ID   6OMT_COPJA              Reviewed;         347 AA.
AC   Q9LEL6;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=(RS)-norcoclaurine 6-O-methyltransferase;
DE            EC=2.1.1.128;
DE   AltName: Full=S-adenosyl-L-methionine:norcoclaurine 6-O-methyltransferase;
DE            Short=6-OMT;
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].
RX   PubMed=10811648; DOI=10.1074/jbc.m002439200;
RA   Morishige T., Tsujita T., Yamada Y., Sato F.;
RT   "Molecular characterization of the S-adenosyl-L-methionine: 3'-hydroxy-N-
RT   methylcoclaurine 4'O-methyltransferase involved in isoquinoline alkaloid
RT   biosynthesis in Coptis japonica.";
RL   J. Biol. Chem. 275:23398-23405(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 88-103, FUNCTION, CATALYTIC ACTIVITY, AND REACTION
RP   MECHANISM.
RX   PubMed=7925429; DOI=10.1111/j.1432-1033.1994.00125.x;
RA   Sato F., Tsujita T., Katagiri Y., Yoshida S., Yamada Y.;
RT   "Purification and characterization of S-adenosyl-L-methionine:
RT   norcoclaurine 6-O-methyltransferase from cultured Coptis japonica cells.";
RL   Eur. J. Biochem. 225:125-131(1994).
CC   -!- FUNCTION: Catalyzes the transfer of the S-methyl group of S-adenosyl-L-
CC       methionine (AdoMet) to the 6-hydroxyl group of norcoclaurine to form
CC       coclaurine. {ECO:0000269|PubMed:7925429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=norcoclaurine + S-adenosyl-L-methionine = coclaurine + H(+) +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19941, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58481, ChEBI:CHEBI:58482,
CC         ChEBI:CHEBI:59789; EC=2.1.1.128;
CC         Evidence={ECO:0000269|PubMed:7925429};
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC       reticuline from (S)-norcoclaurine: step 1/4.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; D29811; BAB08004.1; -; mRNA.
DR   AlphaFoldDB; Q9LEL6; -.
DR   SMR; Q9LEL6; -.
DR   KEGG; ag:BAB08004; -.
DR   BioCyc; MetaCyc:MON-8423; -.
DR   BRENDA; 2.1.1.128; 1610.
DR   SABIO-RK; Q9LEL6; -.
DR   UniPathway; UPA00306; UER00441.
DR   GO; GO:0030786; F:(RS)-norcoclaurine 6-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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   Direct protein sequencing; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..347
FT                   /note="(RS)-norcoclaurine 6-O-methyltransferase"
FT                   /id="PRO_0000204433"
FT   ACT_SITE        253
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         192
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         236
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   347 AA;  38700 MW;  2BC34B3FBE67167C CRC64;
     MEVKKDNLSS QAKLWNFIYG FAESLVLKCA VQLDLANIIH NSGTSMTLSE LSSRLPSQPV
     NEDALYRVMR YLVHMKLFTK ASIDGELRYG LAPPAKYLVK GWDKCMVGSI LAITDKDFMA
     PWHYLKDGLS GESGTAFEKA LGTNIWGYMA EHPEKNQLFN EAMANDSRLI MSALVKECGN
     IFNGITTLVD VGGGTGTAVR NIANAFPHIK CTVYDLPHVI ADSPGYSEVH CVAGDMFKFI
     PKADAIMMKC ILHDWDDKEC IEILKRCKEA VPVKGGKVII VDIVLNVQSE HPYTKMRLTL
     DLDMMLNTGG KERTEEEWKK LIHDAGYKGH KITQITAVQS VIEAYPY