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P33327

- DHE2_YEAST

UniProt

P33327 - DHE2_YEAST

Protein

NAD-specific glutamate dehydrogenase

Gene

GDH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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 – 6261PROSITE-ProRule annotation

    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

    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 dehydrogenasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 124 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.1 Publication

    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