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P00368 (DHE3_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase 1, mitochondrial

Short name=GDH 1
EC=1.4.1.3
Gene names
Name:GLUD1
Synonyms:GLUD
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
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.

Enzyme regulation

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP By similarity.

Subunit structure

Homohexamer.

Subcellular location

Mitochondrion matrix.

Miscellaneous

ADP can occupy the NADH binding site and activate the enzyme 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 – 503503Glutamate dehydrogenase 1, mitochondrial
PRO_0000182742

Regions

Nucleotide binding87 – 893NAD By similarity

Sites

Active site1291 Ref.1
Binding site931Substrate By similarity
Binding site1171Substrate By similarity
Binding site1221NAD By similarity
Binding site1981NAD By similarity
Binding site2121GTP By similarity
Binding site2161GTP By similarity
Binding site2651GTP By similarity
Binding site2681GTP By similarity
Binding site3841Substrate By similarity
Binding site3891NAD By similarity
Binding site3951ADP By similarity
Binding site4611ADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P00368 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 340DDB45BB0A5B04

FASTA50355,712
        10         20         30         40         50         60 
CZAADKEDDP NFFKMVEGFF DRGASIVEDK LVEGLRTRQS MEQRRHRVRG ILRIIKPCNH 

        70         80         90        100        110        120 
VLSVSFPIKR DDGZWEVIEG YRAQHSHQRT PCKGGIRYSL DVSVDEVKAL ASLMTYKCAV 

       130        140        150        160        170        180 
VDVPFGGAKA GVKINPKNYT DEDLEKITRR FTMELAKKGF IGPGVDVPAP NMSTGEREMS 

       190        200        210        220        230        240 
WIADTYASTI GHYDINAHAC VTKPGISQGG IHGRISATGR GLFGHIENFI ENASYMSILG 

       250        260        270        280        290        300 
MTPGFGDKTF AVQGFGNVGL HSMRYLHRFG AKCVAVGEFD GSIWNPDGID PKELEDYKLQ 

       310        320        330        340        350        360 
HGTIMGFPKA QKLEGSILET DCDILIPAAS EKQLTKANAH KVKAKIIAEG ANGPTTPQAD 

       370        380        390        400        410        420 
KIFLERNIMV IPDLYLNAGG VTVSAFZZKN LNHVSYGRLT FKYERDSNYH LLMSVQESLE 

       430        440        450        460        470        480 
RKFGKHGGTI PVVPTAEFQD RISGASEKDI VHSGLAYTME RSARQIMRTA MKYNLGLDLR 

       490        500 
TAAYVNAIEK VFKVYNEAGL TFT 

« Hide

References

[1]"Amino acd sequence of chicken liver glutamate dehydrogenase."
Moon K., Piszkiewicz D., Smith E.L.
J. Biol. Chem. 248:3093-3107(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, ACTIVE SITE.
Tissue: Liver.

Cross-references

Sequence databases

PIRDECHE. A00380.
UniGeneGga.16450.

3D structure databases

ProteinModelPortalP00368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000003139.

Proteomic databases

PaxDbP00368.
PRIDEP00368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHOG000243801.
HOVERGENHBG005479.
InParanoidP00368.
PhylomeDBP00368.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP00368.

Entry information

Entry nameDHE3_CHICK
AccessionPrimary (citable) accession number: P00368
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 97 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