MAM3_ARATH
ID MAM3_ARATH Reviewed; 503 AA.
AC Q9FN52; Q70YR5; Q70YR9; Q70YS1; Q70YS3; Q8VX05; Q8VX46; Q9C5X5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Methylthioalkylmalate synthase 3, chloroplastic;
DE EC=2.3.3.17 {ECO:0000269|PubMed:17369439};
DE AltName: Full=2-isopropylmalate synthase 2;
DE AltName: Full=Methylthioalkylmalate synthase-like;
DE Flags: Precursor;
GN Name=MAM3; Synonyms=IMS2, IPMS_AT1, MAM-L, MAM1;
GN OrderedLocusNames=At5g23020; ORFNames=MYJ24.1;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Pistelli L., De Bellis L., Alpi A.;
RT "Molecular cloning and sequencing of a full lenght cDNA clone encodign 2-
RT isopropylamalate synthase of Arabidopsis thaliana and its expression
RT analysis.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ISOPROPYLMALATE
RP SYNTHASE ACTIVITY.
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. Bl-0, cv. Di-G, cv. Ema-1, cv. Gy-0,
RC cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. Mt-0, cv. No-0,
RC cv. Petergof, cv. Pla-0, cv. Sei-0, cv. Sorbo, cv. Tsu-1, and cv. Wl-0;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=15155874; DOI=10.1104/pp.104.039347;
RA Field B., Cardon G., Traka M., Botterman J., Vancanneyt G., Mithen R.;
RT "Glucosinolate and amino acid biosynthesis in Arabidopsis.";
RL Plant Physiol. 135:828-839(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP GLY-263, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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).
CC -!- FUNCTION: Determines the side chain length of aliphatic glucosinolate
CC structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed
CC to form the known C3 to C8 glucosinolates. Also able to convert
CC pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-
CC 2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived
CC glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates
CC and phenylpyruvate to phenylethylglucosinolate.
CC {ECO:0000269|PubMed:15155874, ECO:0000269|PubMed:17369439}.
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:17369439};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Manganese or any other divalent metal ion.;
CC -!- ACTIVITY REGULATION: Not activated by ATP.
CC {ECO:0000269|PubMed:17369439}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=932 uM for 4-methylthio-2-oxobutanoic acid
CC {ECO:0000269|PubMed:17369439};
CC KM=476 uM for 5-methylthio-2-oxopentanoic acid
CC {ECO:0000269|PubMed:17369439};
CC KM=463 uM for 6-methylthio-2-oxohexanoic acid
CC {ECO:0000269|PubMed:17369439};
CC KM=253 uM for 8-methylthio-2-oxooctanoic acid
CC {ECO:0000269|PubMed:17369439};
CC KM=81 uM for 9-methylthio-2-oxononanoic acid
CC {ECO:0000269|PubMed:17369439};
CC KM=1.0 mM for 2-oxoisovalerate {ECO:0000269|PubMed:17369439};
CC KM=8.6 mM for pyruvate {ECO:0000269|PubMed:17369439};
CC KM=2.3 mM for acetyl-CoA {ECO:0000269|PubMed:17369439};
CC Vmax=1448 nmol/min/mg enzyme with 4-methylthio-2-oxobutanoic acid as
CC substrate {ECO:0000269|PubMed:17369439};
CC Vmax=1495 nmol/min/mg enzyme with 5-methylthio-2-oxopentanoic acid as
CC substrate {ECO:0000269|PubMed:17369439};
CC Vmax=2869 nmol/min/mg enzyme with 6-methylthio-2-oxohexanoic acid as
CC substrate {ECO:0000269|PubMed:17369439};
CC Vmax=364 nmol/min/mg enzyme with 8-methylthio-2-oxooctanoic acid as
CC substrate {ECO:0000269|PubMed:17369439};
CC Vmax=31 nmol/min/mg enzyme with 9-methylthio-2-oxononanoic acid as
CC substrate {ECO:0000269|PubMed:17369439};
CC Vmax=199 nmol/min/mg enzyme with 2-oxoisovalerate as substrate
CC {ECO:0000269|PubMed:17369439};
CC Vmax=191 nmol/min/mg enzyme with pyruvate as substrate
CC {ECO:0000269|PubMed:17369439};
CC Vmax=3344 nmol/min/mg enzyme with acetyl-CoA as substrate
CC {ECO:0000269|PubMed:17369439};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17369439};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius.
CC {ECO:0000269|PubMed:17369439};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17369439}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, leaves, and siliques.
CC Lower amounts in stems and flowers. {ECO:0000269|PubMed:12432038,
CC ECO:0000269|PubMed:17369439}.
CC -!- MISCELLANEOUS: Constitutes an insect resistance quantitative trait
CC locus, caused by variation in glucosinolate profiles conferred by
CC polymorphism of MAM alleles.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; AJ421793; CAD18966.1; -; mRNA.
DR EMBL; AF327648; AAG52883.1; -; mRNA.
DR EMBL; AJ486937; CAD31195.1; -; mRNA.
DR EMBL; AJ486938; CAD31196.1; -; mRNA.
DR EMBL; AJ486939; CAD31197.1; -; mRNA.
DR EMBL; AJ486940; CAD31198.1; -; mRNA.
DR EMBL; AJ486941; CAD31199.1; -; mRNA.
DR EMBL; AJ486942; CAD31200.1; -; mRNA.
DR EMBL; AJ486943; CAD31201.1; -; mRNA.
DR EMBL; AJ486944; CAD31202.1; -; mRNA.
DR EMBL; AJ486945; CAD31203.1; -; mRNA.
DR EMBL; AJ486946; CAD31204.1; -; mRNA.
DR EMBL; AJ486947; CAD31205.1; -; mRNA.
DR EMBL; AJ486948; CAD31206.1; -; mRNA.
DR EMBL; AJ486949; CAD31207.1; -; mRNA.
DR EMBL; AJ486950; CAD31208.1; -; mRNA.
DR EMBL; AJ486951; CAD31209.1; -; mRNA.
DR EMBL; AJ486952; CAD31210.1; -; mRNA.
DR EMBL; AJ486953; CAD31211.1; -; mRNA.
DR EMBL; AJ131518; CAC80103.1; -; mRNA.
DR EMBL; AM180570; CAJ55502.1; -; Genomic_DNA.
DR EMBL; AM180573; CAJ55505.1; -; Genomic_DNA.
DR EMBL; AB006708; BAB09819.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93108.1; -; Genomic_DNA.
DR EMBL; AY099549; AAM20401.1; -; mRNA.
DR EMBL; BT008874; AAP68313.1; -; mRNA.
DR RefSeq; NP_197693.1; NM_122208.4.
DR AlphaFoldDB; Q9FN52; -.
DR SMR; Q9FN52; -.
DR STRING; 3702.AT5G23020.1; -.
DR PaxDb; Q9FN52; -.
DR PRIDE; Q9FN52; -.
DR ProteomicsDB; 238866; -.
DR EnsemblPlants; AT5G23020.1; AT5G23020.1; AT5G23020.
DR GeneID; 832366; -.
DR Gramene; AT5G23020.1; AT5G23020.1; AT5G23020.
DR KEGG; ath:AT5G23020; -.
DR Araport; AT5G23020; -.
DR TAIR; locus:2178317; AT5G23020.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_022158_3_1_1; -.
DR InParanoid; Q9FN52; -.
DR OMA; ERRPEYI; -.
DR OrthoDB; 928619at2759; -.
DR PhylomeDB; Q9FN52; -.
DR BioCyc; MetaCyc:AT5G23020-MON; -.
DR BRENDA; 2.3.3.13; 399.
DR BRENDA; 2.3.3.17; 399.
DR PRO; PR:Q9FN52; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN52; baseline and differential.
DR Genevisible; Q9FN52; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0010177; F:2-(2'-methylthio)ethylmalate synthase activity; IDA:TAIR.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; NAS:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
DR GO; GO:0009098; P:leucine biosynthetic process; TAS: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; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..503
FT /note="Methylthioalkylmalate synthase 3, chloroplastic"
FT /id="PRO_0000315842"
FT DOMAIN 85..359
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT VARIANT 10
FT /note="S -> I (in strain: cv. Sorbo)"
FT VARIANT 17
FT /note="R -> P (in strain: cv. Bl-0, cv. Di-G, cv. Ema-1,
FT cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv.
FT Petergof, cv. Sei-0, cv. Sorbo, cv. Tsu-1, cv. Wl-0 and
FT cv.Pla-0)"
FT VARIANT 24
FT /note="G -> A (in strain: cv. Sorbo)"
FT VARIANT 46
FT /note="F -> L (in strain: cv. Sorbo)"
FT VARIANT 46
FT /note="F -> S (in strain: cv. Ema-1)"
FT VARIANT 68
FT /note="M -> V (in strain: cv. Bl-0, cv. Di-G, cv. Landsberg
FT erecta and cv. Petergof)"
FT VARIANT 156
FT /note="V -> A (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-1 and cv. Wl-0)"
FT VARIANT 241
FT /note="I -> L (in strain: cv. Bl-0, cv. Di-G, cv. Ka-0, cv.
FT Landsberg erecta, cv. Lip-0, cv. No-0, cv. Petergof, cv.
FT Sei-0, cv. Tsu-1 and cv. Wl-0)"
FT MUTAGEN 263
FT /note="G->E: In gsm2-1; loss of activity and lack of C6, C7
FT and C8 aliphatic glucosinolates."
FT /evidence="ECO:0000269|PubMed:17369439"
FT CONFLICT 156
FT /note="V -> A (in Ref. 1; CAD18966)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="C -> S (in Ref. 2; AAG52883)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="I -> L (in Ref. 1; CAD18966)"
FT /evidence="ECO:0000305"
FT CONFLICT 428..429
FT /note="GR -> DV (in Ref. 1; CAD18966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 55230 MW; AF4FBB8F6B1099F8 CRC64;
MASLLLTSSS MITTSCRSMV LRSGLPIGSS FPSLRLTRPY DKATLFVSCC SAESKKVATS
ATDLKPIMER RPEYIPNKLP HKNYVRVLDT TLRDGEQSPG AALTPPQKLE IARQLAKLRV
DIMEVGFPVS SEEEFEAIKT IAKTVGNEVD EETGYVPVIC GIARCKKRDI EATWEALKYA
KRPRVMLFTS TSEIHMKYKL KKTKEEVIEM AVNSVKYAKS LGFKDIQFGC EDGGRTEKDF
ICKILGESIK AGATTVGFAD TVGINMPQEF GELVAYVIEN TPGADDIVFA IHCHNDLGVA
TANTISGICA GARQVEVTIN GIGERSGNAP LEEVVMALKC RGESLMDGVY TKIDSRQIMA
TSKMVQEHTG MYVQPHKPIV GDNCFVHESG IHQDGILKNR STYEILSPED VGIVKSENSG
IVLGKLSGRH AVKDRLKELG YEISDEKFND IFSRYRELTK DKKRITDADL KALVVNGAEI
SSEKLNSKGI NDLMSSPQIS AVV
