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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: -Experimental evidence at protein leveli

Functioni

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

Miscellaneous

Present with 7400 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei626PROSITE-ProRule annotation1

GO - Molecular functioni

  • glutamate dehydrogenase (NAD+) activity Source: SGD

GO - Biological processi

  • glutamate catabolic process to 2-oxoglutarate Source: InterPro
  • nitrogen compound metabolic process Source: SGD

Keywordsi

Molecular functionOxidoreductase
LigandNAD

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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL215C
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001827331 – 1092NAD-specific glutamate dehydrogenaseAdd BLAST1092

Post-translational modificationi

Phosphorylated by a complex containing the NNK1 kinase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33327
PaxDbiP33327
PRIDEiP33327

PTM databases

iPTMnetiP33327

Interactioni

Subunit structurei

Homotetramer. Interacts with NNK1.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi31830, 144 interactors
DIPiDIP-1689N
IntActiP33327, 31 interactors
MINTiP33327
STRINGi4932.YDL215C

Structurei

3D structure databases

ProteinModelPortaliP33327
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000162582
InParanoidiP33327
KOiK15371
OMAiRCYFVYQ
OrthoDBiEOG092C0EFB

Family and domain databases

InterProiView protein in InterPro
IPR033524 Glu/Leu/Phe/Val_DH_AS
IPR006096 Glu/Leu/Phe/Val_DH_C
IPR036291 NAD(P)-bd_dom_sf
IPR016210 NAD-GDH_euk
PfamiView protein in Pfam
PF00208 ELFV_dehydrog, 1 hit
PIRSFiPIRSF000184 GDH_NAD, 1 hit
SMARTiView protein in SMART
SM00839 ELFV_dehydrog, 1 hit
SUPFAMiSSF51735 SSF51735, 2 hits
PROSITEiView protein in PROSITE
PS00074 GLFV_DEHYDROGENASE, 1 hit

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:February 1, 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

Similar proteinsi

Entry informationi

Entry nameiDHE2_YEAST
AccessioniPrimary (citable) accession number: P33327
Secondary accession number(s): D6VRD9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 28, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health