MAM2_ARATH
ID MAM2_ARATH Reviewed; 506 AA.
AC Q8VX04; Q70YW3; Q70YW8; Q70YX0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Methylthioalkylmalate synthase 2, chloroplastic;
DE EC=2.3.3.17 {ECO:0000250|UniProtKB:Q9FG67};
DE Flags: Precursor;
GN Name=MAM2;
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. Landsberg erecta;
RA Kroymann J., Schnabelrauch D., Mitchell-Olds T.;
RT "A MYB transcription factor and a gene similar to MYJ24.1 are encoded in
RT the region between MRN17 and MYJ24.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS.
RC STRAIN=cv. Bl-0, cv. Di-G, cv. Ka-0, cv. Landsberg erecta, cv. Lip-0,
RC cv. No-0, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tsu-0, 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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS, AND FUNCTION.
RC STRAIN=cv. Landsberg erecta, and 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 [4]
RP NOMENCLATURE.
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: Catalyzes only the first methionine chain elongation cycle.
CC {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:0000250|UniProtKB:Q9FG67};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DOMAIN: The N-terminal part of the protein controls substrate
CC specificity.
CC -!- MISCELLANEOUS: The gene encoding this protein is not present in cv. Aa-
CC 0, cv. Ag-0, cv. Columbia, cv. Ema-1, cv. Gy-0, cv. Mt-0 and cv. Pla-0.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; AJ133892; CAC80207.1; -; mRNA.
DR EMBL; AJ486889; CAD31147.1; -; mRNA.
DR EMBL; AJ486890; CAD31148.1; -; mRNA.
DR EMBL; AJ486891; CAD31149.1; -; mRNA.
DR EMBL; AJ486892; CAD31150.1; -; mRNA.
DR EMBL; AJ486893; CAD31151.1; -; mRNA.
DR EMBL; AJ486894; CAD31152.1; -; mRNA.
DR EMBL; AJ486895; CAD31153.1; -; mRNA.
DR EMBL; AJ486896; CAD31154.1; -; mRNA.
DR EMBL; AJ486897; CAD31155.1; -; mRNA.
DR EMBL; AJ486898; CAD31156.1; -; mRNA.
DR EMBL; AJ486899; CAD31157.1; -; mRNA.
DR EMBL; AM180571; CAJ55503.1; -; Genomic_DNA.
DR EMBL; AM180569; CAJ55501.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VX04; -.
DR SMR; Q8VX04; -.
DR BioCyc; ARA:MAM2-MON; -.
DR BRENDA; 2.3.3.17; 399.
DR PRO; PR:Q8VX04; -.
DR ExpressionAtlas; Q8VX04; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0010177; F:2-(2'-methylthio)ethylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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 2: Evidence at transcript level;
KW Chloroplast; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..506
FT /note="Methylthioalkylmalate synthase 2, chloroplastic"
FT /id="PRO_5000064969"
FT DOMAIN 85..359
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT VARIANT 67
FT /note="A -> V (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 75
FT /note="L -> I (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 86
FT /note="R -> H (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 109
FT /note="L -> Q (in strain: cv. Sorbo)"
FT VARIANT 252
FT /note="D -> G (in strain: cv. Bl-0, cv. Ka-0, cv. Lip-0,
FT cv. No-0, cv. Sei-0, cv. Sorbo, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 450
FT /note="A -> V (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 470
FT /note="M -> L (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 479
FT /note="G -> E (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
FT VARIANT 485
FT /note="S -> L (in strain: cv. Ka-0, cv. Lip-0, cv. No-0,
FT cv. Sei-0, cv. Tsu-0 and cv. Wl-0)"
SQ SEQUENCE 506 AA; 55130 MW; DB9C306055E8C82A CRC64;
MASSLLTSSG MIPTTGSTVV GRSVLPFQSS LHSLRLTHSY KNPALFISCC SSVSKNAATS
STDLKPAVER WPEYLPNKLP DENYVRVFDT TLRDGEQAPG GSLTPPQKLE IARQLAKLRV
DIMEVGFPGS SEEELETVKT IAKTVGNEVD EETGYVPVIC AIARSKHRDI EAAWEAVKYA
KRPRILIFTS TSDIHMKYKL KKTQEEVIEM AVSSIRFAKS LGFNDIQLGC EDGGRSDKDF
LCKILGEAIK ADVTVVNVAD TVGINMPHEY AELVTYLKAN TPGIDDVVFS VHCHNDLGLA
TANSIAGIRA GARQVEVTIN GIGERSGNAS LEEVVMALKC RGAYVINGVY TRIDTRQIMA
TSKMVQEYTG LYVQAHKPIV GANCFVHESG IHQDGILKNR STYEILSPED IGIVKSQNSG
LVLGKLSGRH AVKDRLKELG YELDDEKLNA VFSLFRDLTK NKKRITDADM KALVTSSDGI
SLEKSNGANG LKSNGYIPVL QVSSNV
