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Reviewed, UniProtKB/Swiss-Prot P40495 (LYS12_YEAST)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Homoisocitrate dehydrogenase, mitochondrial
    EC=1.1.1.87
Gene names
Name: LYS12
Synonyms: LYS10, LYS11
Ordered Locus Names: YIL094C
ORF Names: YI9910.02C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the NAD+-dependent conversion of homoisocitrate to alpha-ketoadipate. Ref.3

Catalytic activity

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH. Ref.3

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Enzyme regulation

Activity is repressed 4-fold by lysine. Ref.5

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/4.

Subcellular location

Mitochondrion. Ref.7 Ref.9

Miscellaneous

Present with 19079 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Biophysicochemical properties

Kinetic parameters:

The KM for homoisocitrate is lower than 10 µM.

KM=1.5 mM for 2-oxoadipate

KM=330 µM for NAD+

KM=65 µM for NADH

pH dependence:

Optimum pH is 8.3-8.8 for the forward reaction, and 7 for the reverse reaction.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 371349Homoisocitrate dehydrogenase, mitochondrial
PRO_0000043097

Sites

Metal binding2431Magnesium or manganese By similarity
Metal binding2671Magnesium or manganese By similarity
Metal binding2711Magnesium or manganese By similarity
Binding site1141Substrate By similarity
Binding site1241Substrate By similarity
Binding site1431Substrate By similarity
Binding site2431Substrate By similarity
Site1501Critical for catalysis By similarity
Site2061Critical for catalysis By similarity

Amino acid modifications

Modified residue981Phosphoserine Ref.10
Modified residue1071Phosphoserine Ref.10
Modified residue1081Phosphoserine Ref.10
Modified residue1461Phosphothreonine Ref.10
Modified residue2111Phosphoserine Ref.10

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Sequences

Sequence LengthMass (Da)Tools
P40495-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 43CAFA86F75ED3C6

FASTA37140,069
        10         20         30         40         50         60 
MFRSVATRLS ACRGLASNAA RKSLTIGLIP GDGIGKEVIP AGKQVLENLN SKHGLSFNFI 

        70         80         90        100        110        120 
DLYAGFQTFQ ETGKALPDET VKVLKEQCQG ALFGAVQSPT TKVEGYSSPI VALRREMGLF 

       130        140        150        160        170        180 
ANVRPVKSVE GEKGKPIDMV IVRENTEDLY IKIEKTYIDK ATGTRVADAT KRISEIATRR 

       190        200        210        220        230        240 
IATIALDIAL KRLQTRGQAT LTVTHKSNVL SQSDGLFREI CKEVYESNKD KYGQIKYNEQ 

       250        260        270        280        290        300 
IVDSMVYRLF REPQCFDVIV APNLYGDILS DGAAALVGSL GVVPSANVGP EIVIGEPCHG 

       310        320        330        340        350        360 
SAPDIAGKGI ANPIATIRST ALMLEFLGHN EAAQDIYKAV DANLREGSIK TPDLGGKAST 

       370 
QQVVDDVLSR L

« Hide

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References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed: 9169870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Bienvenut W.V., Peters C.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 23-36; 103-114; 116-127; 181-192; 237-248; 309-318 AND 346-370, MASS SPECTROMETRY.
[3]"Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid."
Strassman M., Ceci L.N.
J. Biol. Chem. 240:4357-4361(1965) [PubMed: 4284830] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[4]"Homoisocitric dehydrogenase from yeast."
Rowley B., Tucci A.F.
Arch. Biochem. Biophys. 141:499-510(1970) [PubMed: 4395693] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]"General and specific controls of lysine biosynthesis in Saccharomyces cerevisiae."
Urrestarazu L.A., Borell C.W., Bhattacharjee J.K.
Curr. Genet. 9:341-344(1985) [PubMed: 3939712] [Abstract]
Cited for: ENZYME REGULATION.
[6]"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 BY MASS SPECTROMETRY.
[7]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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].
[9]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]"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 SER-98; SER-107; SER-108; THR-146 AND SER-211, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

Z46728 Genomic DNA. Translation: CAA86700.1.
PIRS49786.
RefSeqNP_012172.1.

3D structure databases

HSSPHSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4162N.
IntActP40495. 98 interactions.

Proteomic databases

PeptideAtlasP40495.
PRIDEP40495.

Genome annotation databases

EnsemblYIL094C. Saccharomyces cerevisiae. [Contig view]
GeneID854714.
GenomeReviewsGene locus YIL094C in contig Z47047_GR.
KEGGsce:YIL094C.
NMPDRfig|4932.3.peg.1699.

Organism-specific databases

CYGDYIL094c.
SGDS000001356. LYS12.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP40495.
OMAP40495. VEGYSSP.

Enzyme and pathway databases

BRENDA1.1.1.87. 250.

Gene expression databases

GermOnlineYIL094C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP40495.
NextBio977383.

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Entry information

Entry nameLYS12_YEAST
AccessionPrimary (citable) accession number: P40495
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents