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Q64I00

- DHE4_PONPY

UniProt

Q64I00 - DHE4_PONPY

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Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Pongo pygmaeus (Bornean orangutan)
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 sitei84 – 841SubstrateBy similarity
Active sitei183 – 1831PROSITE-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
OrganismiPongo pygmaeus (Bornean orangutan)
Taxonomic identifieri9600 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

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 – 5353MitochondrionBy similarityAdd
BLAST
Chaini54 – 558505Glutamate dehydrogenase 2, mitochondrialPRO_0000007211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-succinyllysineBy similarity
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei84 – 841N6-acetyllysine; alternateBy similarity
Modified residuei84 – 841N6-succinyllysine; alternateBy similarity
Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei135 – 1351PhosphotyrosineBy similarity
Modified residuei162 – 1621N6-acetyllysine; alternateBy similarity
Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
Modified residuei171 – 1711N6-acetyllysineBy similarity
Modified residuei172 – 1721ADP-ribosylcysteineBy similarity
Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
Modified residuei183 – 1831N6-succinyllysine; alternateBy similarity
Modified residuei187 – 1871N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei200 – 2001N6-succinyllysineBy similarity
Modified residuei211 – 2111N6-acetyllysineBy similarity
Modified residuei326 – 3261N6-acetyllysineBy similarity
Modified residuei346 – 3461N6-acetyllysine; alternateBy similarity
Modified residuei346 – 3461N6-succinyllysine; alternateBy similarity
Modified residuei363 – 3631N6-acetyllysine; alternateBy similarity
Modified residuei363 – 3631N6-succinyllysine; alternateBy similarity
Modified residuei365 – 3651N6-acetyllysine; alternateBy similarity
Modified residuei365 – 3651N6-succinyllysine; alternateBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei390 – 3901N6-acetyllysine; alternateBy similarity
Modified residuei390 – 3901N6-succinyllysine; alternateBy similarity
Modified residuei399 – 3991N6-acetyllysineBy similarity
Modified residuei415 – 4151N6-acetyllysine; alternateBy similarity
Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity
Modified residuei457 – 4571N6-acetyllysine; alternateBy similarity
Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei503 – 5031N6-acetyllysine; alternateBy similarity
Modified residuei503 – 5031N6-succinyllysine; alternateBy similarity
Modified residuei527 – 5271N6-acetyllysine; alternateBy similarity
Modified residuei527 – 5271N6-succinyllysine; alternateBy similarity
Modified residuei545 – 5451N6-acetyllysine; alternateBy similarity
Modified residuei545 – 5451N6-succinyllysine; alternateBy similarity
Modified residuei548 – 5481N6-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

PRIDEiQ64I00.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi9600.ENSPPYP00000023161.

Structurei

3D structure databases

ProteinModelPortaliQ64I00.
SMRiQ64I00. Positions 63-558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
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.

Q64I00-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MYRYLGKALL LSRAGPAALG SAANHSAALL GRARGQPAAA SQPGLALASR
60 70 80 90 100
RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMNTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SNVGMTPGFG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCVAV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FRLQHGSILG FPKAKPYEGS ILEADCDILI PAATEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NILVIPDVYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFRDSISGA
510 520 530 540 550
SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY

SEAGVTFT
Length:558
Mass (Da):61,386
Last modified:October 25, 2004 - v1
Checksum:iEF26FEC7089E5D44
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY588268 Genomic DNA. Translation: AAU03134.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY588268 Genomic DNA. Translation: AAU03134.1 .

3D structure databases

ProteinModelPortali Q64I00.
SMRi Q64I00. Positions 63-558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9600.ENSPPYP00000023161.

Proteomic databases

PRIDEi Q64I00.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0334.
HOGENOMi HOG000243801.
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_PONPY
AccessioniPrimary (citable) accession number: Q64I00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 25, 2004
Last modified: October 29, 2014
This is version 64 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