Reviewed, UniProtKB/Swiss-Prot Q9LEL5 (4OMT_COPJA)

Names and origin

Protein names	Recommended name:     3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase     EC=2.1.1.116 Alternative name(s):     S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase       Short name=4'-OMT
Organism	Coptis japonica (Japanese goldthread)
Taxonomic identifier	3442 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › Ranunculales › Ranunculaceae › Coptis

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transfer of the methyl group to the 4'-hydroxyl group of 3'-hydroxy-N-methylcoclaurine to form reticuline.
Catalytic activity	S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine = S-adenosyl-L-homocysteine + (S)-reticuline.
Pathway	Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-reticuline from (S)-norcoclaurine: step 4/4.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the methyltransferase superfamily. Type 2 family. COMT subfamily.

Ontologies

Keywords
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Molecular function	3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase activity Inferred from electronic annotation. Source: EC O-methyltransferase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase		PRO_0000204430
Sites
	Active site	257	1	Proton acceptor By similarity
	Binding site	196	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	219	1	S-adenosyl-L-methionine By similarity
	Binding site	239	1	S-adenosyl-L-methionine By similarity
	Binding site	240	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	253	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LEL5-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 547835EBCDEF9182	FASTA	350	38,776
	10 20 30 40 50 60 MAFHGKDDVL DIKAQAHVWK IIYGFADSLV LRCAVELGIV DIIDNNNQPM ALADLASKLP 70 80 90 100 110 120 VSDVNCDNLY RILRYLVKME ILRVEKSDDG QKKYALEPIA TLLSRNAKRS MVPMILGMTQ 130 140 150 160 170 180 KDFMTPWHSM KDGLSDNGTA FEKAMGMTIW EYLEGHPDQS QLFNEGMAGE TRLLTSSLIS 190 200 210 220 230 240 GSRDMFQGID SLVDVGGGNG TTVKAISDAF PHIKCTLFDL PHVIANSYDL PNIERIGGDM 250 260 270 280 290 300 FKSVPSAQAI ILKLILHDWN DEDSIKILKQ CRNAVPKDGG KVIIVDVALD EESDHELSST 310 320 330 340 350 RLILDIDMLV NTGGKERTKE VWEKIVKSAG FSGCKIRHIA AIQSVIEVFP

References

[1]

"Molecular characterization of the S-adenosyl-L-methionine: 3'-hydroxy-N-methylcoclaurine 4'O-methyltransferase involved in isoquinoline alkaloid biosynthesis in Coptis japonica." Morishige T., Tsujita T., Yamada Y., Sato F. J. Biol. Chem. 275:23398-23405(2000) [PubMed: 10811648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D29812 mRNA. Translation: BAB08005.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.1.1.116. 9740.
Family and domain databases
InterPro	IPR016461. O-MeTrfase_COMT_euk. IPR001077. O_MeTrfase_2. IPR012967. Plant_MeTrfase_dimerisation. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF08100. Dimerisation. 1 hit. PF00891. Methyltransf_2. 1 hit. [Graphical view]
PIRSF	PIRSF005739. O-mtase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

4OMT_COPJA

Accession

Primary (citable) accession number: Q9LEL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	October 1, 2000
Last modified:	November 24, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)