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UniProtKB/Swiss-Prot entry P33327


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

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Entry information
Entry name DHE2_YEAST
Primary accession number P33327
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 69)
Name and origin of the protein
Protein name NAD-specific glutamate dehydrogenase
Synonyms NAD-GDH
EC 1.4.1.2
Gene name
Name: GDH2
OrderedLocusNames: YDL215C
ORFNames: D0892
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=EBY23;
PubMed=7901008 [NCBI, ExPASy, EBI, Israel, Japan]
Boles E., Lehnert W., Zimmermann F.K.;
"The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant.";
Eur. J. Biochem. 217:469-477(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
PubMed=1682801 [NCBI, ExPASy, EBI, Israel, Japan]
Miller S.M., Magasanik B.;
"Role of the complex upstream region of the GDH2 gene in nitrogen regulation of the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 11:6229-6247(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 848-1092.
Rasmussen S.W.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-28 AND SER-242, 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).
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
S66436; AAB20327.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X99000; CAA67475.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74263; CAA98793.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X72015; CAA50894.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S37676; S37676.
RefSeq NP_010066.1; -.
3D structure databases
ModBase P33327.
Protein-protein interaction databases
DIP DIP:1689N; -.
IntAct P33327; -.
Organism-specific databases
CYGD YDL215c; -.
SGD S000002374; GDH2.
Yeast-GFP YDL215C.
Gene expression databases
ArrayExpress P33327; -.
GermOnline YDL215C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0005625; Cellular component: soluble fraction (inferred from direct assay from SGD).
GO:0004352; Molecular function: glutamate dehydrogenase activity (inferred from mutant phenotype from SGD).
GO:0006807; Biological process: nitrogen compound metabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR016210; Glu_DHase_NAD-dep.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00208; ELFV_dehydrog; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000184; GDH_NAD; 1.
PROSITE PS00074; GLFV_DEHYDROGENASE; 1.
BLOCKS P33327.
Proteomic databases
PeptideAtlas P33327; -.
Genome annotation databases
Ensembl YDL215C; Saccharomyces cerevisiae. [Contig view]
GeneID 851311; -.
GenomeReviews Z71256_GR; YDL215C.
KEGG sce:YDL215C; -.
NMPDR fig|4932.3.peg.799; -.
Phylogenomic databases
HOGENOM P33327; -.
Other
LinkHub P33327; -.
ProtoNet P33327.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   1092  1092     NAD-specific glutamate dehydrogenase. PRO_0000182733
ACT_SITE   626    626        By similarity. 
MOD_RES   25     25        Phosphoserine. 
MOD_RES   28     28        Phosphoserine. 
MOD_RES   242    242        Phosphoserine. 
MOD_RES   482    482        Phosphoserine. 
Sequence information
Length: 1092 AA [This is the length of the unprocessed precursor] Molecular weight: 124332 Da [This is the MW of the unprocessed precursor] CRC64: DF8358D831E4545F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLFDNKNRGA LNSLNTPDIA SLSISSMSDY HVFDFPGKDL QREEVIDLLD QQGFIPDDLI 

        70         80         90        100        110        120 
EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF FAKSKFNGIQ PRLFSIKNKI 

       130        140        150        160        170        180 
ITNDNHAIFM ESNTGVSISD SQQKNFKFAS DAVGNDTLEH GKDTIKKNRI EMDDSCPPYE 

       190        200        210        220        230        240 
LDSEIDDLFL DNKSQKNCRL VSFWAPESEL KLTFVYESVY PNDDPAGVDI SSQDLLKGDI 

       250        260        270        280        290        300 
ESISDKTMYK VSSNENKKLY GLLLKLVKER EGPVIKTTRS VENKDEIRLL VAYKRFTTKR 

       310        320        330        340        350        360 
YYSALNSLFH YYKLKPSKFY LESFNVKDDD IIIFSVYLNE NQQLEDVLLH DVEAALKQVE 

       370        380        390        400        410        420 
REASLLYAIP NNSFHEVYQR RQFSPKEAIY AHIGAIFINH FVNRLGSDYQ NLLSQITIKR 

       430        440        450        460        470        480 
NDTTLLEIVE NLKRKLRNET LTQQTIINIM SKHYTIISKL YKNFAQIHYY HNSTKDMEKT 

       490        500        510        520        530        540 
LSFQRLEKVE PFKNDQEFEA YLNKFIPNDS PDLLILKTLN IFNKSILKTN FFITRKVAIS 

       550        560        570        580        590        600 
FRLDPSLVMT KFEYPETPYG IFFVVGNTFK GFHIRFRDIA RGGIRIVCSR NQDIYDLNSK 

       610        620        630        640        650        660 
NVIDENYQLA STQQRKNKDI PEGGSKGVIL LNPGLVEHDQ TFVAFSQYVD AMIDILINDP 

       670        680        690        700        710        720 
LKENYVNLLP KEEILFFGPD EGTAGFVDWA TNHARVRNCP WWKSFLTGKS PSLGGIPHDE 

       730        740        750        760        770        780 
YGMTSLGVRA YVNKIYETLN LTNSTVYKFQ TGGPDGDLGS NEILLSSPNE CYLAILDGSG 

       790        800        810        820        830        840 
VLCDPKGLDK DELCRLAHER KMISDFDTSK LSNNGFFVSV DAMDIMLPNG TIVANGTTFR 

       850        860        870        880        890        900 
NTFHTQIFKF VDHVDIFVPC GGRPNSITLN NLHYFVDEKT GKCKIPYIVE GANLFITQPA 

       910        920        930        940        950        960 
KNALEEHGCI LFKDASANKG GVTSSSMEVL ASLALNDNDF VHKFIGDVSG ERSALYKSYV 

       970        980        990       1000       1010       1020 
VEVQSRIQKN AELEFGQLWN LNQLNGTHIS EISNQLSFTI NKLNDDLVAS QELWLNDLKL 

      1030       1040       1050       1060       1070       1080 
RNYLLLDKII PKILIDVAGP QSVLENIPES YLKVLLSSYL SSTFVYQNGI DVNIGKFLEF 

      1090 
IGGLKREAEA SA 

P33327 in FASTA format

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