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Methylthioalkylmalate synthase 3, chloroplastic (EC 2.3.3.17) (2-isopropylmalate synthase 2) (Methylthioalkylmalate synthase-like)

 MAM3_ARATH              Reviewed;         503 AA.
Q9FN52; Q70YR5; Q70YR9; Q70YS1; Q70YS3; Q8VX05; Q8VX46; Q9C5X5;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 114.
RecName: Full=Methylthioalkylmalate synthase 3, chloroplastic;
EC=2.3.3.17 {ECO:0000269|PubMed:17369439};
AltName: Full=2-isopropylmalate synthase 2;
AltName: Full=Methylthioalkylmalate synthase-like;
Flags: Precursor;
Name=MAM3; Synonyms=IMS2, IPMS_AT1, MAM-L, MAM1;
OrderedLocusNames=At5g23020; ORFNames=MYJ24.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Pistelli L., De Bellis L., Alpi A.;
"Molecular cloning and sequencing of a full lenght cDNA clone encodign
2-isopropylamalate synthase of Arabidopsis thaliana and its expression
analysis.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ISOPROPYLMALATE
SYNTHASE ACTIVITY.
PubMed=12432038; DOI=10.1093/jxb/erf112;
Junk D.J., Mourad G.S.;
"Isolation and expression analysis of the isopropylmalate synthase
gene family of Arabidopsis thaliana.";
J. Exp. Bot. 53:2453-2454(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS.
STRAIN=cv. Aa-0, cv. Ag-0, cv. Bl-0, cv. Di-G, cv. Ema-1, cv. Gy-0,
cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. Mt-0, cv. No-0,
cv. Petergof, cv. Pla-0, cv. Sei-0, cv. Sorbo, cv. Tsu-1, and
cv. Wl-0;
PubMed=14506289; DOI=10.1073/pnas.1734046100;
Kroymann J., Donnerhacke S., Schnabelrauch D., Mitchell-Olds T.;
"Evolutionary dynamics of an Arabidopsis insect resistance
quantitative trait locus.";
Proc. Natl. Acad. Sci. U.S.A. 100:14587-14592(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9405937; DOI=10.1093/dnares/4.4.291;
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II.
Sequence features of the regions of 1,044,062 bp covered by thirteen
physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
IDENTIFICATION.
AGRICOLA=IND22089415; DOI=10.1007/s001220051500;
Campos de Quiros H., Magrath R., McCallum D., Kroymann J.,
Scnabelrauch D., Mitchell-Olds T., Mithen R.;
"Alpha-keto acid elongation and glucosinolate biosynthesis in
Arabidopsis thaliana.";
Theor. Appl. Genet. 101:429-437(2000).
[8]
FUNCTION.
PubMed=15155874; DOI=10.1104/pp.104.039347;
Field B., Cardon G., Traka M., Botterman J., Vancanneyt G., Mithen R.;
"Glucosinolate and amino acid biosynthesis in Arabidopsis.";
Plant Physiol. 135:828-839(2004).
[9]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
GLY-263, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=17369439; DOI=10.1104/pp.106.091579;
Textor S., de Kraker J.-W., Hause B., Gershenzon J., Tokuhisa J.G.;
"MAM3 catalyzes the formation of all aliphatic glucosinolate chain
lengths in Arabidopsis.";
Plant Physiol. 144:60-71(2007).
-!- FUNCTION: Determines the side chain length of aliphatic
glucosinolate structures. Accepts all the omega-methylthio-2-
oxoalkanoic acids needed to form the known C3 to C8
glucosinolates. Also able to convert pyruvate to citramalate, 2-
oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-
methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-
oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to
phenylethylglucosinolate. {ECO:0000269|PubMed:15155874,
ECO:0000269|PubMed:17369439}.
-!- CATALYTIC ACTIVITY: An omega-(methylthio)-2-oxoalkanoate + acetyl-
CoA + H(2)O = a 2-(omega-methylthio)alkylmalate + CoA.
{ECO:0000269|PubMed:17369439}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Note=Manganese or any other divalent metal ion.;
-!- ENZYME REGULATION: Not activated by ATP.
{ECO:0000269|PubMed:17369439}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=932 uM for 4-methylthio-2-oxobutanoic acid
{ECO:0000269|PubMed:17369439};
KM=476 uM for 5-methylthio-2-oxopentanoic acid
{ECO:0000269|PubMed:17369439};
KM=463 uM for 6-methylthio-2-oxohexanoic acid
{ECO:0000269|PubMed:17369439};
KM=253 uM for 8-methylthio-2-oxooctanoic acid
{ECO:0000269|PubMed:17369439};
KM=81 uM for 9-methylthio-2-oxononanoic acid
{ECO:0000269|PubMed:17369439};
KM=1.0 mM for 2-oxoisovalerate {ECO:0000269|PubMed:17369439};
KM=8.6 mM for pyruvate {ECO:0000269|PubMed:17369439};
KM=2.3 mM for acetyl-CoA {ECO:0000269|PubMed:17369439};
Vmax=1448 nmol/min/mg enzyme with 4-methylthio-2-oxobutanoic
acid as substrate {ECO:0000269|PubMed:17369439};
Vmax=1495 nmol/min/mg enzyme with 5-methylthio-2-oxopentanoic
acid as substrate {ECO:0000269|PubMed:17369439};
Vmax=2869 nmol/min/mg enzyme with 6-methylthio-2-oxohexanoic
acid as substrate {ECO:0000269|PubMed:17369439};
Vmax=364 nmol/min/mg enzyme with 8-methylthio-2-oxooctanoic acid
as substrate {ECO:0000269|PubMed:17369439};
Vmax=31 nmol/min/mg enzyme with 9-methylthio-2-oxononanoic acid
as substrate {ECO:0000269|PubMed:17369439};
Vmax=199 nmol/min/mg enzyme with 2-oxoisovalerate as substrate
{ECO:0000269|PubMed:17369439};
Vmax=191 nmol/min/mg enzyme with pyruvate as substrate
{ECO:0000269|PubMed:17369439};
Vmax=3344 nmol/min/mg enzyme with acetyl-CoA as substrate
{ECO:0000269|PubMed:17369439};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:17369439};
Temperature dependence:
Optimum temperature is 32 degrees Celsius.
{ECO:0000269|PubMed:17369439};
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:17369439}.
-!- TISSUE SPECIFICITY: Highly expressed in roots, leaves, and
siliques. Lower amounts in stems and flowers.
{ECO:0000269|PubMed:12432038, ECO:0000269|PubMed:17369439}.
-!- MISCELLANEOUS: Constitutes an insect resistance quantitative trait
locus, caused by variation in glucosinolate profiles conferred by
polymorphism of MAM alleles.
-!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ421793; CAD18966.1; -; mRNA.
EMBL; AF327648; AAG52883.1; -; mRNA.
EMBL; AJ486937; CAD31195.1; -; mRNA.
EMBL; AJ486938; CAD31196.1; -; mRNA.
EMBL; AJ486939; CAD31197.1; -; mRNA.
EMBL; AJ486940; CAD31198.1; -; mRNA.
EMBL; AJ486941; CAD31199.1; -; mRNA.
EMBL; AJ486942; CAD31200.1; -; mRNA.
EMBL; AJ486943; CAD31201.1; -; mRNA.
EMBL; AJ486944; CAD31202.1; -; mRNA.
EMBL; AJ486945; CAD31203.1; -; mRNA.
EMBL; AJ486946; CAD31204.1; -; mRNA.
EMBL; AJ486947; CAD31205.1; -; mRNA.
EMBL; AJ486948; CAD31206.1; -; mRNA.
EMBL; AJ486949; CAD31207.1; -; mRNA.
EMBL; AJ486950; CAD31208.1; -; mRNA.
EMBL; AJ486951; CAD31209.1; -; mRNA.
EMBL; AJ486952; CAD31210.1; -; mRNA.
EMBL; AJ486953; CAD31211.1; -; mRNA.
EMBL; AJ131518; CAC80103.1; -; mRNA.
EMBL; AM180570; CAJ55502.1; -; Genomic_DNA.
EMBL; AM180573; CAJ55505.1; -; Genomic_DNA.
EMBL; AB006708; BAB09819.1; -; Genomic_DNA.
EMBL; CP002688; AED93108.1; -; Genomic_DNA.
EMBL; AY099549; AAM20401.1; -; mRNA.
EMBL; BT008874; AAP68313.1; -; mRNA.
RefSeq; NP_197693.1; NM_122208.4.
UniGene; At.20469; -.
ProteinModelPortal; Q9FN52; -.
SMR; Q9FN52; -.
STRING; 3702.AT5G23020.1; -.
PaxDb; Q9FN52; -.
PRIDE; Q9FN52; -.
EnsemblPlants; AT5G23020.1; AT5G23020.1; AT5G23020.
GeneID; 832366; -.
Gramene; AT5G23020.1; AT5G23020.1; AT5G23020.
KEGG; ath:AT5G23020; -.
Araport; AT5G23020; -.
TAIR; locus:2178317; AT5G23020.
eggNOG; KOG2367; Eukaryota.
eggNOG; COG0119; LUCA.
InParanoid; Q9FN52; -.
KO; K15742; -.
OMA; ERRPEYI; -.
OrthoDB; EOG093608QE; -.
PhylomeDB; Q9FN52; -.
BioCyc; MetaCyc:AT5G23020-MONOMER; -.
BRENDA; 2.3.3.13; 399.
PRO; PR:Q9FN52; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9FN52; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0010177; F:2-(2'-methylthio)ethylmalate synthase activity; IDA:TAIR.
GO; GO:0003852; F:2-isopropylmalate synthase activity; NAS:TAIR.
GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
GO; GO:0009098; P:leucine biosynthetic process; TAS:TAIR.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR002034; AIPM/Hcit_synth_CS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000891; PYR_CT.
Pfam; PF00682; HMGL-like; 1.
PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
PROSITE; PS50991; PYR_CT; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Plastid; Reference proteome;
Transferase; Transit peptide.
TRANSIT 1 51 Chloroplast. {ECO:0000255}.
CHAIN 52 503 Methylthioalkylmalate synthase 3,
chloroplastic.
/FTId=PRO_0000315842.
DOMAIN 85 359 Pyruvate carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01151}.
VARIANT 10 10 S -> I (in strain: cv. Sorbo).
VARIANT 17 17 R -> P (in strain: cv. Bl-0, cv. Di-G,
cv. Ema-1, cv. Ka-0, cv. Landsberg
erecta, cv. Lip-0, cv. No-0, cv.
Petergof, cv. Sei-0, cv. Sorbo, cv. Tsu-
1, cv. Wl-0 and cv.Pla-0).
VARIANT 24 24 G -> A (in strain: cv. Sorbo).
VARIANT 46 46 F -> L (in strain: cv. Sorbo).
VARIANT 46 46 F -> S (in strain: cv. Ema-1).
VARIANT 68 68 M -> V (in strain: cv. Bl-0, cv. Di-G,
cv. Landsberg erecta and cv. Petergof).
VARIANT 156 156 V -> A (in strain: cv. Ka-0, cv. Lip-0,
cv. No-0, cv. Sei-0, cv. Tsu-1 and cv.
Wl-0).
VARIANT 241 241 I -> L (in strain: cv. Bl-0, cv. Di-G,
cv. Ka-0, cv. Landsberg erecta, cv. Lip-
0, cv. No-0, cv. Petergof, cv. Sei-0, cv.
Tsu-1 and cv. Wl-0).
MUTAGEN 263 263 G->E: In gsm2-1; loss of activity and
lack of C6, C7 and C8 aliphatic
glucosinolates.
{ECO:0000269|PubMed:17369439}.
CONFLICT 156 156 V -> A (in Ref. 1; CAD18966).
{ECO:0000305}.
CONFLICT 160 160 C -> S (in Ref. 2; AAG52883).
{ECO:0000305}.
CONFLICT 241 241 I -> L (in Ref. 1; CAD18966).
{ECO:0000305}.
CONFLICT 428 429 GR -> DV (in Ref. 1; CAD18966).
{ECO:0000305}.
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


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