Skip Header

Contribute Send feedback
Read comments (?) or add your own

P06168 (ILV5_YEAST) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Mitochondrion Potential
Chain48 – 395348Ketol-acid reductoisomerase, mitochondrial
PRO_0000015634

Regions

Nucleotide binding84 – 9310NADP Potential
Nucleotide binding108 – 1136NADP By similarity
Nucleotide binding146 – 1505NADP By similarity
Region363 – 39533Hydrophilic

Sites

Active site1711 Potential
Metal binding2551Magnesium 1 By similarity
Metal binding2551Magnesium 2 By similarity
Metal binding2591Magnesium 1 By similarity

Amino acid modifications

Modified residue851Phosphotyrosine Ref.7
Modified residue3171Phosphoserine Ref.7
Modified residue3181Phosphothreonine Ref.7
Modified residue3551Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P06168 [UniParc].

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

FASTA39544,368
        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' 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. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., 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.
PIRA24709.
RefSeqNP_013459.1. NM_001182244.1.

3D structure databases

ProteinModelPortalP06168.
SMRP06168. Positions 39-395.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6463N.
IntActP06168. 13 interactions.
MINTMINT-674895.
STRINGP06168.

2D gel databases

SWISS-2DPAGEP06168.

Proteomic databases

PeptideAtlasP06168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR355C; YLR355C; YLR355C.
GeneID851069.
KEGGsce:YLR355C.
NMPDRfig|4932.3.peg.4481.

Organism-specific databases

CYGDYLR355c.
SGDS000004347. ILV5.

Phylogenomic databases

eggNOGfuNOG07507.
HOGENOMHBG286525.
OMAKTLYFSH.
OrthoDBEOG4DFSX2.

Gene expression databases

ArrayExpressP06168.
GenevestigatorP06168.
GermOnlineYLR355C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013023. AcH_isomrdctse.
IPR000506. AcH_isomrdctse_C.
IPR013328. DH_multihelical.
IPR013116. IlvN.
IPR016207. KetolA_reductoisomerase_fun.
[Graphical view]
Gene3DG3DSA:1.10.1040.10. Opine_DH. 1 hit.
KOK00053.
PANTHERPTHR21371. AcH_isomrdctse. 1 hit.
PTHR21371:SF3. PTHR21371:SF3. 1 hit.
PfamPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFPIRSF000119. Ilv5_fungal. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00465. IlvC. 1 hit.
ProtoNetSearch...

Other

NextBio967711.

Entry information

Entry nameILV5_YEAST
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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