MAM1_ARATH
ID MAM1_ARATH Reviewed; 506 AA.
AC Q9FG67; Q70YX4; Q70YX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Methylthioalkylmalate synthase 1, chloroplastic;
DE EC=2.3.3.17 {ECO:0000269|PubMed:14740211};
DE AltName: Full=2-isopropylmalate synthase 3;
DE Flags: Precursor;
GN Name=MAM1; Synonyms=IMS3, IPMS_AT2, MAM-L, MAML;
GN OrderedLocusNames=At5g23010; ORFNames=T20O7.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-102 AND ALA-290, AND
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=11706188; DOI=10.1104/pp.010416;
RA Kroymann J., Textor S., Tokuhisa J.G., Falk K.L., Bartram S.,
RA Gershenzon J., Mitchell-Olds T.;
RT "A gene controlling variation in Arabidopsis glucosinolate composition is
RT part of the methionine chain elongation pathway.";
RL Plant Physiol. 127:1077-1088(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12432038; DOI=10.1093/jxb/erf112;
RA Junk D.J., Mourad G.S.;
RT "Isolation and expression analysis of the isopropylmalate synthase gene
RT family of Arabidopsis thaliana.";
RL J. Exp. Bot. 53:2453-2454(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS.
RC STRAIN=cv. Aa-0, cv. Ag-0, cv. Ema-1, cv. Gy-0, cv. Landsberg erecta,
RC cv. Mt-0, cv. Pla-0, and cv. Sorbo;
RX PubMed=14506289; DOI=10.1073/pnas.1734046100;
RA Kroymann J., Donnerhacke S., Schnabelrauch D., Mitchell-Olds T.;
RT "Evolutionary dynamics of an Arabidopsis insect resistance quantitative
RT trait locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14587-14592(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Sorbo;
RX PubMed=16754868; DOI=10.1073/pnas.0601738103;
RA Benderoth M., Textor S., Windsor A.J., Mitchell-Olds T., Gershenzon J.,
RA Kroymann J.;
RT "Positive selection driving diversification in plant secondary
RT metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9118-9123(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP IDENTIFICATION.
RX AGRICOLA=IND22089415; DOI=10.1007/s001220051500;
RA Campos de Quiros H., Magrath R., McCallum D., Kroymann J., Scnabelrauch D.,
RA Mitchell-Olds T., Mithen R.;
RT "Alpha-keto acid elongation and glucosinolate biosynthesis in Arabidopsis
RT thaliana.";
RL Theor. Appl. Genet. 101:429-437(2000).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=14740211; DOI=10.1007/s00425-003-1184-3;
RA Textor S., Bartram S., Kroymann J., Falk K.L., Hick A., Pickett J.A.,
RA Gershenzon J.;
RT "Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana:
RT recombinant expression and characterization of methylthioalkylmalate
RT synthase, the condensing enzyme of the chain-elongation cycle.";
RL Planta 218:1026-1035(2004).
RN [10]
RP NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=17369439; DOI=10.1104/pp.106.091579;
RA Textor S., de Kraker J.-W., Hause B., Gershenzon J., Tokuhisa J.G.;
RT "MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths
RT in Arabidopsis.";
RL Plant Physiol. 144:60-71(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Determines the side chain length of aliphatic glucosinolate
CC structures. Catalyzes exclusively the condensation reactions of both
CC the first and second methionine carbon chain elongation.
CC {ECO:0000269|PubMed:14740211, ECO:0000269|PubMed:16754868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an omega-(methylsulfanyl)-2-oxoalkanoate + H2O =
CC a 2-(omega-methylsulfanyl)alkylmalate + CoA + H(+);
CC Xref=Rhea:RHEA:50624, Rhea:RHEA-COMP:12823, Rhea:RHEA-COMP:12824,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:133493, ChEBI:CHEBI:133494;
CC EC=2.3.3.17; Evidence={ECO:0000269|PubMed:14740211};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Manganese or any other divalent metal ion, except copper or zinc.;
CC -!- ACTIVITY REGULATION: 1 mM DTT required for activity. Activated by ATP
CC and inhibited by iodoacetamide. {ECO:0000269|PubMed:14740211}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 mM for 4-methylthio-2-oxobutanoic acid
CC {ECO:0000269|PubMed:14740211};
CC KM=11.2 mM for 2-oxohexanoic acid {ECO:0000269|PubMed:14740211};
CC KM=0.64 mM for 5-methylthio-2-oxopentanoic acid
CC {ECO:0000269|PubMed:14740211};
CC KM=7.5 mM for 2-oxoheptanoic acid {ECO:0000269|PubMed:14740211};
CC KM=245 uM for acetyl-CoA {ECO:0000269|PubMed:14740211};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:14740211};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius.
CC {ECO:0000269|PubMed:14740211};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14740211}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, flowers, roots and
CC siliques. Not detected in flowers in PubMed:12432038.
CC {ECO:0000269|PubMed:12432038, ECO:0000269|PubMed:17369439}.
CC -!- DOMAIN: The N-terminal part of the protein controls substrate
CC specificity.
CC -!- MISCELLANEOUS: The 5'-part of the gene encoding this protein is deleted
CC in cv. Bl-0, cv. Di-G, cv. Landsberg erecta and cv. Petergof, while the
CC complete gene is missing in cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0,
CC cv. Tsu-1 and cv. Wl-0.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; AJ131517; CAC80102.1; -; Genomic_DNA.
DR EMBL; AY049037; AAL10687.1; -; mRNA.
DR EMBL; AJ486882; CAD31140.1; -; mRNA.
DR EMBL; AJ486883; CAD31141.1; -; mRNA.
DR EMBL; AJ486884; CAD31142.1; -; mRNA.
DR EMBL; AJ486885; CAD31143.1; -; mRNA.
DR EMBL; AJ486886; CAD31144.1; -; mRNA.
DR EMBL; AJ486887; CAD31145.1; -; mRNA.
DR EMBL; AJ486888; CAD31146.1; -; mRNA.
DR EMBL; AM180572; CAJ55504.1; -; Genomic_DNA.
DR EMBL; AB026660; BAB08874.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93107.1; -; Genomic_DNA.
DR EMBL; AY054203; AAL06864.1; -; mRNA.
DR EMBL; AY070471; AAL49937.1; -; mRNA.
DR EMBL; AY149926; AAN31080.1; -; mRNA.
DR RefSeq; NP_197692.1; NM_122207.3.
DR AlphaFoldDB; Q9FG67; -.
DR SMR; Q9FG67; -.
DR STRING; 3702.AT5G23010.1; -.
DR iPTMnet; Q9FG67; -.
DR PaxDb; Q9FG67; -.
DR PRIDE; Q9FG67; -.
DR ProteomicsDB; 238875; -.
DR EnsemblPlants; AT5G23010.1; AT5G23010.1; AT5G23010.
DR GeneID; 832365; -.
DR Gramene; AT5G23010.1; AT5G23010.1; AT5G23010.
DR KEGG; ath:AT5G23010; -.
DR Araport; AT5G23010; -.
DR TAIR; locus:2181151; AT5G23010.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_022158_3_1_1; -.
DR InParanoid; Q9FG67; -.
DR PhylomeDB; Q9FG67; -.
DR BioCyc; MetaCyc:AT5G23010-MON; -.
DR BRENDA; 2.3.3.13; 399.
DR BRENDA; 2.3.3.17; 399.
DR PRO; PR:Q9FG67; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG67; baseline and differential.
DR Genevisible; Q9FG67; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0010177; F:2-(2'-methylthio)ethylmalate synthase activity; IDA:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009625; P:response to insect; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Phosphoprotein; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..506
FT /note="Methylthioalkylmalate synthase 1, chloroplastic"
FT /id="PRO_0000315841"
FT DOMAIN 85..359
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VARIANT 10
FT /note="V -> G (in strain: cv. Sorbo)"
FT VARIANT 42
FT /note="N -> K (in strain: cv. Ema-1 and cv. Pla-0)"
FT VARIANT 44
FT /note="A -> T (in strain: cv. Sorbo)"
FT VARIANT 505
FT /note="N -> T (in strain: cv. Sorbo)"
FT MUTAGEN 102
FT /note="S->F: In gsm1-1; loss of conversion of C3 to C4
FT glucosinolates."
FT /evidence="ECO:0000269|PubMed:11706188"
FT MUTAGEN 290
FT /note="A->T: In gsm1-2; loss of conversion of C3 to C4
FT glucosinolates."
FT /evidence="ECO:0000269|PubMed:11706188"
SQ SEQUENCE 506 AA; 55125 MW; A3F4CC32508CAE49 CRC64;
MASSLLTSSV MIPTTGSTVV GRSVLPFQSS LHSLRLTHSY KNPALFISCC SSVSKNAATS
STDLKPVVER WPEYIPNKLP DGNYVRVFDT TLRDGEQSPG GSLTPPQKLE IARQLAKLRV
DIMEVGFPGS SEEELETIKT IAKTVGNEVD EETGYVPVIC AIARCKHRDI EATWEALKYA
KRPRILVFTS TSDIHMKYKL KKTQEEVIEM AVSSIRFAKS LGFNDIQFGC EDGGRSDKDF
LCKILGEAIK AGVTVVTIGD TVGINMPHEY GELVTYLKAN TPGIDDVVVA VHCHNDLGLA
TANSIAGIRA GARQVEVTIN GIGERSGNAS LEEVVMALKC RGAYVINGVY TKIDTRQIMA
TSKMVQEYTG LYVQAHKPIV GANCFVHESG IHQDGILKNR STYEILSPED IGIVKSQNSG
LVLGKLSGRH AVKDRLKELG YELDDEKLNA VFSLFRDLTK NKKRITDADL KALVTSSDEI
SLEKLNGANG LKSNGYIPVP QVSSNV
