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Protein

S-adenosylmethionine synthase 3

Gene

METK3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme (By similarity). Involved in the biosynthesis of lignin.By similarity2 Publications

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit.By similarity

Enzyme regulationi

Repressed by 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) and N-ethylmaleimide (NEM).1 Publication

Pathwayi: S-adenosyl-L-methionine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase 4 (METK4), S-adenosylmethionine synthase 2 (SAM2), S-adenosylmethionine synthase 3 (METK3), S-adenosylmethionine synthase 1 (SAM1)
This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171MagnesiumBy similarity
Metal bindingi43 – 431PotassiumBy similarity
Binding sitei147 – 1471ATPSequence analysis
Metal bindingi271 – 2711PotassiumBy similarity
Metal bindingi279 – 2791MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi119 – 1246ATPSequence analysis
Nucleotide bindingi267 – 2748ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • copper ion binding Source: TAIR
  • methionine adenosyltransferase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lignin biosynthesis, One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciARA:AT2G36880-MONOMER.
ARA:GQT-2657-MONOMER.
ReactomeiR-ATH-156581. Methylation.
R-ATH-1614635. Sulfur amino acid metabolism.
R-ATH-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase 3 (EC:2.5.1.6)
Short name:
AdoMet synthase 3
Alternative name(s):
Methionine adenosyltransferase 3
Short name:
MAT 3
Gene namesi
Name:METK3
Ordered Locus Names:At2g36880
ORF Names:T1J8.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G36880.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201A → T in mto3-1; accumulation of free Met, increased resistance to Ethionine, and reduced lignin formation. 1 Publication
Mutagenesisi167 – 1671D → N in mto3-2; accumulation of free Met and increased resistance to Ethionine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390S-adenosylmethionine synthase 3PRO_0000363003Add
BLAST

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9SJL8.
PRIDEiQ9SJL8.

Expressioni

Tissue specificityi

Pollen (at protein level).2 Publications

Gene expression databases

GenevisibleiQ9SJL8. AT.

Interactioni

Subunit structurei

Homotetramer (By similarity). Interacts with GRF3.By similarity1 Publication

Protein-protein interaction databases

BioGridi3604. 4 interactions.
MINTiMINT-8064409.
STRINGi3702.AT2G36880.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SJL8.
SMRiQ9SJL8. Positions 3-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOGENOMiHOG000245710.
InParanoidiQ9SJL8.
KOiK00789.
OMAiCETQIAY.
PhylomeDBiQ9SJL8.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SJL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METFLFTSES VNEGHPDKLC DQISDAILDA CLEQDPESKV ACETCTKTNM
60 70 80 90 100
VMVFGEITTA AKVDYEKIVR STCREIGFIS ADVGLDADKC NVLVNIEQQS
110 120 130 140 150
PDIAQGVHGH LTKKPEDIGA GDQGHMFGYA TDETPELMPL THVLATKLGA
160 170 180 190 200
KLTEVRKNKT CPWLRPDGKT QVTVEYKNDG GAMIPIRVHT VLISTQHDET
210 220 230 240 250
VTNDEIAADL KEHVIKPVIP AKYLDDNTIF HLNPSGRFVI GGPHGDAGLT
260 270 280 290 300
GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVAAGLAR
310 320 330 340 350
RCIVQVSYAI GVPEPLSVFV DTYKTGTIPD KDILVLIKEA FDFRPGMMAI
360 370 380 390
NLDLKRGGNF RFQKTAAYGH FGRDDPDFTW EVVKPLKPKA
Length:390
Mass (Da):42,497
Last modified:May 1, 2000 - v1
Checksum:i5C8BB48838606184
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006922 Genomic DNA. Translation: AAD31573.1.
CP002685 Genomic DNA. Translation: AEC09310.1.
CP002685 Genomic DNA. Translation: AEC09311.1.
AF367310 mRNA. Translation: AAK32897.1.
AY133601 mRNA. Translation: AAM91431.1.
PIRiG84785.
RefSeqiNP_001118458.1. NM_001124986.1.
NP_181225.1. NM_129243.3.
UniGeneiAt.23534.

Genome annotation databases

EnsemblPlantsiAT2G36880.1; AT2G36880.1; AT2G36880.
AT2G36880.2; AT2G36880.2; AT2G36880.
GeneIDi818260.
GrameneiAT2G36880.1; AT2G36880.1; AT2G36880.
AT2G36880.2; AT2G36880.2; AT2G36880.
KEGGiath:AT2G36880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006922 Genomic DNA. Translation: AAD31573.1.
CP002685 Genomic DNA. Translation: AEC09310.1.
CP002685 Genomic DNA. Translation: AEC09311.1.
AF367310 mRNA. Translation: AAK32897.1.
AY133601 mRNA. Translation: AAM91431.1.
PIRiG84785.
RefSeqiNP_001118458.1. NM_001124986.1.
NP_181225.1. NM_129243.3.
UniGeneiAt.23534.

3D structure databases

ProteinModelPortaliQ9SJL8.
SMRiQ9SJL8. Positions 3-387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3604. 4 interactions.
MINTiMINT-8064409.
STRINGi3702.AT2G36880.1.

Proteomic databases

PaxDbiQ9SJL8.
PRIDEiQ9SJL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G36880.1; AT2G36880.1; AT2G36880.
AT2G36880.2; AT2G36880.2; AT2G36880.
GeneIDi818260.
GrameneiAT2G36880.1; AT2G36880.1; AT2G36880.
AT2G36880.2; AT2G36880.2; AT2G36880.
KEGGiath:AT2G36880.

Organism-specific databases

TAIRiAT2G36880.

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOGENOMiHOG000245710.
InParanoidiQ9SJL8.
KOiK00789.
OMAiCETQIAY.
PhylomeDBiQ9SJL8.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciARA:AT2G36880-MONOMER.
ARA:GQT-2657-MONOMER.
ReactomeiR-ATH-156581. Methylation.
R-ATH-1614635. Sulfur amino acid metabolism.
R-ATH-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Miscellaneous databases

PROiQ9SJL8.

Gene expression databases

GenevisibleiQ9SJL8. AT.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "A single-nucleotide mutation in a gene encoding S-adenosylmethionine synthetase is associated with methionine over-accumulation phenotype in Arabidopsis thaliana."
    Goto D.B., Ogi M., Kijima F., Kumagai T., van Werven F., Onouchi H., Naito S.
    Genes Genet. Syst. 77:89-95(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-167.
  5. "High free-methionine and decreased lignin content result from a mutation in the Arabidopsis S-adenosyl-L-methionine synthetase 3 gene."
    Shen B., Li C., Tarczynski M.C.
    Plant J. 29:371-380(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-120.
  6. "A reference map of the Arabidopsis thaliana mature pollen proteome."
    Noir S., Braeutigam A., Colby T., Schmidt J., Panstruga R.
    Biochem. Biophys. Res. Commun. 337:1257-1266(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Proteome mapping of mature pollen of Arabidopsis thaliana."
    Holmes-Davis R., Tanaka C.K., Vensel W.H., Hurkman W.J., McCormick S.
    Proteomics 5:4864-4884(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation."
    Lindermayr C., Saalbach G., Bahnweg G., Durner J.
    J. Biol. Chem. 281:4285-4291(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
    Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
    Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
  10. "14-3-3 proteins fine-tune plant nutrient metabolism."
    Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.
    FEBS Lett. 585:143-147(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRF3.

Entry informationi

Entry nameiMETK3_ARATH
AccessioniPrimary (citable) accession number: Q9SJL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 116 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.