Reviewed, UniProtKB/Swiss-Prot P33327 (DHE2_YEAST)

Names and origin

Protein names

Recommended name:
    NAD-specific glutamate dehydrogenase
      Short name=NAD-GDH
    EC=1.4.1.2

Gene names

Name:	GDH2
Ordered Locus Names:	YDL215C
ORF Names:	D0892

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1092 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.
Subunit structure	Homotetramer.
Miscellaneous	Present with 7400 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate catabolic process to 2-oxoglutarate Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: SGD
Molecular function	glutamate dehydrogenase activity Inferred from mutant phenotype. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-5815,EBI-5815
ARO8	P53090	1	EBI-5815,EBI-2042933
CYS4	P32582	1	EBI-5815,EBI-4167
DNM1	P54861	1	EBI-5815,EBI-6002
GLN1	P32288	1	EBI-5815,EBI-7665
PEX11	Q12462	1	EBI-5815,EBI-13198
RNR1	P21524	1	EBI-5815,EBI-15234
RNR2	P09938	1	EBI-5815,EBI-15240
VMA4	P22203	1	EBI-5815,EBI-20268

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1092	1092	NAD-specific glutamate dehydrogenase		PRO_0000182733
Sites
	Active site	626	1	By similarity
Amino acid modifications
	Modified residue	25	1	Phosphoserine Ref.7
	Modified residue	28	1	Phosphoserine Ref.7
	Modified residue	242	1	Phosphoserine Ref.7
	Modified residue	482	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P33327-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: DF8358D831E4545F	FASTA	1,092	124,332
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant." Boles E., Lehnert W., Zimmermann F.K. Eur. J. Biochem. 217:469-477(1993) [PubMed: 7901008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EBY23.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." 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. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Role of the complex upstream region of the GDH2 gene in nitrogen regulation of the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae." Miller S.M., Magasanik B. Mol. Cell. Biol. 11:6229-6247(1991) [PubMed: 1682801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
[4]	Rasmussen S.W. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 848-1092.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-28 AND SER-242, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S66436 Genomic DNA. Translation: AAB20327.1. X99000 Genomic DNA. Translation: CAA67475.1. Z74263 Genomic DNA. Translation: CAA98793.1. X72015 Genomic DNA. Translation: CAA50894.1.
PIR	S37676.
RefSeq	NP_010066.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1689N.
IntAct	P33327. 28 interactions.
Proteomic databases
PeptideAtlas	P33327.
PRIDE	P33327.
Genome annotation databases
Ensembl	YDL215C. Saccharomyces cerevisiae. [Contig view]
GeneID	851311.
GenomeReviews	Gene locus YDL215C in contig Z71256_GR.
KEGG	sce:YDL215C.
NMPDR	fig|4932.3.peg.799.
Organism-specific databases
CYGD	YDL215c.
SGD	S000002374. GDH2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P33327.
OMA	P33327. VANGTTF.
Enzyme and pathway databases
BRENDA	1.4.1.2. 250.
Gene expression databases
ArrayExpress	P33327.
GermOnline	YDL215C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR016210. Glu_DH_NAD-dep. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. [Graphical view]
PIRSF	PIRSF000184. GDH_NAD. 1 hit.
PROSITE	PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968334.

Entry information

Entry name

DHE2_YEAST

Accession

Primary (citable) accession number: P33327

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)