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Q9LUT2 (METK4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine synthase 4

Short name=AdoMet synthase 4
EC=2.5.1.6
Alternative name(s):
Methionine adenosyltransferase 4
Short name=MAT 4
Gene names
Name:METK4
Synonyms:MTO3, SAMS3
Ordered Locus Names:At3g17390
ORF Names:MGD8.23
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00086

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP-Rule MF_00086

Cofactor

Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.

Binds 1 potassium ion per subunit By similarity. HAMAP-Rule MF_00086

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP-Rule MF_00086

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00086

Subcellular location

Cytoplasm Ref.6.

Tissue specificity

Trichomes. Ref.7

Induction

Induced by cold. Ref.8

Post-translational modification

Ubiquitinated. HAMAP-Rule MF_00086

Sequence similarities

Belongs to the AdoMet synthase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Cobalt
Magnesium
Metal-binding
Nucleotide-binding
Potassium
   Molecular functionTransferase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processS-adenosylmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lignin biosynthetic process

Inferred from mutant phenotype PubMed 11844113. Source: TAIR

methionine metabolic process

Inferred from mutant phenotype PubMed 11844113. Source: TAIR

one-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to cold

Inferred from expression pattern Ref.8. Source: TAIR

   Cellular_componentcell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

nucleolus

Inferred from direct assay PubMed 15496452. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17317660PubMed 17644812. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine adenosyltransferase activity

Inferred from sequence or structural similarity PubMed 11844113. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393S-adenosylmethionine synthase 4 HAMAP-Rule MF_00086
PRO_0000363004

Regions

Nucleotide binding119 – 1246ATP Potential
Nucleotide binding267 – 2748ATP Potential

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2711Potassium By similarity
Metal binding2791Magnesium By similarity
Binding site1471ATP Potential

Experimental info

Sequence conflict1981D → G in BAF01944. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9LUT2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 70034EC2B5E81867

FASTA39342,796
        10         20         30         40         50         60 
MESFLFTSES VNEGHPDKLC DQISDAILDA CLEQDPESKV ACETCTKTNM VMVFGEITTK 

        70         80         90        100        110        120 
ANVDYEQIVR KTCREIGFVS ADVGLDADNC KVLVNIEQQS PDIAQGVHGH LTKKPEEVGA 

       130        140        150        160        170        180 
GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNGT CPWLRPDGKT QVTIEYINES 

       190        200        210        220        230        240 
GAMVPVRVHT VLISTQHDET VTNDEIAADL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI 

       250        260        270        280        290        300 
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVASGLAR 

       310        320        330        340        350        360 
RVIVQVSYAI GVPEPLSVFV DSYGTGKIPD KEILEIVKES FDFRPGMISI NLDLKRGGNG 

       370        380        390 
RFLKTAAYGH FGRDDADFTW EVVKPLKSNK VQA 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"A proteomic study of the Arabidopsis nuclear matrix."
Calikowski T.T., Meulia T., Meier I.
J. Cell. Biochem. 90:361-378(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Cell-specific protein profiling in Arabidopsis thaliana trichomes: identification of trichome-located proteins involved in sulfur metabolism and detoxification."
Wienkoop S., Zoeller D., Ebert B., Simon-Rosin U., Fisahn J., Glinski M., Weckwerth W.
Phytochemistry 65:1641-1649(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology."
Amme S., Matros A., Schlesier B., Mock H.-P.
J. Exp. Bot. 57:1537-1546(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY COLD, IDENTIFICATION BY MASS SPECTROMETRY.
[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB022216 Genomic DNA. Translation: BAB02743.1.
CP002686 Genomic DNA. Translation: AEE75948.1.
AY037214 mRNA. Translation: AAK59799.1.
AY120708 mRNA. Translation: AAM53266.1.
BT000712 mRNA. Translation: AAN31855.1.
BT002665 mRNA. Translation: AAO11581.1.
AK230129 mRNA. Translation: BAF01944.1.
AY087184 mRNA. Translation: AAM64740.1.
RefSeqNP_188365.1. NM_112618.3.
UniGeneAt.5781.
At.70071.

3D structure databases

ProteinModelPortalQ9LUT2.
SMRQ9LUT2. Positions 3-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid6336. 2 interactions.
IntActQ9LUT2. 1 interaction.
MINTMINT-8064905.
STRING3702.AT3G17390.1-P.

Proteomic databases

PRIDEQ9LUT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G17390.1; AT3G17390.1; AT3G17390.
GeneID821003.
KEGGath:AT3G17390.

Organism-specific databases

TAIRAT3G17390.

Phylogenomic databases

HOGENOMHOG000245710.
InParanoidQ9LUT2.
KOK00789.
OMAACDETAN.
PhylomeDBQ9LUT2.
ProtClustDBPLN02243.

Enzyme and pathway databases

BioCycARA:AT3G17390-MONOMER.
UniPathwayUPA00315; UER00080.

Gene expression databases

ArrayExpressQ9LUT2.
GenevestigatorQ9LUT2.

Family and domain databases

HAMAPMF_00086. S_AdoMet_synth1.
InterProIPR022631. 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]
PANTHERPTHR11964. PTHR11964. 1 hit.
PfamPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000497. MAT. 1 hit.
SUPFAMSSF55973. SSF55973. 3 hits.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK4_ARATH
AccessionPrimary (citable) accession number: Q9LUT2
Secondary accession number(s): Q0WLR3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names