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P82264

- DHE3_CHAAC

UniProt

P82264 - DHE3_CHAAC

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Protein

Glutamate dehydrogenase, mitochondrial

Gene
glud1, glud
Organism
Chaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus)
Status
Reviewed - Annotation score: 4 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.

Catalytic activityi

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

Enzyme regulationi

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

pH dependencei

Optimum pH is 8.0.

Temperature dependencei

Optimum temperature is 30 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Substrate By similarity
Binding sitei117 – 1171Substrate By similarity
Binding sitei122 – 1221NAD By similarity
Active sitei129 – 1291 By similarity
Binding sitei198 – 1981NAD By similarity
Binding sitei212 – 2121GTP By similarity
Binding sitei216 – 2161GTP By similarity
Binding sitei265 – 2651GTP By similarity
Binding sitei268 – 2681GTP By similarity
Binding sitei384 – 3841Substrate By similarity
Binding sitei390 – 3901NAD By similarity
Binding sitei396 – 3961ADP By similarity
Binding sitei462 – 4621ADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi87 – 893NAD By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
  3. GTP binding Source: UniProtKB-KW

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

ATP-binding, GTP-binding, NAD, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase, mitochondrial (EC:1.4.1.3)
Short name:
GDH
Gene namesi
Name:glud1
Synonyms:glud
OrganismiChaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus)
Taxonomic identifieri36190 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPercomorphariaPerciformesNotothenioideiChannichthyidaeChaenocephalus

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Glutamate dehydrogenase, mitochondrialPRO_0000182743Add
BLAST

Proteomic databases

PRIDEiP82264.

Interactioni

Subunit structurei

Homohexamer.

Structurei

3D structure databases

ProteinModelPortaliP82264.
SMRiP82264. Positions 9-504.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG005479.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. 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]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P82264-1 [UniParc]FASTAAdd to Basket

« Hide

ADAADKPDDP NFFRMVEGFF DRGASIVEDK LVEDLRTKET PEQKKGRVAG    50
ILRIIKPCNH VLSLSFPIKR DNGEWEVIEG YRAQHSQHRT PCKGGIRYSM 100
DVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVRINTKNYS DNELEKITRR 150
FTIELAKKGF IGPGIDVPAP DMSTGEREMS WIADTYANTI AHTDINAHAC 200
VTGKPISQGG IHGRISATGR GVFHGIENFM NEASYMSMVG LTPGVQDKTF 250
VIQGFGNVGL HSMRYLHRFG AKCVGIGEID GAIYNADGID PKALEEYKLQ 300
NGTIVGFPGA KPYEGSILEA DCDILIPAAG EKQLTRNNAR RIKAKIIAEG 350
ANGPTTPDAD KIFLENNVMV IPDMYLNAGG VTVSYFEWLK NLNHVSYGRL 400
TFKYERDSNY HLLMSVQESL ERKFGKQGGP IPVVPTADFQ ARVAGASEKD 450
IVHSGLAYTM ERSARQIMRT ASKHNLGLDI RTAAYVNAIE KVFKVYNEAG 500
LTFT 504
Length:504
Mass (Da):55,394
Last modified:March 1, 2001 - v1
Checksum:iD8E20681642E3E89
GO

Cross-referencesi

3D structure databases

ProteinModelPortali P82264.
SMRi P82264. Positions 9-504.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P82264.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005479.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. 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 ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000185. Glu_DH. 1 hit.
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiDHE3_CHAAC
AccessioniPrimary (citable) accession number: P82264
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

ADP can occupy the NADH binding site and activate the enzyme By similarity.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi