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UniProtKB/Swiss-Prot entry P31116


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHOM_YEAST
Primary accession number P31116
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    July 1, 2008 (Entry version 71)
Name and origin of the protein
Protein name Homoserine dehydrogenase
Synonyms EC 1.1.1.3
HDH
Gene name
Name: HOM6
OrderedLocusNames: YJR139C
ORFNames: J2132
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26786 / X2180-1A;
DOI=10.1016/0014-5793(93)81359-8; PubMed=8500624 [NCBI, ExPASy, EBI, Israel, Japan]
Thomas D., Barbey R., Surdin-Kerjan Y.;
"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases.";
FEBS Lett. 323:289-293(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[3]
PROTEIN SEQUENCE OF 129-158 AND 327-354.
DOI=10.1016/0003-9861(91)90359-Q; PubMed=1897932 [NCBI, ExPASy, EBI, Israel, Japan]
Yumoto N., Kawata Y., Noda S., Tokushige M.;
"Rapid purification and characterization of homoserine dehydrogenase from Saccharomyces cerevisiae.";
Arch. Biochem. Biophys. 285:270-275(1991).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-239, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-344, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 0:0-0(2008).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-359 IN COMPLEX WITH NAD AND SUBSTRATE, AND MUTAGENESIS OF GLU-208; ASP-219 AND LYS-223.
DOI=10.1038/73359; PubMed=10700284 [NCBI, ExPASy, EBI, Israel, Japan]
DeLaBarre B., Thompson P.R., Wright G.D., Berghuis A.M.;
"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.";
Nat. Struct. Biol. 7:238-244(2000).
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
DOI=10.1016/j.chembiol.2003.09.015; PubMed=14583265 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Enzyme-assisted suicide: molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase.";
Chem. Biol. 10:989-995(2003).
[9]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITORS.
DOI=10.1016/j.bmc.2004.05.009; PubMed=15210149 [NCBI, ExPASy, EBI, Israel, Japan]
Ejim L., Mirza I.A., Capone C., Nazi I., Jenkins S., Chee G.-L., Berghuis A.M., Wright G.D.;
"New phenolic inhibitors of yeast homoserine dehydrogenase.";
Bioorg. Med. Chem. 12:3825-3830(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X64457; CAA45787.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49639; CAA89671.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S33317; S33317.
RefSeq NP_012673.1; -.
3D structure databases
PDB
1EBF; X-ray; 2.30 A; A/B=2-359.[ExPASy / RCSB / EBI]
1EBU; X-ray; 2.60 A; A/B/C/D=2-359.[ExPASy / RCSB / EBI]
1Q7G; X-ray; 2.60 A; A/B=1-359.[ExPASy / RCSB / EBI]
1TVE; X-ray; 3.00 A; A/B=2-359.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EBF; -.
1EBU; -.
1Q7G; -.
1TVE; -.
ModBase P31116.
Protein-protein interaction databases
DIP DIP:6315N; -.
IntAct P31116; -.
Organism-specific databases
CYGD YJR139c; -.
SGD S000003900; HOM6.
Yeast-GFP YJR139C.
Gene expression databases
GermOnline YJR139C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0004412; Molecular function: homoserine dehydrogenase activity (inferred from direct assay from SGD).
GO:0006555; Biological process: methionine metabolic process (traceable author statement from SGD).
GO:0042493; Biological process: response to drug (inferred from mutant phenotype from SGD).
GO:0006566; Biological process: threonine metabolic process (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR005106; Asp/hSer_DHase_NAD-bd.
IPR001342; hSer_DHase_cat.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00742; Homoserine_dh; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.
PROSITE PS01042; HOMOSER_DHGENASE; 1.
BLOCKS P31116.
Proteomic databases
PeptideAtlas P31116; -.
Genome annotation databases
Ensembl YJR139C; Saccharomyces cerevisiae. [Contig view]
GeneID 853604; -.
GenomeReviews Y13136_GR; YJR139C.
KEGG sce:YJR139C; -.
NMPDR fig|4932.3.peg.3649; -.
Phylogenomic databases
HOGENOM P31116; -.
Other
LinkHub P31116; -.
ProtoNet P31116.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Direct protein sequencing; Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase; Phosphoprotein; Threonine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   359  359     Homoserine dehydrogenase. PRO_0000066707
NP_BIND   11    18  8     NADP. 
ACT_SITE   223   223        Proton donor (Potential). 
BINDING   93    93        NADP. 
BINDING   117   117        NADP. 
BINDING   208   208        Substrate. 
MOD_RES   237   237        Phosphoserine. 
MOD_RES   239   239        Phosphothreonine. 
MOD_RES   344   344        Phosphothreonine. 
MUTAGEN   117   117        K->A: Loss of activity. 
MUTAGEN   208   208        E->D: Increases Km for aspartate-semialdehyde 48-fold and reduces Kcat by 50%. 
MUTAGEN   208   208        E->L,Q: Loss of activity. 
MUTAGEN   219   219        D->L: Reduces Kcat 150-fold. 
MUTAGEN   223   223        K->V: Loss of activity. 
CONFLICT   134   134        K -> L (in Ref. 3; AA sequence). 
CONFLICT   152   152        Missing (in Ref. 3; AA sequence). 
CONFLICT   327   327        R -> V (in Ref. 3; AA sequence). 
CONFLICT   333   333        Missing (in Ref. 3; AA sequence). 
STRAND   4    11  8      
HELIX   15    26  12      
STRAND   30    39  10      
STRAND   41    46  6      
HELIX   59    64  6      
HELIX   73    80  8      
STRAND   87    91  5      
HELIX   96    99  4      
HELIX   102   107  6      
STRAND   111   113  3      
HELIX   118   120  3      
HELIX   124   130  7      
HELIX   143   145  3      
TURN   146   149  4      
HELIX   153   162  10      
STRAND   166   172  7      
HELIX   175   184  10      
HELIX   194   204  11      
HELIX   212   215  4      
HELIX   218   230  13      
HELIX   249   251  3      
HELIX   258   264  7      
HELIX   265   267  3      
HELIX   268   278  11      
TURN   279   282  4      
STRAND   283   292  10      
TURN   293   296  4      
STRAND   297   309  13      
HELIX   310   313  4      
STRAND   319   327  9      
STRAND   332   336  5      
HELIX   341   358  18      
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 38502 Da [This is the MW of the unprocessed precursor] CRC64: 6C106F9EB0BD0CC5 [This is a checksum on the sequence]
        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 

P31116 in FASTA format

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