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P42174 (DHE3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase 1, mitochondrial

Short name=GDH 1
EC=1.4.1.3
Alternative name(s):
Membrane protein 50
Short name=MP50
Gene names
Name:GLUD1
Synonyms:GLUD
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length33 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Subunit structure

Homohexamer By similarity.

Subcellular location

Mitochondrion membrane; Peripheral membrane protein.

Tissue specificity

Liver, brain and thyroid.

Post-translational modification

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.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›33›33Glutamate dehydrogenase 1, mitochondrial
PRO_0000182741

Amino acid modifications

Modified residue151N6-succinyllysine By similarity

Experimental info

Non-adjacent residues20 – 212
Non-terminal residue331

Sequences

Sequence LengthMass (Da)Tools
P42174 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 63B6C5C3C479F4DD

FASTA333,624
        10         20         30 
SEAAADREDD PNFFKMVEGF GSILEADXDI LIP 

« Hide

References

[1]"A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity."
Rajas F., Rousset B.
Biochem. J. 295:447-455(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRS39010.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000011056.

Proteomic databases

PaxDbP42174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0334.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameDHE3_PIG
AccessionPrimary (citable) accession number: P42174
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families