Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Hylobates lar (Common gibbon) (White-handed gibbon)
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 sitei81SubstrateBy similarity1
Active sitei180PROSITE-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
OrganismiHylobates lar (Common gibbon) (White-handed gibbon)
Taxonomic identifieri9580 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHylobatidaeHylobates

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50MitochondrionBy similarityAdd BLAST50
ChainiPRO_000000720951 – 555Glutamate dehydrogenase 2, mitochondrialAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei65N6-succinyllysineBy similarity1
Modified residuei76PhosphoserineBy similarity1
Modified residuei81N6-acetyllysine; alternateBy similarity1
Modified residuei81N6-succinyllysine; alternateBy similarity1
Modified residuei107N6-acetyllysine; alternateBy similarity1
Modified residuei107N6-succinyllysine; alternateBy similarity1
Modified residuei125PhosphoserineBy similarity1
Modified residuei132PhosphotyrosineBy similarity1
Modified residuei159N6-acetyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysine; alternateBy similarity1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei169ADP-ribosylcysteineBy similarity1
Modified residuei180N6-acetyllysine; alternateBy similarity1
Modified residuei180N6-succinyllysine; alternateBy similarity1
Modified residuei184N6-acetyllysineBy similarity1
Modified residuei188N6-acetyllysine; alternateBy similarity1
Modified residuei188N6-succinyllysine; alternateBy similarity1
Modified residuei197N6-succinyllysineBy similarity1
Modified residuei208N6-acetyllysineBy similarity1
Modified residuei323N6-acetyllysineBy similarity1
Modified residuei343N6-acetyllysine; alternateBy similarity1
Modified residuei343N6-succinyllysine; alternateBy similarity1
Modified residuei349N6-acetyllysine; alternateBy similarity1
Modified residuei349N6-succinyllysine; alternateBy similarity1
Modified residuei360N6-acetyllysine; alternateBy similarity1
Modified residuei360N6-succinyllysine; alternateBy similarity1
Modified residuei362N6-acetyllysine; alternateBy similarity1
Modified residuei362N6-succinyllysine; alternateBy similarity1
Modified residuei383N6-acetyllysineBy similarity1
Modified residuei387N6-acetyllysine; alternateBy similarity1
Modified residuei387N6-succinyllysine; alternateBy similarity1
Modified residuei396N6-acetyllysineBy similarity1
Modified residuei407PhosphothreonineBy similarity1
Modified residuei412N6-acetyllysine; alternateBy similarity1
Modified residuei412N6-succinyllysine; alternateBy similarity1
Modified residuei454N6-acetyllysine; alternateBy similarity1
Modified residuei454N6-succinyllysine; alternateBy similarity1
Modified residuei474N6-acetyllysine; alternateBy similarity1
Modified residuei474N6-succinyllysine; alternateBy similarity1
Modified residuei477N6-acetyllysine; alternateBy similarity1
Modified residuei477N6-succinyllysine; alternateBy similarity1
Modified residuei500N6-acetyllysine; alternateBy similarity1
Modified residuei500N6-succinyllysine; alternateBy similarity1
Modified residuei524N6-acetyllysine; alternateBy similarity1
Modified residuei524N6-succinyllysine; alternateBy similarity1
Modified residuei542N6-acetyllysine; alternateBy similarity1
Modified residuei542N6-succinyllysine; alternateBy similarity1
Modified residuei545N6-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

PRIDEiQ64HZ9.

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ64HZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG005479.

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.

Q64HZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYCYLGKALL PSGAGPAALG SAGAALLGRA RGQPAAAPQP GLALAAWRHY
60 70 80 90 100
SEVVADRKDD PNFFKMVEGF FDRGASIVED KLVKDLRTRE SEEQKRNRVR
110 120 130 140 150
GILRIIKPCN HVLSLSFPIR RDDGSWEVIE GYRAQHSQHR TPCKGGIRYS
160 170 180 190 200
ADVSVDEVKA LASLMTYKCA VVDVPFGGAK AGVKINPKNY TENELEKITR
210 220 230 240 250
RFTMELAKKG FIGPGIDVPA PDMNTGEREM SWIADTYAST IGHYDINAHA
260 270 280 290 300
CVTGKPISQG GIHGRISATG RGVFHGIENF INEASYMSIL GMTPGFGDKT
310 320 330 340 350
FVVQGFGNVG LHSMRYLHRF GAKCIAVGES DGSIWNPDGI DPKELEDFKL
360 370 380 390 400
QHGSILGFPK AKPYEGSILE ADCDILIPAA SEKQLTKSNA PRVKAKIIAE
410 420 430 440 450
GANGPTTPEA DKIFLERNIM VIPDLYVNAG GVTVSYFEWL KNLNHVSYGR
460 470 480 490 500
LTFKYERDSN YHLLMSVQES LERKFGKHGG TIPIVPTAEF QDSISGASEK
510 520 530 540 550
DIVHSALAYT MERSARQIMR TAMKYNLGLD LRTAAYVNAI EKVFKVYSEA

GVTFT
Length:555
Mass (Da):60,866
Last modified:October 25, 2004 - v1
Checksum:i36BF0E321F993A53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY588269 Genomic DNA. Translation: AAU03135.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY588269 Genomic DNA. Translation: AAU03135.1.

3D structure databases

ProteinModelPortaliQ64HZ9.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ64HZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005479.

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_HYLLA
AccessioniPrimary (citable) accession number: Q64HZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 25, 2004
Last modified: November 30, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.