SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q64HZ9

- DHE4_HYLLA

UniProt

Q64HZ9 - DHE4_HYLLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamate dehydrogenase 2, mitochondrial
Gene
GLUD2
Organism
Hylobates lar (Common gibbon) (White-handed gibbon)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811Substrate By similarity
Active sitei180 – 1801 By similarity

GO - Molecular functioni

  1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
Short name:
GDH 2
Gene namesi
Name:GLUD2
OrganismiHylobates lar (Common gibbon) (White-handed gibbon)
Taxonomic identifieri9580 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHylobatidaeHylobates

Subcellular locationi

Mitochondrion matrix By similarity

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
Transit peptidei1 – 5050Mitochondrion By similarity
Add
BLAST
Chaini51 – 555505Glutamate dehydrogenase 2, mitochondrial
PRO_0000007209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651N6-succinyllysine By similarity
Modified residuei76 – 761Phosphoserine By similarity
Modified residuei81 – 811N6-acetyllysine; alternate By similarity
Modified residuei81 – 811N6-succinyllysine; alternate By similarity
Modified residuei107 – 1071N6-acetyllysine; alternate By similarity
Modified residuei107 – 1071N6-succinyllysine; alternate By similarity
Modified residuei125 – 1251Phosphoserine By similarity
Modified residuei132 – 1321Phosphotyrosine By similarity
Modified residuei159 – 1591N6-acetyllysine; alternate By similarity
Modified residuei159 – 1591N6-succinyllysine; alternate By similarity
Modified residuei168 – 1681N6-acetyllysine By similarity
Modified residuei169 – 1691ADP-ribosylcysteine By similarity
Modified residuei180 – 1801N6-acetyllysine; alternate By similarity
Modified residuei180 – 1801N6-succinyllysine; alternate By similarity
Modified residuei184 – 1841N6-acetyllysine By similarity
Modified residuei188 – 1881N6-acetyllysine; alternate By similarity
Modified residuei188 – 1881N6-succinyllysine; alternate By similarity
Modified residuei197 – 1971N6-succinyllysine By similarity
Modified residuei208 – 2081N6-acetyllysine By similarity
Modified residuei323 – 3231N6-acetyllysine By similarity
Modified residuei343 – 3431N6-acetyllysine; alternate By similarity
Modified residuei343 – 3431N6-succinyllysine; alternate By similarity
Modified residuei349 – 3491N6-acetyllysine; alternate By similarity
Modified residuei349 – 3491N6-succinyllysine; alternate By similarity
Modified residuei360 – 3601N6-acetyllysine; alternate By similarity
Modified residuei360 – 3601N6-succinyllysine; alternate By similarity
Modified residuei362 – 3621N6-acetyllysine; alternate By similarity
Modified residuei362 – 3621N6-succinyllysine; alternate By similarity
Modified residuei383 – 3831N6-acetyllysine By similarity
Modified residuei387 – 3871N6-acetyllysine; alternate By similarity
Modified residuei387 – 3871N6-succinyllysine; alternate By similarity
Modified residuei396 – 3961N6-acetyllysine By similarity
Modified residuei412 – 4121N6-acetyllysine; alternate By similarity
Modified residuei412 – 4121N6-succinyllysine; alternate By similarity
Modified residuei454 – 4541N6-acetyllysine; alternate By similarity
Modified residuei454 – 4541N6-succinyllysine; alternate By similarity
Modified residuei474 – 4741N6-acetyllysine; alternate By similarity
Modified residuei474 – 4741N6-succinyllysine; alternate By similarity
Modified residuei477 – 4771N6-acetyllysine; alternate By similarity
Modified residuei477 – 4771N6-succinyllysine; alternate By similarity
Modified residuei500 – 5001N6-acetyllysine; alternate By similarity
Modified residuei500 – 5001N6-succinyllysine; alternate By similarity
Modified residuei524 – 5241N6-acetyllysine; alternate By similarity
Modified residuei524 – 5241N6-succinyllysine; alternate By similarity
Modified residuei542 – 5421N6-acetyllysine; alternate By similarity
Modified residuei542 – 5421N6-succinyllysine; alternate By similarity
Modified residuei545 – 5451N6-acetyllysine By similarity

Post-translational modificationi

Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer By similarity.

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

PRIDEiQ64HZ9.

Interactioni

Subunit structurei

Homohexamer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ64HZ9.
SMRiQ64HZ9. Positions 60-555.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64HZ9-1 [UniParc]FASTAAdd to Basket

« Hide

MYCYLGKALL PSGAGPAALG SAGAALLGRA RGQPAAAPQP GLALAAWRHY    50
SEVVADRKDD PNFFKMVEGF FDRGASIVED KLVKDLRTRE SEEQKRNRVR 100
GILRIIKPCN HVLSLSFPIR RDDGSWEVIE GYRAQHSQHR TPCKGGIRYS 150
ADVSVDEVKA LASLMTYKCA VVDVPFGGAK AGVKINPKNY TENELEKITR 200
RFTMELAKKG FIGPGIDVPA PDMNTGEREM SWIADTYAST IGHYDINAHA 250
CVTGKPISQG GIHGRISATG RGVFHGIENF INEASYMSIL GMTPGFGDKT 300
FVVQGFGNVG LHSMRYLHRF GAKCIAVGES DGSIWNPDGI DPKELEDFKL 350
QHGSILGFPK AKPYEGSILE ADCDILIPAA SEKQLTKSNA PRVKAKIIAE 400
GANGPTTPEA DKIFLERNIM VIPDLYVNAG GVTVSYFEWL KNLNHVSYGR 450
LTFKYERDSN YHLLMSVQES LERKFGKHGG TIPIVPTAEF QDSISGASEK 500
DIVHSALAYT MERSARQIMR TAMKYNLGLD LRTAAYVNAI EKVFKVYSEA 550
GVTFT 555
Length:555
Mass (Da):60,866
Last modified:October 25, 2004 - v1
Checksum:i36BF0E321F993A53
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY588269 Genomic DNA. Translation: AAU03135.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY588269 Genomic DNA. Translation: AAU03135.1 .

3D structure databases

ProteinModelPortali Q64HZ9.
SMRi Q64HZ9. Positions 60-555.
ModBasei Search...

Proteomic databases

PRIDEi Q64HZ9.

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.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux."
    Burki F., Kaessmann H.
    Nat. Genet. 36:1061-1063(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDHE4_HYLLA
AccessioniPrimary (citable) accession number: Q64HZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 25, 2004
Last modified: March 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi