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Protein

Methylthioalkylmalate synthase 1, chloroplastic

Gene

MAM1

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

Functioni

Determines the side chain length of aliphatic glucosinolate structures. Catalyzes exclusively the condensation reactions of both the first and second methionine carbon chain elongation.2 Publications

Cofactori

Mn2+Note: Manganese or any other divalent metal ion, except copper or zinc.

Enzyme regulationi

1 mM DTT required for activity. Activated by ATP and inhibited by iodoacetamide.1 Publication

Kineticsi

  1. KM=3.0 mM for 4-methylthio-2-oxobutanoic acid1 Publication
  2. KM=11.2 mM for 2-oxohexanoic acid1 Publication
  3. KM=0.64 mM for 5-methylthio-2-oxopentanoic acid1 Publication
  4. KM=7.5 mM for 2-oxoheptanoic acid1 Publication
  5. KM=245 µM for acetyl-CoA1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 32 degrees Celsius.1 Publication

    GO - Molecular functioni

    • 2-(2'-methylthio)ethylmalate synthase activity Source: TAIR

    GO - Biological processi

    • carboxylic acid metabolic process Source: InterPro
    • glucosinolate biosynthetic process Source: TAIR
    • response to insect Source: TAIR
    • response to water deprivation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:AT5G23010-MONOMER.
    BRENDAi2.3.3.13. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylthioalkylmalate synthase 1, chloroplastic (EC:2.3.3.-)
    Alternative name(s):
    2-isopropylmalate synthase 3
    Gene namesi
    Name:MAM1
    Synonyms:IMS3, IPMS_AT2, MAM-L, MAML
    Ordered Locus Names:At5g23010
    ORF Names:T20O7.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G23010.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi102 – 1021S → F in gsm1-1; loss of conversion of C3 to C4 glucosinolates. 1 Publication
    Mutagenesisi290 – 2901A → T in gsm1-2; loss of conversion of C3 to C4 glucosinolates. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4949ChloroplastSequence AnalysisAdd
    BLAST
    Chaini50 – 506457Methylthioalkylmalate synthase 1, chloroplasticPRO_0000315841Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9FG67.
    PRIDEiQ9FG67.

    Expressioni

    Tissue specificityi

    Highly expressed in leaves, flowers, roots and siliques. Not detected in flowers in PubMed:12432038.2 Publications

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT5G23010.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FG67.
    SMRiQ9FG67. Positions 83-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal part of the protein controls substrate specificity.

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0119.
    HOGENOMiHOG000046861.
    InParanoidiQ9FG67.
    KOiK15741.
    OMAiLQININT.
    PhylomeDBiQ9FG67.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR002034. AIPM/Hcit_synth_CS.
    IPR013785. Aldolase_TIM.
    IPR000891. PYR_CT.
    [Graphical view]
    PfamiPF00682. HMGL-like. 1 hit.
    [Graphical view]
    PROSITEiPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
    PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
    PS50991. PYR_CT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9FG67-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSLLTSSV MIPTTGSTVV GRSVLPFQSS LHSLRLTHSY KNPALFISCC
    60 70 80 90 100
    SSVSKNAATS STDLKPVVER WPEYIPNKLP DGNYVRVFDT TLRDGEQSPG
    110 120 130 140 150
    GSLTPPQKLE IARQLAKLRV DIMEVGFPGS SEEELETIKT IAKTVGNEVD
    160 170 180 190 200
    EETGYVPVIC AIARCKHRDI EATWEALKYA KRPRILVFTS TSDIHMKYKL
    210 220 230 240 250
    KKTQEEVIEM AVSSIRFAKS LGFNDIQFGC EDGGRSDKDF LCKILGEAIK
    260 270 280 290 300
    AGVTVVTIGD TVGINMPHEY GELVTYLKAN TPGIDDVVVA VHCHNDLGLA
    310 320 330 340 350
    TANSIAGIRA GARQVEVTIN GIGERSGNAS LEEVVMALKC RGAYVINGVY
    360 370 380 390 400
    TKIDTRQIMA TSKMVQEYTG LYVQAHKPIV GANCFVHESG IHQDGILKNR
    410 420 430 440 450
    STYEILSPED IGIVKSQNSG LVLGKLSGRH AVKDRLKELG YELDDEKLNA
    460 470 480 490 500
    VFSLFRDLTK NKKRITDADL KALVTSSDEI SLEKLNGANG LKSNGYIPVP

    QVSSNV
    Length:506
    Mass (Da):55,125
    Last modified:March 1, 2001 - v1
    Checksum:iA3F4CC32508CAE49
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101V → G in strain: cv. Sorbo.
    Natural varianti42 – 421N → K in strain: cv. Ema-1 and cv. Pla-0.
    Natural varianti44 – 441A → T in strain: cv. Sorbo.
    Natural varianti505 – 5051N → T in strain: cv. Sorbo.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ131517 Genomic DNA. Translation: CAC80102.1.
    AY049037 mRNA. Translation: AAL10687.1.
    AJ486882 mRNA. Translation: CAD31140.1.
    AJ486883 mRNA. Translation: CAD31141.1.
    AJ486884 mRNA. Translation: CAD31142.1.
    AJ486885 mRNA. Translation: CAD31143.1.
    AJ486886 mRNA. Translation: CAD31144.1.
    AJ486887 mRNA. Translation: CAD31145.1.
    AJ486888 mRNA. Translation: CAD31146.1.
    AM180572 Genomic DNA. Translation: CAJ55504.1.
    AB026660 Genomic DNA. Translation: BAB08874.1.
    CP002688 Genomic DNA. Translation: AED93107.1.
    AY054203 mRNA. Translation: AAL06864.1.
    AY070471 mRNA. Translation: AAL49937.1.
    AY149926 mRNA. Translation: AAN31080.1.
    RefSeqiNP_197692.1. NM_122207.3.
    UniGeneiAt.7567.

    Genome annotation databases

    EnsemblPlantsiAT5G23010.1; AT5G23010.1; AT5G23010.
    GeneIDi832365.
    KEGGiath:AT5G23010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ131517 Genomic DNA. Translation: CAC80102.1.
    AY049037 mRNA. Translation: AAL10687.1.
    AJ486882 mRNA. Translation: CAD31140.1.
    AJ486883 mRNA. Translation: CAD31141.1.
    AJ486884 mRNA. Translation: CAD31142.1.
    AJ486885 mRNA. Translation: CAD31143.1.
    AJ486886 mRNA. Translation: CAD31144.1.
    AJ486887 mRNA. Translation: CAD31145.1.
    AJ486888 mRNA. Translation: CAD31146.1.
    AM180572 Genomic DNA. Translation: CAJ55504.1.
    AB026660 Genomic DNA. Translation: BAB08874.1.
    CP002688 Genomic DNA. Translation: AED93107.1.
    AY054203 mRNA. Translation: AAL06864.1.
    AY070471 mRNA. Translation: AAL49937.1.
    AY149926 mRNA. Translation: AAN31080.1.
    RefSeqiNP_197692.1. NM_122207.3.
    UniGeneiAt.7567.

    3D structure databases

    ProteinModelPortaliQ9FG67.
    SMRiQ9FG67. Positions 83-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT5G23010.1.

    Proteomic databases

    PaxDbiQ9FG67.
    PRIDEiQ9FG67.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G23010.1; AT5G23010.1; AT5G23010.
    GeneIDi832365.
    KEGGiath:AT5G23010.

    Organism-specific databases

    TAIRiAT5G23010.

    Phylogenomic databases

    eggNOGiCOG0119.
    HOGENOMiHOG000046861.
    InParanoidiQ9FG67.
    KOiK15741.
    OMAiLQININT.
    PhylomeDBiQ9FG67.

    Enzyme and pathway databases

    BioCyciMetaCyc:AT5G23010-MONOMER.
    BRENDAi2.3.3.13. 399.

    Miscellaneous databases

    PROiQ9FG67.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR002034. AIPM/Hcit_synth_CS.
    IPR013785. Aldolase_TIM.
    IPR000891. PYR_CT.
    [Graphical view]
    PfamiPF00682. HMGL-like. 1 hit.
    [Graphical view]
    PROSITEiPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
    PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
    PS50991. PYR_CT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway."
      Kroymann J., Textor S., Tokuhisa J.G., Falk K.L., Bartram S., Gershenzon J., Mitchell-Olds T.
      Plant Physiol. 127:1077-1088(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-102 AND ALA-290, CHARACTERIZATION.
      Strain: cv. Columbia.
    2. "Isolation and expression analysis of the isopropylmalate synthase gene family of Arabidopsis thaliana."
      Junk D.J., Mourad G.S.
      J. Exp. Bot. 53:2453-2454(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    3. "Evolutionary dynamics of an Arabidopsis insect resistance quantitative trait locus."
      Kroymann J., Donnerhacke S., Schnabelrauch D., Mitchell-Olds T.
      Proc. Natl. Acad. Sci. U.S.A. 100:14587-14592(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS.
      Strain: cv. Aa-0, cv. Ag-0, cv. Ema-1, cv. Gy-0, cv. Landsberg erecta, cv. Mt-0, cv. Pla-0 and cv. Sorbo.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: cv. Sorbo.
    5. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
      Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    6. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    7. "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.
    8. "Alpha-keto acid elongation and glucosinolate biosynthesis in Arabidopsis thaliana."
      Campos de Quiros H., Magrath R., McCallum D., Kroymann J., Scnabelrauch D., Mitchell-Olds T., Mithen R.
      Theor. Appl. Genet. 101:429-437(2000)
      [AGRICOLA] [Europe PMC]
      Cited for: IDENTIFICATION.
    9. "Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana: recombinant expression and characterization of methylthioalkylmalate synthase, the condensing enzyme of the chain-elongation cycle."
      Textor S., Bartram S., Kroymann J., Falk K.L., Hick A., Pickett J.A., Gershenzon J.
      Planta 218:1026-1035(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: cv. Columbia.
    10. "MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths in Arabidopsis."
      Textor S., de Kraker J.-W., Hause B., Gershenzon J., Tokuhisa J.G.
      Plant Physiol. 144:60-71(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE, TISSUE SPECIFICITY.
    11. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAM1_ARATH
    AccessioniPrimary (citable) accession number: Q9FG67
    Secondary accession number(s): Q70YX4, Q70YX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 1, 2001
    Last modified: July 22, 2015
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The 5'-part of the gene encoding this protein is deleted in cv. Bl-0, cv. Di-G, cv. Landsberg erecta and cv. Petergof, while the complete gene is missing in cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-1 and cv. Wl-0.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.