Ketol-acid reductoisomerase, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P06168 (ILV5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ketol-acid reductoisomerase, mitochondrial
EC=1.1.1.86

Alternative name(s):
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacil reductoisomerase

Gene names

Name:	ILV5
Ordered Locus Names:	YLR355C
ORF Names:	L9638.7

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	395 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)

Catalytic activity	(R)-2,3-dihydroxy-3-methylbutanoate + NADP⁺ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP⁺ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
Subcellular location	Mitochondrion.
Miscellaneous	Present with 883000 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the ketol-acid reductoisomerase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from mutant phenotype. Source: SGD mitochondrial genome maintenance Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial nucleoid Inferred from direct assay. Source: SGD
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Inferred from direct assay. Source: SGD ketol-acid reductoisomerase activity Inferred from mutant phenotype Ref.1. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 47

Mitochondrion Potential

Chain

48 – 395

348

Ketol-acid reductoisomerase, mitochondrial

PRO_0000015634

Regions

Nucleotide binding

84 – 93

NADP Potential

Nucleotide binding

108 – 113

NADP By similarity

Nucleotide binding

146 – 150

NADP By similarity

Region

363 – 395

Hydrophilic

Sites

Active site

171

Potential

Metal binding

255

Magnesium 1 By similarity

Metal binding

255

Magnesium 2 By similarity

Metal binding

259

Magnesium 1 By similarity

Amino acid modifications

Modified residue

Phosphotyrosine Ref.7

Modified residue

317

Phosphoserine Ref.7

Modified residue

318

Phosphothreonine Ref.7

Modified residue

355

Phosphoserine Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P06168 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: D76419A6AD68E85E
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FASTA

395

44,368

        10         20         30         40         50         60 
MLRTQAARLI CNSRVITAKR TFALATRAAA YSRPAARFVK PMITTRGLKQ INFGGTVETV 

        70         80         90        100        110        120 
YERADWPREK LLDYFKNDTF ALIGYGSQGY GQGLNLRDNG LNVIIGVRKD GASWKAAIED 

       130        140        150        160        170        180 
GWVPGKNLFT VEDAIKRGSY VMNLLSDAAQ SETWPAIKPL LTKGKTLYFS HGFSPVFKDL 

       190        200        210        220        230        240 
THVEPPKDLD VILVAPKGSG RTVRSLFKEG RGINSSYAVW NDVTGKAHEK AQALAVAIGS 

       250        260        270        280        290        300 
GYVYQTTFER EVNSDLYGER GCLMGGIHGM FLAQYDVLRE NGHSPSEAFN ETVEEATQSL 

       310        320        330        340        350        360 
YPLIGKYGMD YMYDACSTTA RRGALDWYPI FKNALKPVFQ DLYESTKNGT ETKRSLEFNS 

       370        380        390 
QPDYREKLEK ELDTIRNMEI WKVGKEVRKL RPENQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ILV5 gene of Saccharomyces cerevisiae is highly expressed." Petersen J.G.L., Holmberg S. Nucleic Acids Res. 14:9631-9651(1986) [PubMed: 3027658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 166-174. Strain: ATCC 204508 / S288c.
[5]	"Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels." Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M. Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed: 8962070] [Abstract] Cited for: IDENTIFICATION OF PROBABLE N-TERMINUS.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85; SER-317; THR-318 AND SER-355, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04969 Genomic DNA. Translation: CAA28643.1. U19102 Genomic DNA. Translation: AAB67753.1. BK006945 Genomic DNA. Translation: DAA09659.1.
PIR	A24709.
RefSeq	NP_013459.1. NM_001182244.1.
3D structure databases
ProteinModelPortal	P06168.
SMR	P06168. Positions 39-395.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6463N.
IntAct	P06168. 13 interactions.
MINT	MINT-674895.
STRING	P06168.
2D gel databases
SWISS-2DPAGE	P06168.
Proteomic databases
PeptideAtlas	P06168.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR355C; YLR355C; YLR355C.
GeneID	851069.
KEGG	sce:YLR355C.
NMPDR	fig\|4932.3.peg.4481.
Organism-specific databases
CYGD	YLR355c.
SGD	S000004347. ILV5.
Phylogenomic databases
eggNOG	fuNOG07507.
HOGENOM	HBG286525.
OMA	KTLYFSH.
OrthoDB	EOG4DFSX2.
Gene expression databases
ArrayExpress	P06168.
Genevestigator	P06168.
GermOnline	YLR355C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013023. AcH_isomrdctse. IPR000506. AcH_isomrdctse_C. IPR013328. DH_multihelical. IPR013116. IlvN. IPR016207. KetolA_reductoisomerase_fun. [Graphical view]
Gene3D	G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KO	K00053.
PANTHER	PTHR21371. AcH_isomrdctse. 1 hit. PTHR21371:SF3. PTHR21371:SF3. 1 hit.
Pfam	PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view]
PIRSF	PIRSF000119. Ilv5_fungal. 1 hit.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00465. IlvC. 1 hit.
ProtoNet	Search...
Other
NextBio	967711.

Entry information

Entry name

ILV5_YEAST

Accession

Primary (citable) accession number: P06168
Secondary accession number(s): D6VYZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	December 14, 2011
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents