6OMT_COPJA
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