Q12166 (LEU9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-isopropylmalate synthase 2, mitochondrial
EC=2.3.3.13

Alternative name(s):
Alpha-IPM synthase 2
Alpha-isopropylmalate synthase 2
Alpha-isopropylmalate synthase II

Gene names

Name:	LEU9
Ordered Locus Names:	YOR108W
ORF Names:	YOR3227w

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Redundant to LEU4, responsible of about 20% of alpha-IPMS activity. Involved in leucine synthesis. Ref.4
Catalytic activity	Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA.
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular location	Mitochondrion Ref.5.
Miscellaneous	Present with 28800 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	leucine biosynthetic process Inferred from genetic interaction Ref.4. Source: SGD
Cellular_component	mitochondrion Inferred from direct assay PubMed 11158296PubMed 16823961. Source: SGD
Molecular_function	2-isopropylmalate synthase activity Inferred from direct assay PubMed 11158296. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LEU4	P06208	3	EBI-37359,EBI-10116

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 50	50	Mitochondrion Potential
	Chain	51 – 604	554	2-isopropylmalate synthase 2, mitochondrial		PRO_0000255958

Sequences

	Sequence		Length	Mass (Da)
	Q12166 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0E5B049FFBB6097E	FASTA	604	67,200
	10 20 30 40 50 60 MVKHSFIALA EHASKLRRSI PPVKLTYKNM LRDPSVKYRA FAPPKMVKRI WPDKTIQKAP 70 80 90 100 110 120 RWLSTDLRDG NQSLPDPMSV AQKKEYFHKL INIGFKEIEV SFPSASQTDF DFTRYAVENA 130 140 150 160 170 180 PDDVGIQCLV QSREHLIKRT VEALTGAKRA TIHTYLATSD MFREIVFNMS REEAISKAVE 190 200 210 220 230 240 ATKLVRKLTK DDPSQQATRW SYEFSPECFS DTPGEFAVEI CEAVKKAWEP TEENPIIFNL 250 260 270 280 290 300 PATVEVASPN VYADQIEYFS THITEREKVC ISTHCHNDRG CGVAATELGM LAGADRVEGC 310 320 330 340 350 360 LFGNGERTGN VDLVTVAMNM YTQGVSPNLD FSDLTSISEI VHRCNKIPIP PRAPYGGELV 370 380 390 400 410 420 VSAFSGSHQD AIKKGFAIQN KKQAQGETRW RIPYLPLDPK DIGRDYEAVI RVNSQSGKGG 430 440 450 460 470 480 AAWVIMRSLG LDVPRPMQVD FSNTLQKNAD ALGRELKSEE ITKLFKETYN YNNNEHIYVT 490 500 510 520 530 540 LLNYEVKKLN PERRALVGQV EINDKVVNIE GYGNGPISSL VDALSNLLNV KLSVQNYSEH 550 560 570 580 590 600 SLGSGSATQA ASFINLSYIK DINNHATSNM WGVGVSEDTG DASIKAVFAT VNNIIHSGDV LLAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequencing and analysis of 130 kb from yeast chromosome XV." Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W. Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Identification by functional analysis of the gene encoding alpha-isopropylmalate synthase II (LEU9) in Saccharomyces cerevisiae." Casalone E., Barberio C., Cavalieri D., Polsinelli M. Yeast 16:539-545(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94335 Genomic DNA. Translation: CAA64028.1. Z75016 Genomic DNA. Translation: CAA99306.1. BK006948 Genomic DNA. Translation: DAA10883.1.
PIR	S66993.
RefSeq	NP_014751.1. NM_001183527.1.
3D structure databases
HSSP	HSSP built from PDB template 1SR9 based on UniProtKB P96420.
ProteinModelPortal	Q12166.
SMR	Q12166. Positions 34-592.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4153N.
IntAct	Q12166. 4 interactions.
MINT	MINT-562265.
STRING	4932.YOR108W.
Proteomic databases
PaxDb	Q12166.
PeptideAtlas	Q12166.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR108W; YOR108W; YOR108W.
GeneID	854275.
KEGG	sce:YOR108W.
Organism-specific databases
CYGD	YOR108w.
SGD	S000005634. LEU9.
Phylogenomic databases
eggNOG	COG0119.
GeneTree	ENSGT00390000018527.
HOGENOM	HOG000110941.
OMA	FSTHITE.
OrthoDB	EOG4VDT6P.
Enzyme and pathway databases
UniPathway	UPA00048; UER00070.
Gene expression databases
Genevestigator	Q12166.
GermOnline	YOR108W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013709. 2-isopropylmalate_synth_dimer. IPR002034. AIPM/Hcit_synth_CS. IPR013785. Aldolase_TIM. IPR005668. IPM_Synthase. IPR000891. PYR_CT. [Graphical view]
Pfam	PF00682. HMGL-like. 1 hit. PF08502. LeuA_dimer. 1 hit. [Graphical view]
SMART	SM00917. LeuA_dimer. 1 hit. [Graphical view]
SUPFAM	SSF110921. 2-isopropylmalate_synth_dimer. 1 hit.
TIGRFAMs	TIGR00970. leuA_yeast. 1 hit.
PROSITE	PS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit. PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit. PS50991. PYR_CT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976233.

Entry information

Entry name

LEU9_YEAST

Accession

Primary (citable) accession number: Q12166
Secondary accession number(s): D6W2G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program