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Q9LUT2

- METK4_ARATH

UniProt

Q9LUT2 - METK4_ARATH

Protein

S-adenosylmethionine synthase 4

Gene

METK4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.By similarity
    Binds 1 potassium ion per subunit.By similarity

    Pathwayi

    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

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methionine adenosyltransferase activity Source: TAIR

    GO - Biological processi

    1. lignin biosynthetic process Source: TAIR
    2. methionine metabolic process Source: TAIR
    3. one-carbon metabolic process Source: UniProtKB-KW
    4. response to cold Source: TAIR
    5. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciARA:AT3G17390-MONOMER.
    UniPathwayiUPA00315; UER00080.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine synthase 4 (EC:2.5.1.6)
    Short name:
    AdoMet synthase 4
    Alternative name(s):
    Methionine adenosyltransferase 4
    Short name:
    MAT 4
    Gene namesi
    Name:METK4
    Synonyms:MTO3, SAMS3
    Ordered Locus Names:At3g17390
    ORF Names:MGD8.23
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G17390.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cell wall Source: TAIR
    2. cytoplasm Source: UniProtKB-SubCell
    3. membrane Source: TAIR
    4. nucleolus Source: TAIR
    5. plasma membrane Source: TAIR
    6. plasmodesma Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393S-adenosylmethionine synthase 4PRO_0000363004Add
    BLAST

    Post-translational modificationi

    Ubiquitinated.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PRIDEiQ9LUT2.

    Expressioni

    Tissue specificityi

    Trichomes.1 Publication

    Inductioni

    Induced by cold.1 Publication

    Gene expression databases

    ArrayExpressiQ9LUT2.
    GenevestigatoriQ9LUT2.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi6336. 3 interactions.
    IntActiQ9LUT2. 2 interactions.
    MINTiMINT-8064905.
    STRINGi3702.AT3G17390.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LUT2.
    SMRiQ9LUT2. Positions 3-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000245710.
    InParanoidiQ9LUT2.
    KOiK00789.
    OMAiDETEESM.
    PhylomeDBiQ9LUT2.

    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.

    Q9LUT2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESFLFTSES VNEGHPDKLC DQISDAILDA CLEQDPESKV ACETCTKTNM    50
    VMVFGEITTK ANVDYEQIVR KTCREIGFVS ADVGLDADNC KVLVNIEQQS 100
    PDIAQGVHGH LTKKPEEVGA GDQGHMFGYA TDETPELMPL THVLATKLGA 150
    KLTEVRKNGT CPWLRPDGKT QVTIEYINES GAMVPVRVHT VLISTQHDET 200
    VTNDEIAADL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI GGPHGDAGLT 250
    GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVASGLAR 300
    RVIVQVSYAI GVPEPLSVFV DSYGTGKIPD KEILEIVKES FDFRPGMISI 350
    NLDLKRGGNG RFLKTAAYGH FGRDDADFTW EVVKPLKSNK VQA 393
    Length:393
    Mass (Da):42,796
    Last modified:October 1, 2000 - v1
    Checksum:i70034EC2B5E81867
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti198 – 1981D → G in BAF01944. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_188365.1. NM_112618.3.
    UniGeneiAt.5781.
    At.70071.

    Genome annotation databases

    EnsemblPlantsiAT3G17390.1; AT3G17390.1; AT3G17390.
    GeneIDi821003.
    KEGGiath:AT3G17390.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_188365.1. NM_112618.3.
    UniGenei At.5781.
    At.70071.

    3D structure databases

    ProteinModelPortali Q9LUT2.
    SMRi Q9LUT2. Positions 3-387.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 6336. 3 interactions.
    IntActi Q9LUT2. 2 interactions.
    MINTi MINT-8064905.
    STRINGi 3702.AT3G17390.1-P.

    Proteomic databases

    PRIDEi Q9LUT2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G17390.1 ; AT3G17390.1 ; AT3G17390 .
    GeneIDi 821003.
    KEGGi ath:AT3G17390.

    Organism-specific databases

    TAIRi AT3G17390.

    Phylogenomic databases

    HOGENOMi HOG000245710.
    InParanoidi Q9LUT2.
    KOi K00789.
    OMAi DETEESM.
    PhylomeDBi Q9LUT2.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    BioCyci ARA:AT3G17390-MONOMER.

    Gene expression databases

    ArrayExpressi Q9LUT2.
    Genevestigatori Q9LUT2.

    Family and domain databases

    HAMAPi MF_00086. S_AdoMet_synth1.
    InterProi IPR022631. 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 ]
    PANTHERi PTHR11964. PTHR11964. 1 hit.
    Pfami PF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000497. MAT. 1 hit.
    SUPFAMi SSF55973. SSF55973. 3 hits.
    TIGRFAMsi TIGR01034. metK. 1 hit.
    PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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].

    Entry informationi

    Entry nameiMETK4_ARATH
    AccessioniPrimary (citable) accession number: Q9LUT2
    Secondary accession number(s): Q0WLR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 105 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

    External Data

    Dasty 3