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P31116 (DHOM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Homoserine dehydrogenase

Short name=HDH
EC=1.1.1.3
Gene names
Name:HOM6
Ordered Locus Names:YJR139C
ORF Names:J2132
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.

Subunit structure

Homodimer.

Miscellaneous

Present with 48900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the homoserine dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Homoserine dehydrogenase
PRO_0000066707

Regions

Nucleotide binding11 – 188NADP

Sites

Active site2231Proton donor Potential
Binding site931NADP
Binding site1171NADP
Binding site2081Substrate

Experimental info

Mutagenesis1171K → A: Loss of activity.
Mutagenesis2081E → D: Increases KM for aspartate-semialdehyde 48-fold and reduces Kcat by 50%. Ref.9
Mutagenesis2081E → L or Q: Loss of activity. Ref.9
Mutagenesis2191D → L: Reduces Kcat 150-fold. Ref.9
Mutagenesis2231K → V: Loss of activity. Ref.9
Sequence conflict1341K → L AA sequence Ref.4
Sequence conflict1521Missing AA sequence Ref.4
Sequence conflict3271R → V AA sequence Ref.4
Sequence conflict3331Missing AA sequence Ref.4

Secondary structure

.............................................................. 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31116 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 6C106F9EB0BD0CC5

FASTA35938,502
        10         20         30         40         50         60 
MSTKVVNVAV IGAGVVGSAF LDQLLAMKST ITYNLVLLAE AERSLISKDF SPLNVGSDWK 

        70         80         90        100        110        120 
AALAASTTKT LPLDDLIAHL KTSPKPVILV DNTSSAYIAG FYTKFVENGI SIATPNKKAF 

       130        140        150        160        170        180 
SSDLATWKAL FSNKPTNGFV YHEATVGAGL PIISFLREII QTGDEVEKIE GIFSGTLSYI 

       190        200        210        220        230        240 
FNEFSTSQAN DVKFSDVVKV AKKLGYTEPD PRDDLNGLDV ARKVTIVGRI SGVEVESPTS 

       250        260        270        280        290        300 
FPVQSLIPKP LESVKSADEF LEKLSDYDKD LTQLKKEAAT ENKVLRFIGK VDVATKSVSV 

       310        320        330        340        350 
GIEKYDYSHP FASLKGSDNV ISIKTKRYTN PVVIQGAGAG AAVTAAGVLG DVIKIAQRL 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases."
Thomas D., Barbey R., Surdin-Kerjan Y.
FEBS Lett. 323:289-293(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26786 / X2180-1A.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Rapid purification and characterization of homoserine dehydrogenase from Saccharomyces cerevisiae."
Yumoto N., Kawata Y., Noda S., Tokushige M.
Arch. Biochem. Biophys. 285:270-275(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 129-158 AND 327-354.
[5]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases."
DeLaBarre B., Thompson P.R., Wright G.D., Berghuis A.M.
Nat. Struct. Biol. 7:238-244(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-359 IN COMPLEX WITH NAD AND SUBSTRATE, MUTAGENESIS OF GLU-208; ASP-219 AND LYS-223.
[10]"Enzyme-assisted suicide: molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase."
Jacques S.L., Mirza I.A., Ejim L., Koteva K., Hughes D.W., Green K., Kinach R., Honek J.F., Lai H.K., Berghuis A.M., Wright G.D.
Chem. Biol. 10:989-995(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[11]"New phenolic inhibitors of yeast homoserine dehydrogenase."
Ejim L., Mirza I.A., Capone C., Nazi I., Jenkins S., Chee G.-L., Berghuis A.M., Wright G.D.
Bioorg. Med. Chem. 12:3825-3830(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITORS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64457 Genomic DNA. Translation: CAA45787.1.
Z49639 Genomic DNA. Translation: CAA89671.1.
BK006943 Genomic DNA. Translation: DAA08924.1.
PIRS33317.
RefSeqNP_012673.3. NM_001181797.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EBFX-ray2.30A/B2-359[»]
1EBUX-ray2.60A/B/C/D2-359[»]
1Q7GX-ray2.60A/B1-359[»]
1TVEX-ray3.00A/B2-359[»]
ProteinModelPortalP31116.
SMRP31116. Positions 2-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33895. 269 interactions.
DIPDIP-6315N.
IntActP31116. 6 interactions.
MINTMINT-2731902.

Proteomic databases

PaxDbP31116.
PeptideAtlasP31116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR139C; YJR139C; YJR139C.
GeneID853604.
KEGGsce:YJR139C.

Organism-specific databases

CYGDYJR139c.
SGDS000003900. HOM6.

Phylogenomic databases

eggNOGCOG0460.
HOGENOMHOG000024037.
KOK00003.
OMAMVNIGIV.
OrthoDBEOG7BGHWP.

Enzyme and pathway databases

BioCycYEAST:YJR139C-MONOMER.
UniPathwayUPA00050; UER00063.
UPA00051; UER00465.

Gene expression databases

ArrayExpressP31116.
GenevestigatorP31116.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR005106. Asp/hSer_DH_NAD-bd.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR022697. HDH_short.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF036497. HDH_short. 1 hit.
PROSITEPS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP31116.
NextBio974436.

Entry information

Entry nameDHOM_YEAST
AccessionPrimary (citable) accession number: P31116
Secondary accession number(s): D6VWV8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways