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P33327 (DHE2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1092 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NAD+-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.

Catalytic activity

L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.

Subunit structure

Homotetramer. Interacts with NNK1. Ref.8

Post-translational modification

Phosphorylated by a complex containing the NNK1 kinase. Ref.8

Disruption phenotype

Leads to rapamycin resistance when grown on glutamate as the sole nitrogen source. Ref.8

Miscellaneous

Present with 7400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NNK1P360033EBI-5815,EBI-9796

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10921092NAD-specific glutamate dehydrogenase
PRO_0000182733

Sites

Active site6261 By similarity

Sequences

Sequence LengthMass (Da)Tools
P33327 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: DF8358D831E4545F

FASTA1,092124,332
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [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]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
[5]Rasmussen S.W.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 848-1092.
[6]"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].
[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]"A global protein kinase and phosphatase interaction network in yeast."
Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B., Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D., Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C., Nesvizhskii A.I., Tyers M.
Science 328:1043-1046(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NNK1, DISRUPTION PHENOTYPE, PHOSPHORYLATION.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S66436 Genomic DNA. Translation: AAB20327.1.
X99000 Genomic DNA. Translation: CAA67475.1.
Z74263 Genomic DNA. Translation: CAA98793.1.
X72015 Genomic DNA. Translation: CAA50894.1.
BK006938 Genomic DNA. Translation: DAA11649.1.
PIRS37676.
RefSeqNP_010066.1. NM_001180275.1.

3D structure databases

ProteinModelPortalP33327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31830. 96 interactions.
DIPDIP-1689N.
IntActP33327. 17 interactions.
MINTMINT-390019.
STRING4932.YDL215C.

Proteomic databases

PaxDbP33327.
PeptideAtlasP33327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL215C; YDL215C; YDL215C.
GeneID851311.
KEGGsce:YDL215C.

Organism-specific databases

CYGDYDL215c.
SGDS000002374. GDH2.

Phylogenomic databases

eggNOGCOG2902.
HOGENOMHOG000162582.
KOK15371.
OMAAPPIEHS.
OrthoDBEOG780RVR.

Enzyme and pathway databases

BioCycYEAST:YDL215C-MONOMER.

Gene expression databases

GenevestigatorP33327.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR016210. NAD-GDH_euk.
[Graphical view]
PfamPF00208. ELFV_dehydrog. 1 hit.
[Graphical view]
PIRSFPIRSF000184. GDH_NAD. 1 hit.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968334.

Entry information

Entry nameDHE2_YEAST
AccessionPrimary (citable) accession number: P33327
Secondary accession number(s): D6VRD9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 19, 2014
This is version 120 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 IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families