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P28270 (DHE3_ELEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 59. 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 attributes

Sequence length51 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 By similarity.

Catalytic activity

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

Subunit structure

Homohexamer.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentMitochondrion
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglutamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

tricarboxylic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate dehydrogenase [NAD(P)+] activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›51›51Glutamate dehydrogenase
PRO_0000182744

Sites

Binding site311Substrate By similarity

Experimental info

Non-adjacent residues43 – 442
Non-terminal residue511

Sequences

Sequence LengthMass (Da)Tools
P28270 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 499A36DF9A05B004

FASTA515,650
        10         20         30         40         50 
SEAVAEKEDD PNFFKMVEGF FDKGAAIVEN KLVEDLKTRG SPEVEGNLTF T 

« Hide

References

[1]"The trypsin-catalyzed activation of glutamate dehydrogenase purified from eel liver."
Tang M.-Q., Ando S., Yamada S., Hayashi S.
J. Biochem. 111:655-661(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

3D structure databases

ProteinModelPortalP28270.
SMRP28270. Positions 5-47.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameDHE3_ELEEL
AccessionPrimary (citable) accession number: P28270
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 11, 2014
This is version 59 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