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Protein

Ketol-acid reductoisomerase, mitochondrial

Gene

ILV5

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

Functioni

Catalytic activityi

(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711Sequence analysis
Metal bindingi255 – 2551Magnesium 1By similarity
Metal bindingi255 – 2551Magnesium 2By similarity
Metal bindingi259 – 2591Magnesium 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi84 – 9310NADPSequence analysis
Nucleotide bindingi108 – 1136NADPBy similarity
Nucleotide bindingi146 – 1505NADPBy similarity

GO - Molecular functioni

  • double-stranded DNA binding Source: SGD
  • ketol-acid reductoisomerase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: SGD
  • isoleucine biosynthetic process Source: UniProtKB-UniPathway
  • mitochondrial genome maintenance Source: SGD
  • valine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, NADP

Enzyme and pathway databases

BioCyciYEAST:YLR355C-MONOMER.
UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase, mitochondrial (EC:1.1.1.86)
Alternative name(s):
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacyl reductoisomerase
Gene namesi
Name:ILV5
Ordered Locus Names:YLR355C
ORF Names:L9638.7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR355C.
SGDiS000004347. ILV5.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial nucleoid Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747MitochondrionSequence analysisAdd
BLAST
Chaini48 – 395348Ketol-acid reductoisomerase, mitochondrialPRO_0000015634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei355 – 3551PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06168.
PeptideAtlasiP06168.
PRIDEiP06168.
TopDownProteomicsiP06168.

2D gel databases

SWISS-2DPAGEP06168.

PTM databases

iPTMnetiP06168.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ILV1P009272EBI-9082,EBI-19200

Protein-protein interaction databases

BioGridi31617. 45 interactions.
DIPiDIP-6463N.
IntActiP06168. 10 interactions.
MINTiMINT-674895.

Structurei

3D structure databases

ProteinModelPortaliP06168.
SMRiP06168. Positions 72-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni363 – 39533HydrophilicAdd
BLAST

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000016231.
InParanoidiP06168.
KOiK00053.
OMAiSSYAVWN.
OrthoDBiEOG7VHT6S.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016207. KetolA_reductoisomerase_fun.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFiPIRSF000119. Ilv5_fungal. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P06168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTQAARLI CNSRVITAKR TFALATRAAA YSRPAARFVK PMITTRGLKQ
60 70 80 90 100
INFGGTVETV YERADWPREK LLDYFKNDTF ALIGYGSQGY GQGLNLRDNG
110 120 130 140 150
LNVIIGVRKD GASWKAAIED GWVPGKNLFT VEDAIKRGSY VMNLLSDAAQ
160 170 180 190 200
SETWPAIKPL LTKGKTLYFS HGFSPVFKDL THVEPPKDLD VILVAPKGSG
210 220 230 240 250
RTVRSLFKEG RGINSSYAVW NDVTGKAHEK AQALAVAIGS GYVYQTTFER
260 270 280 290 300
EVNSDLYGER GCLMGGIHGM FLAQYDVLRE NGHSPSEAFN ETVEEATQSL
310 320 330 340 350
YPLIGKYGMD YMYDACSTTA RRGALDWYPI FKNALKPVFQ DLYESTKNGT
360 370 380 390
ETKRSLEFNS QPDYREKLEK ELDTIRNMEI WKVGKEVRKL RPENQ
Length:395
Mass (Da):44,368
Last modified:January 1, 1988 - v1
Checksum:iD76419A6AD68E85E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04969 Genomic DNA. Translation: CAA28643.1.
U19102 Genomic DNA. Translation: AAB67753.1.
BK006945 Genomic DNA. Translation: DAA09659.1.
PIRiA24709.
RefSeqiNP_013459.1. NM_001182244.1.

Genome annotation databases

EnsemblFungiiYLR355C; YLR355C; YLR355C.
GeneIDi851069.
KEGGisce:YLR355C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04969 Genomic DNA. Translation: CAA28643.1.
U19102 Genomic DNA. Translation: AAB67753.1.
BK006945 Genomic DNA. Translation: DAA09659.1.
PIRiA24709.
RefSeqiNP_013459.1. NM_001182244.1.

3D structure databases

ProteinModelPortaliP06168.
SMRiP06168. Positions 72-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31617. 45 interactions.
DIPiDIP-6463N.
IntActiP06168. 10 interactions.
MINTiMINT-674895.

PTM databases

iPTMnetiP06168.

2D gel databases

SWISS-2DPAGEP06168.

Proteomic databases

MaxQBiP06168.
PeptideAtlasiP06168.
PRIDEiP06168.
TopDownProteomicsiP06168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR355C; YLR355C; YLR355C.
GeneIDi851069.
KEGGisce:YLR355C.

Organism-specific databases

EuPathDBiFungiDB:YLR355C.
SGDiS000004347. ILV5.

Phylogenomic databases

HOGENOMiHOG000016231.
InParanoidiP06168.
KOiK00053.
OMAiSSYAVWN.
OrthoDBiEOG7VHT6S.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BioCyciYEAST:YLR355C-MONOMER.

Miscellaneous databases

NextBioi967711.
PROiP06168.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016207. KetolA_reductoisomerase_fun.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFiPIRSF000119. Ilv5_fungal. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ILV5 gene of Saccharomyces cerevisiae is highly expressed."
    Petersen J.G.L., Holmberg S.
    Nucleic Acids Res. 14:9631-9651(1986) [PubMed] [Europe PMC] [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.
    , 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] [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. 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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE N-TERMINUS.
  6. 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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiILV5_YEAST
AccessioniPrimary (citable) accession number: P06168
Secondary accession number(s): D6VYZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 162 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 883000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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 one 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.