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Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Gorilla gorilla gorilla (Western lowland gorilla)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei84SubstrateBy similarity1
Active sitei183PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
Short name:
GDH 2
Gene namesi
Name:GLUD2
OrganismiGorilla gorilla gorilla (Western lowland gorilla)
Taxonomic identifieri9595 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla
Proteomesi
  • UP000001519 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53MitochondrionBy similarityAdd BLAST53
ChainiPRO_000000720754 – 558Glutamate dehydrogenase 2, mitochondrialAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei84N6-acetyllysine; alternateBy similarity1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei110N6-acetyllysine; alternateBy similarity1
Modified residuei110N6-succinyllysine; alternateBy similarity1
Modified residuei128PhosphoserineBy similarity1
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 residuei326N6-acetyllysineBy similarity1
Modified residuei346N6-acetyllysine; alternateBy similarity1
Modified residuei346N6-succinyllysine; alternateBy similarity1
Modified residuei363N6-acetyllysine; alternateBy similarity1
Modified residuei363N6-succinyllysine; alternateBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Modified residuei410PhosphothreonineBy similarity1
Modified residuei457N6-acetyllysine; 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-succinyllysine; alternateBy similarity1
Modified residuei527N6-acetyllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateBy similarity1
Modified residuei545N6-acetyllysine; alternateBy similarity1
Modified residuei545N6-succinyllysine; alternateBy similarity1
Modified residuei548N6-acetyllysineBy similarity1

Post-translational modificationi

Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

PRIDEiQ64I01.

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ64I01.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG005479.
InParanoidiQ64I01.

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.

Q64I01-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRYLAKALL PSRAGTAALG SAANHSAALL GRSRGQPAAA SQPGLALAAR
60 70 80 90 100
RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLCF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FRLQHGSILG FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADRIFQER NILVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT ADFQDSISGA
510 520 530 540 550
SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY

SEAGVTFT
Length:558
Mass (Da):61,559
Last modified:October 25, 2004 - v1
Checksum:i1D63DDA43335A95A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY588267 Genomic DNA. Translation: AAU03133.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY588267 Genomic DNA. Translation: AAU03133.1.

3D structure databases

ProteinModelPortaliQ64I01.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ64I01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005479.
InParanoidiQ64I01.

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 nameiDHE4_GORGO
AccessioniPrimary (citable) accession number: Q64I01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 25, 2004
Last modified: November 30, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.