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Q9FG67

- MAM1_ARATH

UniProt

Q9FG67 - MAM1_ARATH

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Protein

Methylthioalkylmalate synthase 1, chloroplastic

Gene

MAM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

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

  1. 2-(2'-methylthio)ethylmalate synthase activity Source: TAIR

GO - Biological processi

  1. carboxylic acid metabolic process Source: InterPro
  2. glucosinolate biosynthetic process Source: TAIR
  3. response to insect Source: TAIR
  4. 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: Chromosome 5

Organism-specific databases

TAIRiAT5G23010.

Subcellular locationi

Plastidchloroplast Curated

GO - Cellular componenti

  1. 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

Gene expression databases

ExpressionAtlasiQ9FG67. baseline and differential.
GenevestigatoriQ9FG67.

Interactioni

Subunit structurei

Monomer.1 Publication

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.
OMAiIEMAVSS.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_197692.1. NM_122207.3.
UniGenei At.7567.

3D structure databases

ProteinModelPortali Q9FG67.
SMRi Q9FG67. Positions 83-473.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9FG67.
PRIDEi Q9FG67.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G23010.1 ; AT5G23010.1 ; AT5G23010 .
GeneIDi 832365.
KEGGi ath:AT5G23010.

Organism-specific databases

TAIRi AT5G23010.

Phylogenomic databases

eggNOGi COG0119.
HOGENOMi HOG000046861.
InParanoidi Q9FG67.
KOi K15741.
OMAi IEMAVSS.
PhylomeDBi Q9FG67.

Enzyme and pathway databases

BioCyci MetaCyc:AT5G23010-MONOMER.
BRENDAi 2.3.3.13. 399.

Gene expression databases

ExpressionAtlasi Q9FG67. baseline and differential.
Genevestigatori Q9FG67.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR000891. PYR_CT.
[Graphical view ]
Pfami PF00682. HMGL-like. 1 hit.
[Graphical view ]
PROSITEi PS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 93 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