTION: The tissue specificity and the characterization shown in
CC PubMed:11722126 are from a soluble protein extract not making the
CC distinction between the two proteins produced by NCS1 and NCS2.
CC {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; AY860501; AAX56304.1; -; mRNA.
DR AlphaFoldDB; Q4QTJ1; -.
DR SMR; Q4QTJ1; -.
DR PRIDE; Q4QTJ1; -.
DR BRENDA; 4.2.1.78; 4515.
DR UniPathway; UPA00306; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050474; F:(S)-norcoclaurine synthase activity; IDA:UniProtKB.
DR GO; GO:1901010; P:(S)-reticuline metabolic process; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0002238; P:response to molecule of fungal origin; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alkaloid metabolism; Endoplasmic reticulum; Lyase; Membrane; Signal;
KW Transmembrane; Transmembrane helix; Vacuole.
FT SIGNAL 1..?
FT /evidence="ECO:0000305|PubMed:21037103"
FT CHAIN ?..231
FT /note="S-norcoclaurine synthase 2"
FT /id="PRO_0000433980"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q67A25"
FT BINDING 107..109
FT /ligand="dopamine"
FT /ligand_id="ChEBI:CHEBI:59905"
FT /evidence="ECO:0000250|UniProtKB:Q67A25"
FT BINDING 140
FT /ligand="(4-hydroxyphenyl)acetaldehyde"
FT /ligand_id="ChEBI:CHEBI:15621"
FT /evidence="ECO:0000250|UniProtKB:Q67A25"
SQ SEQUENCE 231 AA; 26001 MW; BE03A3B6911D8E3B CRC64;
MSKLITTEPL KSMAEVISNY VIQRESFSAR NILNKNSLVK KEIRYDLEVP TSADSIWSVY
SCPDIPRLLR DVLLPGVFQK LDVIEGNGGV GTVLDIVFPP GAVPRSYKEK FVNINHEKRL
KEVIMIEGGY LDMGCTFYMD RIHIFEKTPN SCVIESSIIY EVKEEYAGKM AKLITTEPLE
SMAEVISGYV LKKRLQVFGF EIKPKLRFNL LLCLIICLVI AGGMFVAGVP L
