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P33327

- DHE2_YEAST

UniProt

P33327 - DHE2_YEAST

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Protein
NAD-specific glutamate dehydrogenase
Gene
GDH2, YDL215C, D0892
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei626 – 6261 By similarity

GO - Molecular functioni

  1. glutamate dehydrogenase (NAD+) activity Source: SGD
  2. protein binding Source: IntAct

GO - Biological processi

  1. glutamate catabolic process to 2-oxoglutarate Source: InterPro
  2. nitrogen compound metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:YDL215C-MONOMER.
YEAST:YDL215C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-specific glutamate dehydrogenase (EC:1.4.1.2)
Short name:
NAD-GDH
Gene namesi
Name:GDH2
Ordered Locus Names:YDL215C
ORF Names:D0892
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL215c.
SGDiS000002374. GDH2.

Pathology & Biotechi

Disruption phenotypei

Leads to rapamycin resistance when grown on glutamate as the sole nitrogen source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10921092NAD-specific glutamate dehydrogenase
PRO_0000182733Add
BLAST

Post-translational modificationi

Phosphorylated by a complex containing the NNK1 kinase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33327.
PaxDbiP33327.
PeptideAtlasiP33327.

Expressioni

Gene expression databases

GenevestigatoriP33327.

Interactioni

Subunit structurei

Homotetramer. Interacts with NNK1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NNK1P360033EBI-5815,EBI-9796

Protein-protein interaction databases

BioGridi31830. 96 interactions.
DIPiDIP-1689N.
IntActiP33327. 17 interactions.
MINTiMINT-390019.
STRINGi4932.YDL215C.

Structurei

3D structure databases

ProteinModelPortaliP33327.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2902.
HOGENOMiHOG000162582.
KOiK15371.
OMAiAPPIEHS.
OrthoDBiEOG780RVR.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR028971. NAD-GDH.
IPR016210. NAD-GDH_euk.
[Graphical view]
PfamiPF05088. Bac_GDH. 1 hit.
PF00208. ELFV_dehydrog. 1 hit.
[Graphical view]
PIRSFiPIRSF000184. GDH_NAD. 1 hit.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33327-1 [UniParc]FASTAAdd to Basket

« Hide

MLFDNKNRGA LNSLNTPDIA SLSISSMSDY HVFDFPGKDL QREEVIDLLD     50
QQGFIPDDLI EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF 100
FAKSKFNGIQ PRLFSIKNKI ITNDNHAIFM ESNTGVSISD SQQKNFKFAS 150
DAVGNDTLEH GKDTIKKNRI EMDDSCPPYE LDSEIDDLFL DNKSQKNCRL 200
VSFWAPESEL KLTFVYESVY PNDDPAGVDI SSQDLLKGDI ESISDKTMYK 250
VSSNENKKLY GLLLKLVKER EGPVIKTTRS VENKDEIRLL VAYKRFTTKR 300
YYSALNSLFH YYKLKPSKFY LESFNVKDDD IIIFSVYLNE NQQLEDVLLH 350
DVEAALKQVE REASLLYAIP NNSFHEVYQR RQFSPKEAIY AHIGAIFINH 400
FVNRLGSDYQ NLLSQITIKR NDTTLLEIVE NLKRKLRNET LTQQTIINIM 450
SKHYTIISKL YKNFAQIHYY HNSTKDMEKT LSFQRLEKVE PFKNDQEFEA 500
YLNKFIPNDS PDLLILKTLN IFNKSILKTN FFITRKVAIS FRLDPSLVMT 550
KFEYPETPYG IFFVVGNTFK GFHIRFRDIA RGGIRIVCSR NQDIYDLNSK 600
NVIDENYQLA STQQRKNKDI PEGGSKGVIL LNPGLVEHDQ TFVAFSQYVD 650
AMIDILINDP LKENYVNLLP KEEILFFGPD EGTAGFVDWA TNHARVRNCP 700
WWKSFLTGKS PSLGGIPHDE YGMTSLGVRA YVNKIYETLN LTNSTVYKFQ 750
TGGPDGDLGS NEILLSSPNE CYLAILDGSG VLCDPKGLDK DELCRLAHER 800
KMISDFDTSK LSNNGFFVSV DAMDIMLPNG TIVANGTTFR NTFHTQIFKF 850
VDHVDIFVPC GGRPNSITLN NLHYFVDEKT GKCKIPYIVE GANLFITQPA 900
KNALEEHGCI LFKDASANKG GVTSSSMEVL ASLALNDNDF VHKFIGDVSG 950
ERSALYKSYV VEVQSRIQKN AELEFGQLWN LNQLNGTHIS EISNQLSFTI 1000
NKLNDDLVAS QELWLNDLKL RNYLLLDKII PKILIDVAGP QSVLENIPES 1050
YLKVLLSSYL SSTFVYQNGI DVNIGKFLEF IGGLKREAEA SA 1092
Length:1,092
Mass (Da):124,332
Last modified:February 1, 1994 - v1
Checksum:iDF8358D831E4545F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS37676.
RefSeqiNP_010066.1. NM_001180275.1.

Genome annotation databases

EnsemblFungiiYDL215C; YDL215C; YDL215C.
GeneIDi851311.
KEGGisce:YDL215C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S37676.
RefSeqi NP_010066.1. NM_001180275.1.

3D structure databases

ProteinModelPortali P33327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31830. 96 interactions.
DIPi DIP-1689N.
IntActi P33327. 17 interactions.
MINTi MINT-390019.
STRINGi 4932.YDL215C.

Proteomic databases

MaxQBi P33327.
PaxDbi P33327.
PeptideAtlasi P33327.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL215C ; YDL215C ; YDL215C .
GeneIDi 851311.
KEGGi sce:YDL215C.

Organism-specific databases

CYGDi YDL215c.
SGDi S000002374. GDH2.

Phylogenomic databases

eggNOGi COG2902.
HOGENOMi HOG000162582.
KOi K15371.
OMAi APPIEHS.
OrthoDBi EOG780RVR.

Enzyme and pathway databases

BioCyci MetaCyc:YDL215C-MONOMER.
YEAST:YDL215C-MONOMER.

Miscellaneous databases

NextBioi 968334.

Gene expression databases

Genevestigatori P33327.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR028971. NAD-GDH.
IPR016210. NAD-GDH_euk.
[Graphical view ]
Pfami PF05088. Bac_GDH. 1 hit.
PF00208. ELFV_dehydrog. 1 hit.
[Graphical view ]
PIRSFi PIRSF000184. GDH_NAD. 1 hit.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: INTERACTION WITH NNK1, DISRUPTION PHENOTYPE, PHOSPHORYLATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDHE2_YEAST
AccessioniPrimary (citable) accession number: P33327
Secondary accession number(s): D6VRD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi