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P28270

- DHE3_ELEEL

UniProt

P28270 - DHE3_ELEEL

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Protein

Glutamate dehydrogenase

Gene
N/A
Organism
Electrophorus electricus (Electric eel) (Gymnotus electricus)
Status
Reviewed - Annotation score: 2 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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311SubstrateBy similarity

GO - Molecular functioni

  1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB
  2. tricarboxylic acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase (EC:1.4.1.3)
Short name:
GDH
OrganismiElectrophorus electricus (Electric eel) (Gymnotus electricus)
Taxonomic identifieri8005 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiGymnotiformesGymnotoideiGymnotidaeElectrophorus

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›51›51Glutamate dehydrogenasePRO_0000182744Add
BLAST

Interactioni

Subunit structurei

Homohexamer.

Structurei

3D structure databases

ProteinModelPortaliP28270.
SMRiP28270. Positions 5-47.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragments.

P28270-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
SEAVAEKEDD PNFFKMVEGF FDKGAAIVEN KLVEDLKTRG SPEVEGNLTF

T
Length:51
Mass (Da):5,650
Last modified:December 1, 1992 - v1
Checksum:i499A36DF9A05B004
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi43 – 442Curated
Non-terminal residuei51 – 511

Cross-referencesi

3D structure databases

ProteinModelPortali P28270.
SMRi P28270. Positions 5-47.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiDHE3_ELEEL
AccessioniPrimary (citable) accession number: P28270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 61 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3