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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Bos taurus (Bovine)
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.2 Publications

Catalytic activityi

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

Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei147Substrate1 Publication1
Binding sitei171Substrate1 Publication1
Binding sitei176NAD1 Publication1
Active sitei1831
Binding sitei252NAD1 Publication1
Binding sitei266GTP1 Publication1
Binding sitei270GTP1 Publication1
Binding sitei319GTP1 Publication1
Binding sitei322GTP1 Publication1
Binding sitei438Substrate1 Publication1
Binding sitei444NAD1 Publication1
Binding sitei450ADP1 Publication1
Binding sitei516ADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi141 – 143NAD1 Publication3

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi1.4.1.2 908
SABIO-RKiP00366

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4628

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 57Mitochondrion1 PublicationAdd BLAST57
ChainiPRO_000000720558 – 558Glutamate dehydrogenase 1, mitochondrialAdd BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei84N6-acetyllysine; alternate1 Publication1
Modified residuei84N6-succinyllysine; alternate1 Publication1
Modified residuei90N6-acetyllysine1 Publication1
Modified residuei110N6-acetyllysine; alternate1 Publication1
Modified residuei110N6-succinyllysine; alternate1 Publication1
Modified residuei128PhosphoserineBy similarity1
Modified residuei135PhosphotyrosineBy similarity1
Modified residuei162N6-acetyllysine; alternate1 Publication1
Modified residuei162N6-succinyllysine; alternate1 Publication1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei172ADP-ribosylcysteineBy similarity1
Modified residuei183N6-acetyllysine; alternate1 Publication1
Modified residuei183N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternate1 Publication1
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; alternate1 Publication1
Modified residuei363N6-succinyllysine; alternate1 Publication1
Modified residuei365N6-acetyllysine; alternate1 Publication1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei386N6-acetyllysine1 Publication1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysine1 Publication1
Modified residuei410PhosphothreonineBy similarity1
Modified residuei415N6-acetyllysine; alternate1 Publication1
Modified residuei415N6-succinyllysine; alternate1 Publication1
Modified residuei457N6-acetyllysine; alternate1 Publication1
Modified residuei457N6-malonyllysine; alternate1 Publication1
Modified residuei457N6-succinyllysine; alternate1 Publication1
Modified residuei477N6-acetyllysine; alternateBy similarity1
Modified residuei477N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysine; alternate1 Publication1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei503N6-acetyllysine; alternate1 Publication1
Modified residuei503N6-malonyllysine; alternate1 Publication1
Modified residuei503N6-succinyllysine; alternate1 Publication1
Modified residuei512PhosphotyrosineBy similarity1
Modified residuei527N6-acetyllysine; alternate1 Publication1
Modified residuei527N6-malonyllysine; alternate1 Publication1
Modified residuei527N6-succinyllysine; alternate1 Publication1
Modified residuei545N6-acetyllysine; alternate1 Publication1
Modified residuei545N6-succinyllysine; alternate1 Publication1

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

PaxDbiP00366
PeptideAtlasiP00366
PRIDEiP00366

PTM databases

iPTMnetiP00366

Interactioni

Subunit structurei

Homohexamer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1221442,EBI-1221442

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-39002N
IntActiP00366, 1 interactor
MINTiP00366
STRINGi9913.ENSBTAP00000009923

Chemistry databases

BindingDBiP00366

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00366
SMRiP00366
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00366

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
HOGENOMiHOG000243801
HOVERGENiHBG005479
InParanoidiP00366
KOiK00261
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.

P00366-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLVPPAR
60 70 80 90 100
RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRETEEQKRN
110 120 130 140 150
RVRSILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGVD VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCITV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGTILG FPKAKIYEGS ILEVDCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLNNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFRVY

NEAGVTFT
Length:558
Mass (Da):61,512
Last modified:September 13, 2004 - v2
Checksum:i194D74A33F2310E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4Y → C in AAI03337 (Ref. 2) Curated1
Sequence conflicti14A → I in AAI03337 (Ref. 2) Curated1
Sequence conflicti22 – 23AS → VA in AAI03337 (Ref. 2) Curated2
Sequence conflicti28A → V in AAI03337 (Ref. 2) Curated1
Sequence conflicti32W → R in AAI03337 (Ref. 2) Curated1
Sequence conflicti37 – 38PA → AAAAV in AAI03337 (Ref. 2) Curated2
Sequence conflicti93 – 95ETE → QTQ AA sequence (PubMed:4735572).Curated3
Sequence conflicti104S → G in AAI03337 (Ref. 2) Curated1
Sequence conflicti104S → G AA sequence (PubMed:4735572).Curated1
Sequence conflicti141 – 142QH → HQ AA sequence (PubMed:4735572).Curated2
Sequence conflicti196 – 197NE → ED AA sequence (PubMed:4735572).Curated2
Sequence conflicti225D → N AA sequence (PubMed:4735572).Curated1
Sequence conflicti257 – 259GKP → KPG AA sequence (PubMed:4735572).Curated3
Sequence conflicti278 – 279HG → GH AA sequence (PubMed:4735572).Curated2
Sequence conflicti305V → A in AAI03337 (Ref. 2) Curated1
Sequence conflicti305V → A AA sequence (PubMed:4735572).Curated1
Sequence conflicti328I → V in AAI03337 (Ref. 2) Curated1
Sequence conflicti328I → V AA sequence (PubMed:4735572).Curated1
Sequence conflicti329T → A in AAI03337 (Ref. 2) Curated1
Sequence conflicti389T → P in AAP55683 (PubMed:14659072).Curated1
Sequence conflicti412E → Q AA sequence (PubMed:4735572).Curated1
Sequence conflicti441 – 442EW → QI AA sequence (PubMed:4735572).Curated2
Sequence conflicti444N → K in AAI03337 (Ref. 2) Curated1
Sequence conflicti444N → K AA sequence (PubMed:4735572).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY138843 mRNA Translation: AAN15276.1
AY256856 mRNA Translation: AAP55683.1
BC103336 mRNA Translation: AAI03337.1
PIRiA92129 DEBOE
RefSeqiNP_872593.2, NM_182652.2
UniGeneiBt.107155
Bt.55415

Genome annotation databases

GeneIDi281785
KEGGibta:281785

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY138843 mRNA Translation: AAN15276.1
AY256856 mRNA Translation: AAP55683.1
BC103336 mRNA Translation: AAI03337.1
PIRiA92129 DEBOE
RefSeqiNP_872593.2, NM_182652.2
UniGeneiBt.107155
Bt.55415

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HWYX-ray3.20A/B/C/D/E/F58-558[»]
1NQTX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
1NR7X-ray3.30A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
3ETDX-ray2.50A/B/C/D/E/F58-558[»]
3ETEX-ray3.00A/B/C/D/E/F58-558[»]
3ETGX-ray2.50A/B/C/D/E/F58-558[»]
3JCZelectron microscopy3.26A/B/C/D/E/F58-558[»]
3JD0electron microscopy3.47A/B/C/D/E/F58-558[»]
3JD1electron microscopy3.30A/B/C/D/E/F58-558[»]
3JD2electron microscopy3.30A/B/C/D/E/F58-558[»]
3JD3electron microscopy3.60A/B/C/D/E/F58-558[»]
3JD4electron microscopy3.40A/B/C/D/E/F58-558[»]
5K12electron microscopy1.80A/B/C/D/E/F1-558[»]
6DHDX-ray2.50A/B/C/D/E/F58-558[»]
6DHLX-ray3.62A/B/C/D/E/F58-558[»]
6DHMX-ray3.00A/B/C/D/E/F58-558[»]
6DHNX-ray3.30A/B/C/D/E/F58-558[»]
6DHQX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L58-558[»]
ProteinModelPortaliP00366
SMRiP00366
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39002N
IntActiP00366, 1 interactor
MINTiP00366
STRINGi9913.ENSBTAP00000009923

Chemistry databases

BindingDBiP00366
ChEMBLiCHEMBL4628

PTM databases

iPTMnetiP00366

Proteomic databases

PaxDbiP00366
PeptideAtlasiP00366
PRIDEiP00366

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281785
KEGGibta:281785

Organism-specific databases

CTDi2746

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
HOGENOMiHOG000243801
HOVERGENiHBG005479
InParanoidiP00366
KOiK00261
TreeFamiTF313945

Enzyme and pathway databases

BRENDAi1.4.1.2 908
SABIO-RKiP00366

Miscellaneous databases

EvolutionaryTraceiP00366

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
ProtoNetiSearch...

Entry informationi

Entry nameiDHE3_BOVIN
AccessioniPrimary (citable) accession number: P00366
Secondary accession number(s): Q3SYY0, Q7YS29, Q8HZ49
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2004
Last modified: October 10, 2018
This is version 151 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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