4OMT_COPJA
ID 4OMT_COPJA Reviewed; 350 AA.
AC Q9LEL5;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase;
DE EC=2.1.1.116;
DE AltName: Full=S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase;
DE Short=4'-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], AND CHARACTERIZATION.
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).
CC -!- FUNCTION: Catalyzes the transfer of the methyl group to the 4'-hydroxyl
CC group of 3'-hydroxy-N-methylcoclaurine to form reticuline.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3'-hydroxy-N-methylcoclaurine + S-adenosyl-L-methionine =
CC (S)-reticuline + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57873, ChEBI:CHEBI:58010, ChEBI:CHEBI:59789;
CC EC=2.1.1.116;
CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC reticuline from (S)-norcoclaurine: step 4/4.
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; D29812; BAB08005.1; -; mRNA.
DR AlphaFoldDB; Q9LEL5; -.
DR SMR; Q9LEL5; -.
DR KEGG; ag:BAB08005; -.
DR BioCyc; MetaCyc:MON-8441; -.
DR BRENDA; 2.1.1.116; 1610.
DR UniPathway; UPA00306; UER00444.
DR GO; GO:0030784; F:3'-hydroxy-N-methyl-(S)-coclaurine 4'-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 Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..350
FT /note="3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-
FT methyltransferase"
FT /id="PRO_0000204430"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 350 AA; 38776 MW; 547835EBCDEF9182 CRC64;
MAFHGKDDVL DIKAQAHVWK IIYGFADSLV LRCAVELGIV DIIDNNNQPM ALADLASKLP
VSDVNCDNLY RILRYLVKME ILRVEKSDDG QKKYALEPIA TLLSRNAKRS MVPMILGMTQ
KDFMTPWHSM KDGLSDNGTA FEKAMGMTIW EYLEGHPDQS QLFNEGMAGE TRLLTSSLIS
GSRDMFQGID SLVDVGGGNG TTVKAISDAF PHIKCTLFDL PHVIANSYDL PNIERIGGDM
FKSVPSAQAI ILKLILHDWN DEDSIKILKQ CRNAVPKDGG KVIIVDVALD EESDHELSST
RLILDIDMLV NTGGKERTKE VWEKIVKSAG FSGCKIRHIA AIQSVIEVFP