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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.1 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 sitei183PROSITE-ProRule annotation1
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

GO - Biological processi

  • cerebellum development Source: Ensembl
  • glutamate biosynthetic process Source: MGI
  • glutamate catabolic process Source: MGI
  • glutamine metabolic process Source: UniProtKB
  • long-term memory Source: Ensembl
  • positive regulation of insulin secretion Source: MGI
  • response to aluminum ion Source: Ensembl
  • tricarboxylic acid metabolic process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
LigandATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.4.1.3 3474
ReactomeiR-MMU-2151201 Transcriptional activation of mitochondrial biogenesis
R-MMU-70614 Amino acid synthesis and interconversion (transamination)

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Gene namesi
Name:Glud1
Synonyms:Glud
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:95753 Glud1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53MitochondrionAdd BLAST53
ChainiPRO_000000721254 – 558Glutamate dehydrogenase 1, mitochondrialAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-succinyllysineCombined sources1
Modified residuei79PhosphoserineCombined sources1
Modified residuei84N6-acetyllysine; alternateCombined sources1
Modified residuei84N6-succinyllysine; alternateCombined sources1
Modified residuei90N6-acetyllysineCombined sources1
Modified residuei110N6-acetyllysine; alternateCombined sources1
Modified residuei110N6-succinyllysine; alternateBy similarity1
Modified residuei128PhosphoserineCombined sources1
Modified residuei135PhosphotyrosineCombined sources1
Modified residuei162N6-acetyllysine; alternateCombined sources1
Modified residuei162N6-succinyllysine; alternateCombined sources1
Modified residuei171N6-acetyllysineCombined sources1
Modified residuei172ADP-ribosylcysteineBy similarity1
Modified residuei183N6-acetyllysine; alternateBy similarity1
Modified residuei183N6-succinyllysine; alternateCombined sources1
Modified residuei187N6-acetyllysineCombined sources1
Modified residuei191N6-acetyllysine; alternateCombined sources1
Modified residuei191N6-succinyllysine; alternateCombined sources1
Modified residuei200N6-succinyllysineCombined sources1
Modified residuei211N6-acetyllysineCombined sources1
Modified residuei227PhosphoserineBy similarity1
Modified residuei326N6-acetyllysineCombined sources1
Modified residuei346N6-acetyllysine; alternateCombined sources1
Modified residuei346N6-succinyllysine; alternateCombined sources1
Modified residuei352N6-acetyllysine; alternateCombined sources1
Modified residuei352N6-succinyllysine; alternateCombined sources1
Modified residuei363N6-acetyllysine; alternateCombined sources1
Modified residuei363N6-succinyllysine; alternateCombined sources1
Modified residuei365N6-acetyllysine; alternateCombined sources1
Modified residuei365N6-succinyllysine; alternateCombined sources1
Modified residuei384PhosphoserineBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei390N6-acetyllysine; alternateCombined sources1
Modified residuei390N6-succinyllysine; alternateCombined sources1
Modified residuei399N6-acetyllysineCombined sources1
Modified residuei410PhosphothreonineBy similarity1
Modified residuei415N6-acetyllysine; alternateCombined sources1
Modified residuei415N6-succinyllysine; alternateBy similarity1
Modified residuei457N6-acetyllysine; alternateCombined sources1
Modified residuei457N6-malonyllysine; alternateBy similarity1
Modified residuei457N6-succinyllysine; alternateBy similarity1
Modified residuei477N6-acetyllysine; alternateCombined sources1
Modified residuei477N6-succinyllysine; alternateCombined sources1
Modified residuei480N6-acetyllysine; alternateCombined sources1
Modified residuei480N6-succinyllysine; alternateCombined sources1
Modified residuei503N6-acetyllysine; alternateCombined sources1
Modified residuei503N6-malonyllysine; alternateBy similarity1
Modified residuei503N6-succinyllysine; alternateCombined sources1
Modified residuei512PhosphotyrosineBy similarity1
Modified residuei527N6-acetyllysine; alternateCombined sources1
Modified residuei527N6-malonyllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateCombined sources1
Modified residuei545N6-acetyllysine; alternateCombined sources1
Modified residuei545N6-succinyllysine; alternateCombined sources1
Modified residuei548N6-acetyllysineCombined sources1

Post-translational modificationi

Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.
ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

EPDiP26443
MaxQBiP26443
PaxDbiP26443
PeptideAtlasiP26443
PRIDEiP26443

2D gel databases

REPRODUCTION-2DPAGEiP26443
SWISS-2DPAGEiP26443
UCD-2DPAGEiP26443

PTM databases

iPTMnetiP26443
PhosphoSitePlusiP26443
SwissPalmiP26443

Expressioni

Gene expression databases

BgeeiENSMUSG00000021794
ExpressionAtlasiP26443 baseline and differential
GenevisibleiP26443 MM

Interactioni

Subunit structurei

Homohexamer.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199956, 6 interactors
IntActiP26443, 12 interactors
MINTiP26443
STRINGi10090.ENSMUSP00000022322

Structurei

3D structure databases

ProteinModelPortaliP26443
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
GeneTreeiENSGT00390000000854
HOGENOMiHOG000243801
HOVERGENiHBG005479
InParanoidiP26443
KOiK00261
OMAiPCFAAFP
OrthoDBiEOG091G0KMT
PhylomeDBiP26443
TreeFamiTF313945

Family and domain databases

CDDicd01076 NAD_bind_1_Glu_DH, 1 hit
InterProiView protein in InterPro
IPR006095 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
IPR036291 NAD(P)-bd_dom_sf
IPR033922 NAD_bind_Glu_DH
PfamiView protein in Pfam
PF00208 ELFV_dehydrog, 1 hit
PF02812 ELFV_dehydrog_N, 1 hit
PRINTSiPR00082 GLFDHDRGNASE
SMARTiView protein in SMART
SM00839 ELFV_dehydrog, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00074 GLFV_DEHYDROGENASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

P26443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR
60 70 80 90 100
RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN
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 SILGMTPGFG
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):61,337
Last modified:August 1, 1992 - v1
Checksum:i92738AA5A133838A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti495D → G in BAC40767 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57024 mRNA Translation: CAA40341.1
AK089152 mRNA Translation: BAC40767.1
BC052724 mRNA Translation: AAH52724.1
BC057347 mRNA Translation: AAH57347.1
CCDSiCCDS26935.1
PIRiS16239
RefSeqiNP_032159.1, NM_008133.4
UniGeneiMm.10600

Genome annotation databases

EnsembliENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794
GeneIDi14661
KEGGimmu:14661
UCSCiuc007tas.2 mouse

Similar proteinsi

Entry informationi

Entry nameiDHE3_MOUSE
AccessioniPrimary (citable) accession number: P26443
Secondary accession number(s): Q8C273
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 25, 2018
This is version 163 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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