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Q64HZ9

- DHE4_HYLLA

UniProt

Q64HZ9 - DHE4_HYLLA

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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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811SubstrateBy similarity
Active sitei180 – 1801PROSITE-ProRule annotation

GO - Molecular functioni

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

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. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050MitochondrionBy similarityAdd
BLAST
Chaini51 – 555505Glutamate dehydrogenase 2, mitochondrialPRO_0000007209Add
BLAST

Amino acid modifications

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

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

        10         20         30         40         50
MYCYLGKALL PSGAGPAALG SAGAALLGRA RGQPAAAPQP GLALAAWRHY
60 70 80 90 100
SEVVADRKDD PNFFKMVEGF FDRGASIVED KLVKDLRTRE SEEQKRNRVR
110 120 130 140 150
GILRIIKPCN HVLSLSFPIR RDDGSWEVIE GYRAQHSQHR TPCKGGIRYS
160 170 180 190 200
ADVSVDEVKA LASLMTYKCA VVDVPFGGAK AGVKINPKNY TENELEKITR
210 220 230 240 250
RFTMELAKKG FIGPGIDVPA PDMNTGEREM SWIADTYAST IGHYDINAHA
260 270 280 290 300
CVTGKPISQG GIHGRISATG RGVFHGIENF INEASYMSIL GMTPGFGDKT
310 320 330 340 350
FVVQGFGNVG LHSMRYLHRF GAKCIAVGES DGSIWNPDGI DPKELEDFKL
360 370 380 390 400
QHGSILGFPK AKPYEGSILE ADCDILIPAA SEKQLTKSNA PRVKAKIIAE
410 420 430 440 450
GANGPTTPEA DKIFLERNIM VIPDLYVNAG GVTVSYFEWL KNLNHVSYGR
460 470 480 490 500
LTFKYERDSN YHLLMSVQES LERKFGKHGG TIPIVPTAEF QDSISGASEK
510 520 530 540 550
DIVHSALAYT MERSARQIMR TAMKYNLGLD LRTAAYVNAI EKVFKVYSEA

GVTFT
Length:555
Mass (Da):60,866
Last modified:October 25, 2004 - v1
Checksum:i36BF0E321F993A53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY588269 Genomic DNA. Translation: AAU03135.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY588269 Genomic DNA. Translation: AAU03135.1 .

3D structure databases

ProteinModelPortali Q64HZ9.
SMRi Q64HZ9. Positions 60-555.
ModBasei Search...
MobiDBi 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: October 29, 2014
This is version 56 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