ID   N7OMT_PAPSO             Reviewed;         357 AA.
AC   C7SDN9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Norreticuline-7-O-methyltransferase {ECO:0000303|PubMed:19500305};
DE            EC=2.1.1.- {ECO:0000305};
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:ACN88562.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19500305; DOI=10.1111/j.1365-313x.2009.03937.x;
RA   Pienkny S., Brandt W., Schmidt J., Kramell R., Ziegler J.;
RT   "Functional characterization of a novel benzylisoquinoline O-
RT   methyltransferase suggests its involvement in papaverine biosynthesis in
RT   opium poppy (Papaver somniferum L).";
RL   Plant J. 60:56-67(2009).
RN   [2]
RP   FUNCTION.
RX   PubMed=22725256; DOI=10.1111/j.1365-313x.2012.05084.x;
RA   Desgagne-Penix I., Facchini P.J.;
RT   "Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes
RT   reveals the major route to papaverine in opium poppy.";
RL   Plant J. 72:331-344(2012).
RN   [3]
RP   FUNCTION.
RX   PubMed=23738019; DOI=10.1371/journal.pone.0065622;
RA   Pathak S., Lakhwani D., Gupta P., Mishra B.K., Shukla S., Asif M.H.,
RA   Trivedi P.K.;
RT   "Comparative transcriptome analysis using high papaverine mutant of Papaver
RT   somniferum reveals pathway and uncharacterized steps of papaverine
RT   biosynthesis.";
RL   PLoS ONE 8:E65622-E65622(2013).
CC   -!- FUNCTION: Involved in the biosynthesis of benzylisoquinoline alkaloids
CC       (PubMed:19500305). Catalyzes specifically the methylation of
CC       norreticuline at position seven to produce norlaudanine
CC       (PubMed:19500305). No activity with norcoclaurine, reticuline,
CC       norlaudanosoline, norisoorientaline, scoulerine, salutaridinol,
CC       oripavine, salsolinol, codeine or morphine (PubMed:19500305). Involved
CC       in papaverine biosynthesis (PubMed:22725256, PubMed:23738019).
CC       {ECO:0000269|PubMed:19500305, ECO:0000269|PubMed:22725256,
CC       ECO:0000269|PubMed:23738019}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=44 uM for norreticuline {ECO:0000269|PubMed:19500305};
CC         KM=19 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19500305};
CC         Note=kcat is 0.074 sec(-1) for norreticuline.
CC         {ECO:0000269|PubMed:19500305};
CC       pH dependence:
CC         Optimum pH is between 7.0 and 9.5. {ECO:0000269|PubMed:19500305};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:19500305};
CC   -!- TISSUE SPECIFICITY: Expressed instems, leaves, roots and seedlings.
CC       {ECO:0000269|PubMed:19500305}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; FJ156103; ACN88562.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7SDN9; -.
DR   SMR; C7SDN9; -.
DR   KEGG; ag:ACN88562; -.
DR   BioCyc; MetaCyc:MON-18210; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..357
FT                   /note="Norreticuline-7-O-methyltransferase"
FT                   /id="PRO_0000433986"
FT   ACT_SITE        263
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         225
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   357 AA;  39701 MW;  D1682F6B4E08953F CRC64;
     MEVVSQIDQE NQAIIWKQIY GFSESLLLKC AVQCEIAETI HNHGTPMSIL ELAAKLPIDQ
     PVNIDRLYRV MRYLVHQKLF NKEVISTLNG GTVQVTEKYW LAPPAKYLIR GSQQSMVPSV
     LGIIDEDMFA PWHILKDSLT GECNIFETAL GKSISVYMSE NPEMNQISNG AMAFDSGLVT
     SHLVNECKSV FGDEIKTLVD VGGGTGTALR AISKAFPNIK CTLFDLPHVI ADSPEIPTIT
     KVSGDMFKSI PSADAIFMKN ILHDWNDDEC IQILKRCKDV VSAGGKLIMV EMVLDEDSFH
     PYSKLRLTSD IDMMVNNGGK ERTEKEWEKL FDAAGFASCK FTQMSVGFAA QSIIEVY