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P82264

- DHE3_CHAAC

UniProt

P82264 - DHE3_CHAAC

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Protein

Glutamate dehydrogenase, mitochondrial

Gene

glud1

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.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.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 – 931SubstrateBy similarity
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei122 – 1221NADBy similarity
Active sitei129 – 1291By similarity
Binding sitei198 – 1981NADBy similarity
Binding sitei212 – 2121GTPBy similarity
Binding sitei216 – 2161GTPBy similarity
Binding sitei265 – 2651GTPBy similarity
Binding sitei268 – 2681GTPBy similarity
Binding sitei384 – 3841SubstrateBy similarity
Binding sitei390 – 3901NADBy similarity
Binding sitei396 – 3961ADPBy similarity
Binding sitei462 – 4621ADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi87 – 893NADBy 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesNotothenioideiChannichthyidaeChaenocephalus

Subcellular locationi

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 – 504504Glutamate dehydrogenase, mitochondrialPRO_0000182743Add
BLAST

Proteomic databases

PRIDEiP82264.

Interactioni

Subunit structurei

Homohexamer.

Structurei

3D structure databases

ProteinModelPortaliP82264.
SMRiP82264. Positions 9-504.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
ADAADKPDDP NFFRMVEGFF DRGASIVEDK LVEDLRTKET PEQKKGRVAG
60 70 80 90 100
ILRIIKPCNH VLSLSFPIKR DNGEWEVIEG YRAQHSQHRT PCKGGIRYSM
110 120 130 140 150
DVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVRINTKNYS DNELEKITRR
160 170 180 190 200
FTIELAKKGF IGPGIDVPAP DMSTGEREMS WIADTYANTI AHTDINAHAC
210 220 230 240 250
VTGKPISQGG IHGRISATGR GVFHGIENFM NEASYMSMVG LTPGVQDKTF
260 270 280 290 300
VIQGFGNVGL HSMRYLHRFG AKCVGIGEID GAIYNADGID PKALEEYKLQ
310 320 330 340 350
NGTIVGFPGA KPYEGSILEA DCDILIPAAG EKQLTRNNAR RIKAKIIAEG
360 370 380 390 400
ANGPTTPDAD KIFLENNVMV IPDMYLNAGG VTVSYFEWLK NLNHVSYGRL
410 420 430 440 450
TFKYERDSNY HLLMSVQESL ERKFGKQGGP IPVVPTADFQ ARVAGASEKD
460 470 480 490 500
IVHSGLAYTM ERSARQIMRT ASKHNLGLDI RTAAYVNAIE KVFKVYNEAG

LTFT
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: October 29, 2014
This is version 72 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