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Protein

NADP-specific glutamate dehydrogenase 1

Gene

GDH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 20330NADBy similarityAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. ammonia assimilation cycle Source: SGD
  2. glutamate biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11504.
YEAST:YOR375C-MONOMER.
ReactomeiREACT_245457. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-specific glutamate dehydrogenase 1 (EC:1.4.1.4)
Short name:
NADP-GDH 1
Alternative name(s):
NADP-dependent glutamate dehydrogenase 1
Gene namesi
Name:GDH1
Synonyms:URE1
Ordered Locus Names:YOR375C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR375c.
SGDiS000005902. GDH1.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 454453NADP-specific glutamate dehydrogenase 1PRO_0000182798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Cross-linki325 – 325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki371 – 371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP07262.
PaxDbiP07262.
PeptideAtlasiP07262.
PRIDEiP07262.

Expressioni

Gene expression databases

GenevestigatoriP07262.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi34758. 49 interactions.
DIPiDIP-1329N.
IntActiP07262. 36 interactions.
MINTiMINT-390545.
STRINGi4932.YOR375C.

Structurei

3D structure databases

ProteinModelPortaliP07262.
SMRiP07262. Positions 3-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243799.
InParanoidiP07262.
KOiK00262.
OMAiIACTRIL.
OrthoDBiEOG7XSTPW.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07262-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEPEFQQAY EEVVSSLEDS TLFEQHPEYR KVLPIVSVPE RIIQFRVTWE
60 70 80 90 100
NDKGEQEVAQ GYRVQYNSAK GPYKGGLRFH PSVNLSILKF LGFEQIFKNS
110 120 130 140 150
LTGLDMGGGK GGLCVDLKGR SNNEIRRICY AFMRELSRHI GQDTDVPAGD
160 170 180 190 200
IGVGGREIGY LFGAYRSYKN SWEGVLTGKG LNWGGSLIRP EATGYGLVYY
210 220 230 240 250
TQAMIDYATN GKESFEGKRV TISGSGNVAQ YAALKVIELG GTVVSLSDSK
260 270 280 290 300
GCIISETGIT SEQVADISSA KVNFKSLEQI VNEYSTFSEN KVQYIAGARP
310 320 330 340 350
WTHVQKVDIA LPCATQNEVS GEEAKALVAQ GVKFIAEGSN MGSTPEAIAV
360 370 380 390 400
FETARSTATG PSEAVWYGPP KAANLGGVAV SGLEMAQNSQ RITWTSERVD
410 420 430 440 450
QELKRIMINC FNECIDYAKK YTKDGKVLPS LVKGANIASF IKVSDAMFDQ

GDVF
Length:454
Mass (Da):49,570
Last modified:November 1, 1997 - v2
Checksum:i707F921B6FE5B5B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831V → G in AAB03898. (PubMed:2989290)Curated
Sequence conflicti198 – 1981V → L in AAB03898. (PubMed:2989290)Curated
Sequence conflicti255 – 2551S → L in AAB03898. (PubMed:2989290)Curated
Sequence conflicti266 – 2661D → V in AAB03898. (PubMed:2989290)Curated
Sequence conflicti358 – 3647ATGPSEA → PLDQAT in AAA34642. (PubMed:2932370)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11297 Genomic DNA. Translation: AAB03898.1.
M10590 Genomic DNA. Translation: AAA34642.1.
Z75283 Genomic DNA. Translation: CAA99706.1.
BK006948 Genomic DNA. Translation: DAA11134.1.
PIRiS67287. A25275.
RefSeqiNP_015020.3. NM_001183795.3.

Genome annotation databases

EnsemblFungiiYOR375C; YOR375C; YOR375C.
GeneIDi854557.
KEGGisce:YOR375C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11297 Genomic DNA. Translation: AAB03898.1.
M10590 Genomic DNA. Translation: AAA34642.1.
Z75283 Genomic DNA. Translation: CAA99706.1.
BK006948 Genomic DNA. Translation: DAA11134.1.
PIRiS67287. A25275.
RefSeqiNP_015020.3. NM_001183795.3.

3D structure databases

ProteinModelPortaliP07262.
SMRiP07262. Positions 3-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34758. 49 interactions.
DIPiDIP-1329N.
IntActiP07262. 36 interactions.
MINTiMINT-390545.
STRINGi4932.YOR375C.

Proteomic databases

MaxQBiP07262.
PaxDbiP07262.
PeptideAtlasiP07262.
PRIDEiP07262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR375C; YOR375C; YOR375C.
GeneIDi854557.
KEGGisce:YOR375C.

Organism-specific databases

CYGDiYOR375c.
SGDiS000005902. GDH1.

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243799.
InParanoidiP07262.
KOiK00262.
OMAiIACTRIL.
OrthoDBiEOG7XSTPW.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11504.
YEAST:YOR375C-MONOMER.
ReactomeiREACT_245457. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi976988.

Gene expression databases

GenevestigatoriP07262.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase."
    Moye W.S., Amuro N., Rao J.K.M., Zalkin H.
    J. Biol. Chem. 260:8502-8508(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the GDH gene coding for the NADP-specific glutamate dehydrogenase of Saccharomyces cerevisiae."
    Nagasu T., Hall B.D.
    Gene 37:247-253(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
    Norbeck J., Blomberg A.
    FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 79-88; 157-165 AND 236-246.
    Strain: ATCC 38531 / Y41.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-325 AND LYS-371.
    Strain: SUB592.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDHE4_YEAST
AccessioniPrimary (citable) accession number: P07262
Secondary accession number(s): D6W368, Q08899
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 77500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.