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Protein

(RS)-norcoclaurine 6-O-methyltransferase

Gene
N/A
Organism
Coptis japonica (Japanese goldthread)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the S-methyl group of S-adenosyl-L-methionine (AdoMet) to the 6-hydroxyl group of norcoclaurine to form coclaurine.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + (RS)-norcoclaurine = S-adenosyl-L-homocysteine + (RS)-coclaurine.1 Publication

Pathwayi: (S)-reticuline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (S)-reticuline from (S)-norcoclaurine.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. (RS)-norcoclaurine 6-O-methyltransferase
  2. no protein annotated in this organism
  3. Probable (S)-N-methylcoclaurine 3'-hydroxylase isozyme 2 (CYP80B2)
  4. 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase
This subpathway is part of the pathway (S)-reticuline biosynthesis, which is itself part of Alkaloid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-reticuline from (S)-norcoclaurine, the pathway (S)-reticuline biosynthesis and in Alkaloid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei215 – 2151S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei235 – 2351S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei236 – 2361S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei249 – 2491S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei253 – 2531Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.128. 1610.
SABIO-RKQ9LEL6.
UniPathwayiUPA00306; UER00441.

Names & Taxonomyi

Protein namesi
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
OrganismiCoptis japonica (Japanese goldthread)
Taxonomic identifieri3442 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesRanunculaceaeCoptidoideaeCoptis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347(RS)-norcoclaurine 6-O-methyltransferasePRO_0000204433Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliQ9LEL6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.PROSITE-ProRule annotation

Phylogenomic databases

KOiK13383.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LEL6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVKKDNLSS QAKLWNFIYG FAESLVLKCA VQLDLANIIH NSGTSMTLSE
60 70 80 90 100
LSSRLPSQPV NEDALYRVMR YLVHMKLFTK ASIDGELRYG LAPPAKYLVK
110 120 130 140 150
GWDKCMVGSI LAITDKDFMA PWHYLKDGLS GESGTAFEKA LGTNIWGYMA
160 170 180 190 200
EHPEKNQLFN EAMANDSRLI MSALVKECGN IFNGITTLVD VGGGTGTAVR
210 220 230 240 250
NIANAFPHIK CTVYDLPHVI ADSPGYSEVH CVAGDMFKFI PKADAIMMKC
260 270 280 290 300
ILHDWDDKEC IEILKRCKEA VPVKGGKVII VDIVLNVQSE HPYTKMRLTL
310 320 330 340
DLDMMLNTGG KERTEEEWKK LIHDAGYKGH KITQITAVQS VIEAYPY
Length:347
Mass (Da):38,700
Last modified:October 1, 2000 - v1
Checksum:i2BC34B3FBE67167C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29811 mRNA. Translation: BAB08004.1.

Genome annotation databases

KEGGiag:BAB08004.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29811 mRNA. Translation: BAB08004.1.

3D structure databases

ProteinModelPortaliQ9LEL6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAB08004.

Phylogenomic databases

KOiK13383.

Enzyme and pathway databases

UniPathwayiUPA00306; UER00441.
BRENDAi2.1.1.128. 1610.
SABIO-RKQ9LEL6.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 88-103, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry namei6OMT_COPJA
AccessioniPrimary (citable) accession number: Q9LEL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: October 1, 2000
Last modified: December 9, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.