LEU9_YEAST
ID LEU9_YEAST Reviewed; 604 AA.
AC Q12166; D6W2G7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=2-isopropylmalate synthase 2, mitochondrial;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase 2;
DE AltName: Full=Alpha-isopropylmalate synthase 2;
DE AltName: Full=Alpha-isopropylmalate synthase II;
DE Flags: Precursor;
GN Name=LEU9; OrderedLocusNames=YOR108W; ORFNames=YOR3227w;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=10790691;
RX DOI=10.1002/(sici)1097-0061(200004)16:6<539::aid-yea547>3.0.co;2-k;
RA Casalone E., Barberio C., Cavalieri D., Polsinelli M.;
RT "Identification by functional analysis of the gene encoding alpha-
RT isopropylmalate synthase II (LEU9) in Saccharomyces cerevisiae.";
RL Yeast 16:539-545(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
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). Redundant to LEU4,
CC responsible of about 20% of alpha-IPMS activity. Involved in leucine
CC synthesis. {ECO:0000269|PubMed:10790691}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- INTERACTION:
CC Q12166; P06208: LEU4; NbExp=3; IntAct=EBI-37359, EBI-10116;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 28800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000305}.
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DR EMBL; X94335; CAA64028.1; -; Genomic_DNA.
DR EMBL; Z75016; CAA99306.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10883.1; -; Genomic_DNA.
DR PIR; S66993; S66993.
DR RefSeq; NP_014751.1; NM_001183527.1.
DR AlphaFoldDB; Q12166; -.
DR SMR; Q12166; -.
DR BioGRID; 34504; 72.
DR DIP; DIP-4153N; -.
DR IntAct; Q12166; 5.
DR MINT; Q12166; -.
DR STRING; 4932.YOR108W; -.
DR iPTMnet; Q12166; -.
DR MaxQB; Q12166; -.
DR PaxDb; Q12166; -.
DR PRIDE; Q12166; -.
DR EnsemblFungi; YOR108W_mRNA; YOR108W; YOR108W.
DR GeneID; 854275; -.
DR KEGG; sce:YOR108W; -.
DR SGD; S000005634; LEU9.
DR VEuPathDB; FungiDB:YOR108W; -.
DR eggNOG; KOG2367; Eukaryota.
DR GeneTree; ENSGT00940000176815; -.
DR HOGENOM; CLU_004588_3_0_1; -.
DR InParanoid; Q12166; -.
DR OMA; WPDKVID; -.
DR BioCyc; YEAST:MON3O-59; -.
DR UniPathway; UPA00048; UER00070.
DR PRO; PR:Q12166; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12166; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IDA:SGD.
DR GO; GO:0009098; P:leucine biosynthetic process; IMP:SGD.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_00572; LeuA_type2; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
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; TIGR00970; leuA_yeast; 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 Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..604
FT /note="2-isopropylmalate synthase 2, mitochondrial"
FT /id="PRO_0000255958"
FT DOMAIN 60..335
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 604 AA; 67200 MW; 0E5B049FFBB6097E CRC64;
MVKHSFIALA EHASKLRRSI PPVKLTYKNM LRDPSVKYRA FAPPKMVKRI WPDKTIQKAP
RWLSTDLRDG NQSLPDPMSV AQKKEYFHKL INIGFKEIEV SFPSASQTDF DFTRYAVENA
PDDVGIQCLV QSREHLIKRT VEALTGAKRA TIHTYLATSD MFREIVFNMS REEAISKAVE
ATKLVRKLTK DDPSQQATRW SYEFSPECFS DTPGEFAVEI CEAVKKAWEP TEENPIIFNL
PATVEVASPN VYADQIEYFS THITEREKVC ISTHCHNDRG CGVAATELGM LAGADRVEGC
LFGNGERTGN VDLVTVAMNM YTQGVSPNLD FSDLTSISEI VHRCNKIPIP PRAPYGGELV
VSAFSGSHQD AIKKGFAIQN KKQAQGETRW RIPYLPLDPK DIGRDYEAVI RVNSQSGKGG
AAWVIMRSLG LDVPRPMQVD FSNTLQKNAD ALGRELKSEE ITKLFKETYN YNNNEHIYVT
LLNYEVKKLN PERRALVGQV EINDKVVNIE GYGNGPISSL VDALSNLLNV KLSVQNYSEH
SLGSGSATQA ASFINLSYIK DINNHATSNM WGVGVSEDTG DASIKAVFAT VNNIIHSGDV
LLAE
