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Protein

Flavone 3'-O-methyltransferase 1

Gene

COMT

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Methylates OH residues of flavonoid compounds. Can methylate eriodictyol, luteolin, quercetin and taxifolin (PubMed:16412485). Methylates caffeate to produce ferrulate (PubMed:21210840, Ref. 16). Catalyzes the methylation of monolignols, the lignin precursors. Functions cooperatively with CAD2 in the culm internodes for the biosynthesis of monolignols. May be involved in lignin biosynthesis in leaves and roots (PubMed:21912859). Involved in syringyl lignin biosynthesis. Can function as 5-hydroxyconiferaldehyde O-methyltransferase in the biosynthetic pathway to syringyl lignin (Ref. 16). Involved in melatonin biosynthesis. Can function as acetylserotonin O-methyltransferase. Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine) (PubMed:26276868).5 Publications

Caution

Was initially thought to constitute the naringenin 7-O-methyltransferase (NOMT), a methyltransferase involved in the biosynthesis of the sakuranetin, an inducible defense mechanism of O.sativa against pathogen attack (PubMed:10814825). However, it was later shown that it is not the case (PubMed:22493492).2 Publications

Catalytic activityi

S-adenosyl-L-methionine + 3'-hydroxyflavone = S-adenosyl-L-homocysteine + 3'-methoxyflavone.1 Publication
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin.1 Publication
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate.1 Publication

Enzyme regulationi

Acetylserotonin O-methyltransferase activity is inhibited by quercetin and caffeate.1 Publication

Kineticsi

Measured at pH 7.5 and 37 degrees Celsius for all experiments.1 Publication
  1. KM=61.8 µM for quercetin1 Publication
  2. KM=61.9 µM for luteolin1 Publication
  3. KM=62 µM for eriodictyol1 Publication
  4. KM=201.8 µM for caffeate (at pH 7.5 and 30 degrees Celsius)1 Publication
  5. KM=22.2 µM for 5-hydroxyferulate (at pH 7.5 and 30 degrees Celsius)1 Publication
  6. KM=65.8 µM for caffealdehyde (at pH 7.5 and 30 degrees Celsius)1 Publication
  7. KM=26.4 µM for 5-hydroxyconiferaldehyde (at pH 7.5 and 30 degrees Celsius)1 Publication
  8. KM=50 µM for caffeyl alcohol (at pH 7.5 and 30 degrees Celsius)1 Publication
  9. KM=132.3 µM for 5-hydroxyconiferyl alcohol (at pH 7.5 and 30 degrees Celsius)1 Publication
  10. KM=243 µM for N-acetylserotonin (at pH 7.8 and 37 degrees Celsius)1 Publication
  1. Vmax=1250 pmol/sec/mg enzyme with quercetin as substrate1 Publication
  2. Vmax=833 pmol/sec/mg enzyme with luteolin as substrate1 Publication
  3. Vmax=625 pmol/sec/mg enzyme with eriodictyol as substrate1 Publication
  4. Vmax=2.4 nmol/min/mg enzyme with N-acetylserotonin as substrate (at pH 7.8 and 37 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius for acetylserotonin O-methyltransferase activity.1 Publication

Pathwayi: quercetin degradation

This protein is involved in the pathway quercetin degradation, which is part of Flavonoid metabolism.
View all proteins of this organism that are known to be involved in the pathway quercetin degradation and in Flavonoid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei135SubstrateBy similarity1
Binding sitei212S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei235S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei255S-adenosyl-L-methionineBy similarity1
Binding sitei256S-adenosyl-L-methionine; via amide nitrogenBy similarity1
Binding sitei270S-adenosyl-L-methionineBy similarity1
Active sitei274Proton acceptorPROSITE-ProRule annotation1
Active sitei302By similarity1
Active sitei334By similarity1

GO - Molecular functioni

  • acetylserotonin O-methyltransferase activity Source: UniProtKB
  • caffeate O-methyltransferase activity Source: CACAO
  • luteolin O-methyltransferase activity Source: UniProtKB
  • protein dimerization activity Source: InterPro
  • quercetin 3'-O-methyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  • flavonol biosynthetic process Source: UniProtKB
  • lignin biosynthetic process Source: UniProtKB
  • melatonin biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processMelatonin biosynthesis
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-20526
ReactomeiR-OSA-209931 Serotonin and melatonin biosynthesis
UniPathwayiUPA00724

Names & Taxonomyi

Protein namesi
Recommended name:
Flavone 3'-O-methyltransferase 1Curated (EC:2.1.1.421 Publication)
Short name:
OsOMT1Curated
Alternative name(s):
Acetylserotonin O-methyltransferase COMTCurated (EC:2.1.1.41 Publication)
Caffeate O-methyltransferase 1Curated (EC:2.1.1.681 Publication)
Short name:
OsCOMT11 Publication
OsCOMT1 Publication
Quercetin 3'-O-methyltransferase 1Curated
Gene namesi
Name:COMTCurated
Synonyms:ROMT-91 Publication
Ordered Locus Names:Os08g0157500, LOC_Os08g06100
ORF Names:OsJ_26105, P0438H08.29
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryzaOryza sativa
Proteomesi
  • UP000059680 Componenti: Chromosome 8

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00002489691 – 21 Publication2
ChainiPRO_00002336993 – 368Flavone 3'-O-methyltransferase 1Add BLAST366

Proteomic databases

PaxDbiQ6ZD89
PRIDEiQ6ZD89

Expressioni

Tissue specificityi

Expressed in roots and stems, and at lower levels in leaves.1 Publication

Inductioni

By probenazole (at protein level) (PubMed:17950386). Induced by UV-C (PubMed:24035516).2 Publications

Gene expression databases

ExpressionAtlasiQ6ZD89 differential
GenevisibleiQ6ZD89 OS

Interactioni

Subunit structurei

Monomer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi39947.LOC_Os08g06100.1

Structurei

3D structure databases

ProteinModelPortaliQ6ZD89
SMRiQ6ZD89
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3178 Eukaryota
ENOG410XS7T LUCA
HOGENOMiHOG000238276
InParanoidiQ6ZD89
KOiK22439
OMAiYLTANED
OrthoDBiEOG09360E51

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016461 O-MeTrfase_COMT
IPR001077 O_MeTrfase_2
IPR012967 Plant_MeTrfase_dimerisation
IPR029063 SAM-dependent_MTases
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF08100 Dimerisation, 1 hit
PF00891 Methyltransf_2, 1 hit
PIRSFiPIRSF005739 O-mtase, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51683 SAM_OMT_II, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6ZD89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTAADMAA AADEEACMYA LQLASSSILP MTLKNAIELG LLETLQSAAV
60 70 80 90 100
AGGGGKAALL TPAEVADKLP SKANPAAADM VDRMLRLLAS YNVVRCEMEE
110 120 130 140 150
GADGKLSRRY AAAPVCKWLT PNEDGVSMAA LALMNQDKVL MESWYYLKDA
160 170 180 190 200
VLDGGIPFNK AYGMTAFEYH GTDARFNRVF NEGMKNHSVI ITKKLLDLYT
210 220 230 240 250
GFDAASTVVD VGGGVGATVA AVVSRHPHIR GINYDLPHVI SEAPPFPGVE
260 270 280 290 300
HVGGDMFASV PRGGDAILMK WILHDWSDEH CARLLKNCYD ALPEHGKVVV
310 320 330 340 350
VECVLPESSD ATAREQGVFH VDMIMLAHNP GGKERYEREF RELARAAGFT
360
GFKATYIYAN AWAIEFTK
Length:368
Mass (Da):39,749
Last modified:July 5, 2004 - v1
Checksum:i2491B4FA7447558E
GO

Sequence cautioni

The sequence EAZ41571 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54G → R in EAZ41571 (PubMed:15685292).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ288259 mRNA Translation: ABB90678.1
DQ530257 mRNA Translation: ABF72191.1
AP004460 Genomic DNA Translation: BAC99512.1
AP008214 Genomic DNA Translation: BAF22945.1
AP014964 Genomic DNA Translation: BAT03903.1
CM000145 Genomic DNA Translation: EAZ41571.1 Different initiation.
AK064768 mRNA Translation: BAG89194.1
AB122056 mRNA Translation: BAD14923.1
RefSeqiXP_015650053.1, XM_015794567.1
UniGeneiOs.11202

Genome annotation databases

EnsemblPlantsiOs08t0157500-01; Os08t0157500-01; Os08g0157500
GeneIDi4344702
GrameneiOs08t0157500-01; Os08t0157500-01; Os08g0157500
KEGGiosa:4344702

Similar proteinsi

Entry informationi

Entry nameiOMT1_ORYSJ
AccessioniPrimary (citable) accession number: Q6ZD89
Secondary accession number(s): A0A0P0XBV5
, A3BPT2, Q19BJ6, Q75W57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2004
Last modified: June 20, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  3. SIMILARITY comments
    Index of protein domains and families

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