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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (By similarity). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.By similarity1 Publication

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

Enzyme regulationi

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei147SubstrateBy similarity1
Binding sitei171SubstrateBy similarity1
Binding sitei176NADBy similarity1
Active sitei1831
Binding sitei252NADBy similarity1
Binding sitei266GTPBy similarity1
Binding sitei270GTPBy similarity1
Binding sitei319GTPBy similarity1
Binding sitei322GTPBy similarity1
Binding sitei438SubstrateBy similarity1
Binding sitei444NADBy similarity1
Binding sitei450ADPBy similarity1
Binding sitei516ADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi141 – 143NADBy similarity3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: RGD
  • glutamate dehydrogenase (NAD+) activity Source: RGD
  • glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • cerebellum development Source: RGD
  • glutamate catabolic process Source: RGD
  • glutamine metabolic process Source: UniProtKB
  • long-term memory Source: RGD
  • positive regulation of insulin secretion Source: Ensembl
  • response to aluminum ion Source: RGD
  • tricarboxylic acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

ATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.4.1.3. 5301.
ReactomeiR-RNO-70614. Amino acid synthesis and interconversion (transamination).
SABIO-RKP10860.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Alternative name(s):
Memory-related gene 2 protein
Short name:
MRG-2
Gene namesi
Name:Glud1
Synonyms:Glud
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi2708. Glud1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176833.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53MitochondrionBy similarityAdd BLAST53
ChainiPRO_000000721354 – 558Glutamate dehydrogenase 1, mitochondrialAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei79PhosphoserineCombined sources1
Modified residuei84N6-acetyllysine; alternateBy similarity1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei90N6-acetyllysineBy similarity1
Modified residuei110N6-acetyllysine; alternateBy similarity1
Modified residuei110N6-succinyllysine; alternateBy similarity1
Modified residuei128PhosphoserineCombined sources1
Modified residuei135PhosphotyrosineBy similarity1
Modified residuei162N6-acetyllysine; alternateBy similarity1
Modified residuei162N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei172ADP-ribosylcysteineBy similarity1
Modified residuei183N6-acetyllysine; alternateBy similarity1
Modified residuei183N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei200N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1
Modified residuei227PhosphoserineBy similarity1
Modified residuei326N6-acetyllysineBy similarity1
Modified residuei346N6-acetyllysine; alternateBy similarity1
Modified residuei346N6-succinyllysine; alternateBy similarity1
Modified residuei352N6-acetyllysine; alternateBy similarity1
Modified residuei352N6-succinyllysine; alternateBy similarity1
Modified residuei363N6-acetyllysine; alternateBy similarity1
Modified residuei363N6-succinyllysine; alternateBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Modified residuei410PhosphothreonineCombined sources1
Modified residuei415N6-acetyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysine; alternateBy similarity1
Modified residuei457N6-acetyllysine; alternateBy similarity1
Modified residuei457N6-malonyllysine; alternateBy similarity1
Modified residuei457N6-succinyllysine; alternateBy similarity1
Modified residuei477N6-acetyllysine; alternateBy similarity1
Modified residuei477N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysine; alternateBy similarity1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei503N6-acetyllysine; alternateBy similarity1
Modified residuei503N6-malonyllysine; alternateBy similarity1
Modified residuei503N6-succinyllysine; alternateBy similarity1
Modified residuei512PhosphotyrosineBy similarity1
Modified residuei527N6-acetyllysine; alternateBy similarity1
Modified residuei527N6-malonyllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateBy similarity1
Modified residuei545N6-acetyllysine; alternateBy similarity1
Modified residuei545N6-succinyllysine; alternateBy similarity1
Modified residuei548N6-acetyllysineBy similarity1

Post-translational modificationi

ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer (By similarity).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

PaxDbiP10860.
PRIDEiP10860.

2D gel databases

World-2DPAGE0004:P10860.

PTM databases

iPTMnetiP10860.
PhosphoSitePlusiP10860.

Expressioni

Tissue specificityi

Widely expressed throughout the hippocampus. After induction by training, highly expressed in the dentate gyrus, pyrimidal layer and lacunosum molecolare.1 Publication

Inductioni

By water maze training in the hippocampus and in other regions of the brain including the laterodorsal nucleus of the thalamus and the cingulate cortex.1 Publication

Gene expression databases

BgeeiENSRNOG00000010222.
GenevisibleiP10860. RN.

Interactioni

Subunit structurei

Homohexamer.

GO - Molecular functioni

  • enzyme binding Source: RGD

Protein-protein interaction databases

BioGridi246566. 1 interactor.
IntActiP10860. 4 interactors.
MINTiMINT-2793533.
STRINGi10116.ENSRNOP00000013789.

Structurei

3D structure databases

ProteinModelPortaliP10860.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2250. Eukaryota.
COG0334. LUCA.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP10860.
KOiK00261.
OMAiYMSMIGT.
OrthoDBiEOG091G0KMT.
PhylomeDBiP10860.
TreeFamiTF313945.

Family and domain databases

CDDicd01076. NAD_bind_1_Glu_DH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
IPR033922. NAD_bind_Glu_DH.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR
60 70 80 90 100
RHYSEAATDR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGLG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY

NEAGVTFT
Length:558
Mass (Da):61,416
Last modified:April 4, 2006 - v2
Checksum:i388B8B5490C10F31
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56 – 57AA → GP in CAA32441 (PubMed:2704625).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14223 mRNA. Translation: CAA32441.1.
X14044 mRNA. Translation: CAA32202.1.
BC081841 mRNA. Translation: AAH81841.1.
X64365 Genomic DNA. Translation: CAA45717.1.
U95148 mRNA. Translation: AAB70012.1.
PIRiS03707.
RefSeqiNP_036702.1. NM_012570.2.
UniGeneiRn.55106.

Genome annotation databases

EnsembliENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367.
GeneIDi24399.
KEGGirno:24399.
UCSCiRGD:2708. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14223 mRNA. Translation: CAA32441.1.
X14044 mRNA. Translation: CAA32202.1.
BC081841 mRNA. Translation: AAH81841.1.
X64365 Genomic DNA. Translation: CAA45717.1.
U95148 mRNA. Translation: AAB70012.1.
PIRiS03707.
RefSeqiNP_036702.1. NM_012570.2.
UniGeneiRn.55106.

3D structure databases

ProteinModelPortaliP10860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246566. 1 interactor.
IntActiP10860. 4 interactors.
MINTiMINT-2793533.
STRINGi10116.ENSRNOP00000013789.

Chemistry databases

ChEMBLiCHEMBL2176833.

PTM databases

iPTMnetiP10860.
PhosphoSitePlusiP10860.

2D gel databases

World-2DPAGE0004:P10860.

Proteomic databases

PaxDbiP10860.
PRIDEiP10860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367.
GeneIDi24399.
KEGGirno:24399.
UCSCiRGD:2708. rat.

Organism-specific databases

CTDi2746.
RGDi2708. Glud1.

Phylogenomic databases

eggNOGiKOG2250. Eukaryota.
COG0334. LUCA.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP10860.
KOiK00261.
OMAiYMSMIGT.
OrthoDBiEOG091G0KMT.
PhylomeDBiP10860.
TreeFamiTF313945.

Enzyme and pathway databases

BRENDAi1.4.1.3. 5301.
ReactomeiR-RNO-70614. Amino acid synthesis and interconversion (transamination).
SABIO-RKP10860.

Miscellaneous databases

PROiP10860.

Gene expression databases

BgeeiENSRNOG00000010222.
GenevisibleiP10860. RN.

Family and domain databases

CDDicd01076. NAD_bind_1_Glu_DH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
IPR033922. NAD_bind_Glu_DH.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHE3_RAT
AccessioniPrimary (citable) accession number: P10860
Secondary accession number(s): Q66HI8, Q6LC16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 4, 2006
Last modified: November 30, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.