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P00368

- DHE3_CHICK

UniProt

P00368 - DHE3_CHICK

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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Gallus gallus (Chicken)
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.PROSITE-ProRule annotation

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931SubstrateBy similarity
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei122 – 1221NADBy similarity
Active sitei129 – 12911 PublicationPROSITE-ProRule annotation
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 sitei389 – 3891NADBy similarity
Binding sitei395 – 3951ADPBy similarity
Binding sitei461 – 4611ADPBy 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, NADP, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Gene namesi
Name:GLUD1
Synonyms:GLUD
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

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 – 503503Glutamate dehydrogenase 1, mitochondrialPRO_0000182742Add
BLAST

Proteomic databases

PaxDbiP00368.
PRIDEiP00368.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000003139.

Structurei

3D structure databases

ProteinModelPortaliP00368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP00368.
PhylomeDBiP00368.

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]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00368-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
CZAADKEDDP NFFKMVEGFF DRGASIVEDK LVEGLRTRQS MEQRRHRVRG
60 70 80 90 100
ILRIIKPCNH VLSVSFPIKR DDGZWEVIEG YRAQHSHQRT PCKGGIRYSL
110 120 130 140 150
DVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVKINPKNYT DEDLEKITRR
160 170 180 190 200
FTMELAKKGF IGPGVDVPAP NMSTGEREMS WIADTYASTI GHYDINAHAC
210 220 230 240 250
VTKPGISQGG IHGRISATGR GLFGHIENFI ENASYMSILG MTPGFGDKTF
260 270 280 290 300
AVQGFGNVGL HSMRYLHRFG AKCVAVGEFD GSIWNPDGID PKELEDYKLQ
310 320 330 340 350
HGTIMGFPKA QKLEGSILET DCDILIPAAS EKQLTKANAH KVKAKIIAEG
360 370 380 390 400
ANGPTTPQAD KIFLERNIMV IPDLYLNAGG VTVSAFZZKN LNHVSYGRLT
410 420 430 440 450
FKYERDSNYH LLMSVQESLE RKFGKHGGTI PVVPTAEFQD RISGASEKDI
460 470 480 490 500
VHSGLAYTME RSARQIMRTA MKYNLGLDLR TAAYVNAIEK VFKVYNEAGL

TFT
Length:503
Mass (Da):55,712
Last modified:July 21, 1986 - v1
Checksum:i340DDB45BB0A5B04
GO

Sequence databases

PIRiA00380. DECHE.
UniGeneiGga.16450.

Cross-referencesi

Sequence databases

PIRi A00380. DECHE.
UniGenei Gga.16450.

3D structure databases

ProteinModelPortali P00368.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000003139.

Proteomic databases

PaxDbi P00368.
PRIDEi P00368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0334.
HOGENOMi HOG000243801.
HOVERGENi HBG005479.
InParanoidi P00368.
PhylomeDBi P00368.

Miscellaneous databases

PROi P00368.

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 ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiDHE3_CHICK
AccessioniPrimary (citable) accession number: P00368
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 99 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3