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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Bos taurus (Bovine)
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. 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

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.

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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi1.4.1.2. 908.
SABIO-RKP00366.

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

GO - Cellular componenti

Complete GO annotation...

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.

Expressioni

Gene expression databases

BgeeiENSBTAG00000007540.

Interactioni

Subunit structurei

Homohexamer.2 Publications

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00366.

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 62Combined sources3
Helixi66 – 88Combined sources23
Helixi97 – 109Combined sources13
Beta strandi113 – 123Combined sources11
Beta strandi125 – 127Combined sources3
Beta strandi129 – 138Combined sources10
Beta strandi142 – 147Combined sources6
Beta strandi150 – 152Combined sources3
Helixi158 – 174Combined sources17
Beta strandi180 – 186Combined sources7
Helixi190 – 192Combined sources3
Helixi195 – 211Combined sources17
Beta strandi214 – 216Combined sources3
Turni217 – 219Combined sources3
Beta strandi220 – 223Combined sources4
Helixi230 – 242Combined sources13
Turni243 – 247Combined sources5
Helixi251 – 253Combined sources3
Beta strandi255 – 257Combined sources3
Helixi260 – 262Combined sources3
Turni266 – 270Combined sources5
Helixi271 – 284Combined sources14
Helixi287 – 292Combined sources6
Beta strandi297 – 299Combined sources3
Beta strandi303 – 307Combined sources5
Helixi311 – 322Combined sources12
Beta strandi326 – 331Combined sources6
Beta strandi336 – 338Combined sources3
Helixi345 – 355Combined sources11
Beta strandi356 – 358Combined sources3
Beta strandi364 – 367Combined sources4
Helixi371 – 373Combined sources3
Beta strandi377 – 381Combined sources5
Beta strandi383 – 385Combined sources3
Turni390 – 392Combined sources3
Helixi393 – 395Combined sources3
Beta strandi399 – 402Combined sources4
Beta strandi405 – 407Combined sources3
Helixi411 – 419Combined sources9
Beta strandi423 – 425Combined sources3
Helixi427 – 430Combined sources4
Helixi433 – 447Combined sources15
Turni451 – 455Combined sources5
Helixi456 – 477Combined sources22
Turni480 – 482Combined sources3
Helixi491 – 496Combined sources6
Helixi502 – 527Combined sources26
Helixi534 – 552Combined sources19
Turni554 – 556Combined sources3

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[»]
1HWZX-ray2.80A/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[»]
3MVOX-ray3.23A/B/C/D/E/F58-558[»]
3MVQX-ray2.94A/B/C/D/E/F58-558[»]
3MW9X-ray2.50A/B/C/D/E/F58-558[»]
3QMUX-ray3.62A/B/C/D/E/F/G/H/I/J/K/L58-558[»]
5K12electron microscopy1.80A/B/C/D/E/F1-558[»]
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.
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.

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.

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[»]
1HWZX-ray2.80A/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[»]
3MVOX-ray3.23A/B/C/D/E/F58-558[»]
3MVQX-ray2.94A/B/C/D/E/F58-558[»]
3MW9X-ray2.50A/B/C/D/E/F58-558[»]
3QMUX-ray3.62A/B/C/D/E/F/G/H/I/J/K/L58-558[»]
5K12electron microscopy1.80A/B/C/D/E/F1-558[»]
ProteinModelPortaliP00366.
SMRiP00366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00366.
ChEMBLiCHEMBL4628.

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-RKP00366.

Miscellaneous databases

EvolutionaryTraceiP00366.

Gene expression databases

BgeeiENSBTAG00000007540.

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_BOVIN
AccessioniPrimary (citable) accession number: P00366
Secondary accession number(s): Q3SYY0, Q7YS29, Q8HZ49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2004
Last modified: November 30, 2016
This is version 144 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

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.