LEU12_ARATH
ID LEU12_ARATH Reviewed; 631 AA.
AC Q9C550; Q8GWX8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=2-isopropylmalate synthase 2, chloroplastic {ECO:0000303|PubMed:17189332};
DE EC=2.3.3.13 {ECO:0000269|PubMed:15155874, ECO:0000269|PubMed:17189332};
DE AltName: Full=2-isopropylmalate synthase 1 {ECO:0000303|PubMed:12432038};
DE AltName: Full=Methylthioalkylmalate synthase-like 3 {ECO:0000303|PubMed:15155874};
DE Flags: Precursor;
GN Name=IPMS2 {ECO:0000303|PubMed:17189332};
GN Synonyms=IMS1 {ECO:0000303|PubMed:12432038},
GN MAML-3 {ECO:0000303|PubMed:15155874};
GN OrderedLocusNames=At1g74040 {ECO:0000312|Araport:AT1G74040};
GN ORFNames=F2P9.9 {ECO:0000312|EMBL:AAG52530.1};
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
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 [7]
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION
RP PHENOTYPE, AND COFACTOR.
RC STRAIN=cv. Columbia;
RX PubMed=17189332; DOI=10.1104/pp.106.085555;
RA de Kraker J.-W., Luck K., Textor S., Tokuhisa J.G., Gershenzon J.;
RT "Two Arabidopsis genes (IPMS1 and IPMS2) encode isopropylmalate synthase,
RT the branchpoint step in the biosynthesis of leucine.";
RL Plant Physiol. 143:970-986(2007).
RN [8]
RP 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: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). Involved in Leu
CC biosynthesis, but do not participate in the chain elongation of
CC glucosinolates. {ECO:0000269|PubMed:15155874,
CC ECO:0000269|PubMed:17189332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000269|PubMed:15155874, ECO:0000269|PubMed:17189332};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17189332};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17189332};
CC -!- ACTIVITY REGULATION: Feedback inhibition by Leu.
CC {ECO:0000269|PubMed:17189332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=279 uM for 2-oxoisovalerate {ECO:0000269|PubMed:17189332};
CC KM=16 uM for acetyl-CoA {ECO:0000269|PubMed:17189332};
CC Vmax=2200 umol/min/g enzyme with 2-oxoisovalerate as substrate
CC {ECO:0000269|PubMed:17189332};
CC Vmax=1800 umol/min/g enzyme with acetyl-CoA as substrate
CC {ECO:0000269|PubMed:17189332};
CC Note=kcat is 2.3 sec(-1) with 2-oxoisovalerate as substrate
CC (PubMed:17189332). kcat is 1.9 sec(-1) with acetyl-CoA as substrate
CC (PubMed:17189332). {ECO:0000269|PubMed:17189332};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17189332};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000269|PubMed:15155874,
CC ECO:0000269|PubMed:17189332}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:17189332}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:12432038, ECO:0000269|PubMed:17189332}.
CC -!- DISRUPTION PHENOTYPE: Plants do not show any changes in soluble amino
CC acid content. {ECO:0000269|PubMed:17189332}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43169.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF327647; AAG52882.1; -; mRNA.
DR EMBL; AC016662; AAG52530.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35540.1; -; Genomic_DNA.
DR EMBL; AY057659; AAL15290.1; -; mRNA.
DR EMBL; BT000815; AAN33190.1; -; mRNA.
DR EMBL; AK118569; BAC43169.1; ALT_FRAME; mRNA.
DR PIR; C96768; C96768.
DR RefSeq; NP_177544.1; NM_106063.3.
DR AlphaFoldDB; Q9C550; -.
DR SMR; Q9C550; -.
DR BioGRID; 28961; 4.
DR STRING; 3702.AT1G74040.1; -.
DR iPTMnet; Q9C550; -.
DR PaxDb; Q9C550; -.
DR PRIDE; Q9C550; -.
DR ProteomicsDB; 250740; -.
DR EnsemblPlants; AT1G74040.1; AT1G74040.1; AT1G74040.
DR GeneID; 843742; -.
DR Gramene; AT1G74040.1; AT1G74040.1; AT1G74040.
DR KEGG; ath:AT1G74040; -.
DR Araport; AT1G74040; -.
DR TAIR; locus:2031586; AT1G74040.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_022158_0_1_1; -.
DR InParanoid; Q9C550; -.
DR OrthoDB; 928619at2759; -.
DR PhylomeDB; Q9C550; -.
DR BRENDA; 2.3.3.13; 399.
DR UniPathway; UPA00048; UER00070.
DR PRO; PR:Q9C550; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C550; baseline and differential.
DR Genevisible; Q9C550; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IDA:TAIR.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IDA:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_01025; LeuA_type1; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Leucine biosynthesis; Lyase; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..631
FT /note="2-isopropylmalate synthase 2, chloroplastic"
FT /id="PRO_0000315840"
FT DOMAIN 87..360
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT CONFLICT 213
FT /note="R -> K (in Ref. 5; BAC43169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 68136 MW; 3499333687B8AE77 CRC64;
MESSILKSPN LSSPSFGVPS IPALSSSSTS PFSSLHLRSQ NHRTISLTTA GKFRVSYSLS
ASSPLPPHAP RRRPNYIPNR ISDPNYVRIF DTTLRDGEQS PGATLTSKEK LDIARQLAKL
GVDIIEAGFP AASKDDFEAV KTIAETVGNT VDENGYVPVI CGLSRCNKKD IETAWEAVKY
AKRPRIHTFI ATSDIHLKYK LKKSKEEVIE IARNMVRFAR SLGCEDVEFS PEDAGRSERE
YLYEILGEVI KAGATTLNIP DTVGITLPSE FGQLIADIKA NTPGIQNVII STHCQNDLGL
STANTLSGAH SGARQVEVTI NGIGERAGNA SLEEVVMAIK CRGDHVLGGL FTGIDTRHIV
MTSKMVEEYT GMQTQPHKAI VGANAFAHES GIHQDGMLKH KGTYEIMSPE EIGLERSNDA
GIVLGKLSGR HALKDRLNEL GYVLDDGQLS NLFWRFKAVA EQKKRVTDAD LIALVSDEVF
QPEAVWKLLD MQITCGTLGL STSTVKLADS DGKEHVACSV GTGPVDAAYK AVDLIVKEPA
TLLEYSMNAV TEGIDAIATT RVLIRGDNNY SSTNAVTGES VERTFSGTGA GMDIVVSSVK
AYVGALNKML GFKEHTSTLS KTPLETNEVP A
