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P82264 (DHE3_CHAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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, mitochondrial

Short name=GDH
EC=1.4.1.3
Gene names
Name:glud1
Synonyms:glud
OrganismChaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus)
Taxonomic identifier36190 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaPerciformesNotothenioideiChannichthyidaeChaenocephalus

Protein attributes

Sequence length504 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.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504Glutamate dehydrogenase, mitochondrial
PRO_0000182743

Regions

Nucleotide binding87 – 893NAD By similarity

Sites

Active site1291 By similarity
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 site3901NAD By similarity
Binding site3961ADP By similarity
Binding site4621ADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P82264 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D8E20681642E3E89

FASTA50455,394
        10         20         30         40         50         60 
ADAADKPDDP NFFRMVEGFF DRGASIVEDK LVEDLRTKET PEQKKGRVAG ILRIIKPCNH 

        70         80         90        100        110        120 
VLSLSFPIKR DNGEWEVIEG YRAQHSQHRT PCKGGIRYSM DVSVDEVKAL ASLMTYKCAV 

       130        140        150        160        170        180 
VDVPFGGAKA GVRINTKNYS DNELEKITRR FTIELAKKGF IGPGIDVPAP DMSTGEREMS 

       190        200        210        220        230        240 
WIADTYANTI AHTDINAHAC VTGKPISQGG IHGRISATGR GVFHGIENFM NEASYMSMVG 

       250        260        270        280        290        300 
LTPGVQDKTF VIQGFGNVGL HSMRYLHRFG AKCVGIGEID GAIYNADGID PKALEEYKLQ 

       310        320        330        340        350        360 
NGTIVGFPGA KPYEGSILEA DCDILIPAAG EKQLTRNNAR RIKAKIIAEG ANGPTTPDAD 

       370        380        390        400        410        420 
KIFLENNVMV IPDMYLNAGG VTVSYFEWLK NLNHVSYGRL TFKYERDSNY HLLMSVQESL 

       430        440        450        460        470        480 
ERKFGKQGGP IPVVPTADFQ ARVAGASEKD IVHSGLAYTM ERSARQIMRT ASKHNLGLDI 

       490        500 
RTAAYVNAIE KVFKVYNEAG LTFT 

« Hide

References

[1]"L-glutamate dehydrogenase from the antarctic fish Chaenocephalus aceratus. Primary structure, function and thermodynamic characterisation: relationship with cold adaptation."
Ciardiello M.A., Camardella L., Carratore V., di Prisco G.
Biochim. Biophys. Acta 1543:11-23(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

3D structure databases

ProteinModelPortalP82264.
SMRP82264. Positions 9-504.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP82264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005479.

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]
ProtoNetSearch...

Entry information

Entry nameDHE3_CHAAC
AccessionPrimary (citable) accession number: P82264
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 69 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