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Protein

NAD-specific glutamate dehydrogenase

Gene

GDH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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 – 6261PROSITE-ProRule annotation

GO - Molecular functioni

  1. glutamate dehydrogenase (NAD+) activity Source: SGD

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 Componenti: 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. 97 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.
InParanoidiP33327.
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

        10         20         30         40         50
MLFDNKNRGA LNSLNTPDIA SLSISSMSDY HVFDFPGKDL QREEVIDLLD
60 70 80 90 100
QQGFIPDDLI EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF
110 120 130 140 150
FAKSKFNGIQ PRLFSIKNKI ITNDNHAIFM ESNTGVSISD SQQKNFKFAS
160 170 180 190 200
DAVGNDTLEH GKDTIKKNRI EMDDSCPPYE LDSEIDDLFL DNKSQKNCRL
210 220 230 240 250
VSFWAPESEL KLTFVYESVY PNDDPAGVDI SSQDLLKGDI ESISDKTMYK
260 270 280 290 300
VSSNENKKLY GLLLKLVKER EGPVIKTTRS VENKDEIRLL VAYKRFTTKR
310 320 330 340 350
YYSALNSLFH YYKLKPSKFY LESFNVKDDD IIIFSVYLNE NQQLEDVLLH
360 370 380 390 400
DVEAALKQVE REASLLYAIP NNSFHEVYQR RQFSPKEAIY AHIGAIFINH
410 420 430 440 450
FVNRLGSDYQ NLLSQITIKR NDTTLLEIVE NLKRKLRNET LTQQTIINIM
460 470 480 490 500
SKHYTIISKL YKNFAQIHYY HNSTKDMEKT LSFQRLEKVE PFKNDQEFEA
510 520 530 540 550
YLNKFIPNDS PDLLILKTLN IFNKSILKTN FFITRKVAIS FRLDPSLVMT
560 570 580 590 600
KFEYPETPYG IFFVVGNTFK GFHIRFRDIA RGGIRIVCSR NQDIYDLNSK
610 620 630 640 650
NVIDENYQLA STQQRKNKDI PEGGSKGVIL LNPGLVEHDQ TFVAFSQYVD
660 670 680 690 700
AMIDILINDP LKENYVNLLP KEEILFFGPD EGTAGFVDWA TNHARVRNCP
710 720 730 740 750
WWKSFLTGKS PSLGGIPHDE YGMTSLGVRA YVNKIYETLN LTNSTVYKFQ
760 770 780 790 800
TGGPDGDLGS NEILLSSPNE CYLAILDGSG VLCDPKGLDK DELCRLAHER
810 820 830 840 850
KMISDFDTSK LSNNGFFVSV DAMDIMLPNG TIVANGTTFR NTFHTQIFKF
860 870 880 890 900
VDHVDIFVPC GGRPNSITLN NLHYFVDEKT GKCKIPYIVE GANLFITQPA
910 920 930 940 950
KNALEEHGCI LFKDASANKG GVTSSSMEVL ASLALNDNDF VHKFIGDVSG
960 970 980 990 1000
ERSALYKSYV VEVQSRIQKN AELEFGQLWN LNQLNGTHIS EISNQLSFTI
1010 1020 1030 1040 1050
NKLNDDLVAS QELWLNDLKL RNYLLLDKII PKILIDVAGP QSVLENIPES
1060 1070 1080 1090
YLKVLLSSYL SSTFVYQNGI DVNIGKFLEF IGGLKREAEA SA
Length:1,092
Mass (Da):124,332
Last modified:January 31, 1994 - v1
Checksum:iDF8358D831E4545F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP33327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31830. 97 interactions.
DIPiDIP-1689N.
IntActiP33327. 17 interactions.
MINTiMINT-390019.
STRINGi4932.YDL215C.

Proteomic databases

MaxQBiP33327.
PaxDbiP33327.
PeptideAtlasiP33327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYDL215c.
SGDiS000002374. GDH2.

Phylogenomic databases

eggNOGiCOG2902.
HOGENOMiHOG000162582.
InParanoidiP33327.
KOiK15371.
OMAiAPPIEHS.
OrthoDBiEOG780RVR.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi968334.

Gene expression databases

GenevestigatoriP33327.

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]
ProtoNetiSearch...

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(1992) [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(1996) [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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
  5. Rasmussen S.W.
    Submitted (JUN-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(2007) [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: January 31, 1994
Last sequence update: January 31, 1994
Last modified: January 6, 2015
This is version 126 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.