Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-isopropylmalate synthase 2, mitochondrial

Gene

LEU9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA.

Pathwayi

GO - Molecular functioni

  • 2-isopropylmalate synthase activity Source: SGD

GO - Biological processi

  • leucine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-59.
UniPathwayiUPA00048; UER00070.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LEU9
Ordered Locus Names:YOR108W
ORF Names:YOR3227w
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR108w.
EuPathDBiFungiDB:YOR108W.
SGDiS000005634. LEU9.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050MitochondrionSequence AnalysisAdd
BLAST
Chaini51 – 6045542-isopropylmalate synthase 2, mitochondrialPRO_0000255958Add
BLAST

Proteomic databases

MaxQBiQ12166.
PaxDbiQ12166.
PeptideAtlasiQ12166.

Expressioni

Gene expression databases

GenevestigatoriQ12166.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LEU4P062083EBI-37359,EBI-10116

Protein-protein interaction databases

BioGridi34504. 60 interactions.
DIPiDIP-4153N.
IntActiQ12166. 4 interactions.
MINTiMINT-562265.
STRINGi4932.YOR108W.

Structurei

3D structure databases

ProteinModelPortaliQ12166.
SMRiQ12166. Positions 34-592.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0119.
GeneTreeiENSGT00390000018527.
HOGENOMiHOG000110941.
InParanoidiQ12166.
KOiK01649.
OMAiETEWNLE.
OrthoDBiEOG73NGC6.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00572. LeuA_type2.
InterProiIPR013709. 2-isopropylmalate_synth_dimer.
IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR005668. IPM_Synthase.
IPR000891. PYR_CT.
[Graphical view]
PfamiPF00682. HMGL-like. 1 hit.
PF08502. LeuA_dimer. 1 hit.
[Graphical view]
SMARTiSM00917. LeuA_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF110921. SSF110921. 1 hit.
TIGRFAMsiTIGR00970. leuA_yeast. 1 hit.
PROSITEiPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12166-1 [UniParc]FASTAAdd to basket

« Hide

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

LLAE
Length:604
Mass (Da):67,200
Last modified:November 1, 1996 - v1
Checksum:i0E5B049FFBB6097E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64028.1.
Z75016 Genomic DNA. Translation: CAA99306.1.
BK006948 Genomic DNA. Translation: DAA10883.1.
PIRiS66993.
RefSeqiNP_014751.1. NM_001183527.1.

Genome annotation databases

EnsemblFungiiYOR108W; YOR108W; YOR108W.
GeneIDi854275.
KEGGisce:YOR108W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64028.1.
Z75016 Genomic DNA. Translation: CAA99306.1.
BK006948 Genomic DNA. Translation: DAA10883.1.
PIRiS66993.
RefSeqiNP_014751.1. NM_001183527.1.

3D structure databases

ProteinModelPortaliQ12166.
SMRiQ12166. Positions 34-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34504. 60 interactions.
DIPiDIP-4153N.
IntActiQ12166. 4 interactions.
MINTiMINT-562265.
STRINGi4932.YOR108W.

Proteomic databases

MaxQBiQ12166.
PaxDbiQ12166.
PeptideAtlasiQ12166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR108W; YOR108W; YOR108W.
GeneIDi854275.
KEGGisce:YOR108W.

Organism-specific databases

CYGDiYOR108w.
EuPathDBiFungiDB:YOR108W.
SGDiS000005634. LEU9.

Phylogenomic databases

eggNOGiCOG0119.
GeneTreeiENSGT00390000018527.
HOGENOMiHOG000110941.
InParanoidiQ12166.
KOiK01649.
OMAiETEWNLE.
OrthoDBiEOG73NGC6.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00070.
BioCyciYEAST:MONOMER3O-59.

Miscellaneous databases

NextBioi976233.
PROiQ12166.

Gene expression databases

GenevestigatoriQ12166.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00572. LeuA_type2.
InterProiIPR013709. 2-isopropylmalate_synth_dimer.
IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR005668. IPM_Synthase.
IPR000891. PYR_CT.
[Graphical view]
PfamiPF00682. HMGL-like. 1 hit.
PF08502. LeuA_dimer. 1 hit.
[Graphical view]
SMARTiSM00917. LeuA_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF110921. SSF110921. 1 hit.
TIGRFAMsiTIGR00970. leuA_yeast. 1 hit.
PROSITEiPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLEU9_YEAST
AccessioniPrimary (citable) accession number: Q12166
Secondary accession number(s): D6W2G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 28800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.