Reviewed, UniProtKB/Swiss-Prot Q9LEL6 (6OMT_COPJA)

Names and origin

Protein names	Recommended name:     (RS)-norcoclaurine 6-O-methyltransferase     EC=2.1.1.128 Alternative name(s):     S-adenosyl-L-methionine:norcoclaurine 6-O-methyltransferase       Short name=6-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	347 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 S-methyl group of S-adenosyl-L-methionine (AdoMet) to the 6-hydroxyl group of norcoclaurine to form coclaurine.
Catalytic activity	S-adenosyl-L-methionine + (RS)-norcoclaurine = S-adenosyl-L-homocysteine + (RS)-coclaurine.
Pathway	Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-reticuline from (S)-norcoclaurine: step 1/4.
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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	(RS)-norcoclaurine 6-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 – 347	347	(RS)-norcoclaurine 6-O-methyltransferase		PRO_0000204433
Sites
	Active site	253	1	Proton acceptor By similarity
	Binding site	192	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	215	1	S-adenosyl-L-methionine By similarity
	Binding site	235	1	S-adenosyl-L-methionine By similarity
	Binding site	236	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	249	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LEL6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2BC34B3FBE67167C	FASTA	347	38,700
	10 20 30 40 50 60 MEVKKDNLSS QAKLWNFIYG FAESLVLKCA VQLDLANIIH NSGTSMTLSE LSSRLPSQPV 70 80 90 100 110 120 NEDALYRVMR YLVHMKLFTK ASIDGELRYG LAPPAKYLVK GWDKCMVGSI LAITDKDFMA 130 140 150 160 170 180 PWHYLKDGLS GESGTAFEKA LGTNIWGYMA EHPEKNQLFN EAMANDSRLI MSALVKECGN 190 200 210 220 230 240 IFNGITTLVD VGGGTGTAVR NIANAFPHIK CTVYDLPHVI ADSPGYSEVH CVAGDMFKFI 250 260 270 280 290 300 PKADAIMMKC ILHDWDDKEC IEILKRCKEA VPVKGGKVII VDIVLNVQSE HPYTKMRLTL 310 320 330 340 DLDMMLNTGG KERTEEEWKK LIHDAGYKGH KITQITAVQS VIEAYPY

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].
[2]	"Purification and characterization of S-adenosyl-L-methionine: norcoclaurine 6-O-methyltransferase from cultured Coptis japonica cells." Sato F., Tsujita T., Katagiri Y., Yoshida S., Yamada Y. Eur. J. Biochem. 225:125-131(1994) [PubMed: 7925429] [Abstract] Cited for: PROTEIN SEQUENCE OF 88-103, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D29811 mRNA. Translation: BAB08004.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.1.1.128. 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

6OMT_COPJA

Accession

Primary (citable) accession number: Q9LEL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	October 1, 2000
Last modified:	November 24, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)