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P00366 (DHE3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase 1, mitochondrial

Short name=GDH 1
EC=1.4.1.3
Gene names
Name:GLUD1
Synonyms:GLUD
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. Ref.1 Ref.9

Catalytic activity

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

Enzyme regulation

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme.

Subunit structure

Homohexamer. Ref.10

Subcellular location

Mitochondrion matrix.

Post-translational modification

ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer By similarity.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5757Mitochondrion Ref.3
Chain58 – 558501Glutamate dehydrogenase 1, mitochondrial
PRO_0000007205

Regions

Nucleotide binding141 – 1433NAD

Sites

Active site1831
Binding site1471Substrate
Binding site1711Substrate
Binding site1761NAD
Binding site2521NAD
Binding site2661GTP
Binding site2701GTP
Binding site3191GTP
Binding site3221GTP
Binding site4381Substrate
Binding site4441NAD
Binding site4501ADP
Binding site5161ADP

Amino acid modifications

Modified residue681N6-succinyllysine By similarity
Modified residue791Phosphoserine By similarity
Modified residue841N6-acetyllysine; alternate Ref.7
Modified residue841N6-succinyllysine; alternate Ref.7
Modified residue901N6-acetyllysine Ref.7
Modified residue1101N6-acetyllysine; alternate Ref.7
Modified residue1101N6-succinyllysine; alternate Ref.7
Modified residue1281Phosphoserine By similarity
Modified residue1351Phosphotyrosine By similarity
Modified residue1621N6-acetyllysine; alternate Ref.7
Modified residue1621N6-succinyllysine; alternate Ref.7
Modified residue1711N6-acetyllysine By similarity
Modified residue1721ADP-ribosylcysteine By similarity
Modified residue1831N6-acetyllysine; alternate
Modified residue1831N6-succinyllysine; alternate By similarity
Modified residue1871N6-acetyllysine By similarity
Modified residue1911N6-acetyllysine; alternate
Modified residue1911N6-succinyllysine; alternate By similarity
Modified residue2001N6-succinyllysine By similarity
Modified residue2111N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine By similarity
Modified residue3461N6-acetyllysine; alternate By similarity
Modified residue3461N6-succinyllysine; alternate By similarity
Modified residue3521N6-acetyllysine; alternate By similarity
Modified residue3521N6-succinyllysine; alternate By similarity
Modified residue3631N6-acetyllysine; alternate Ref.7
Modified residue3631N6-succinyllysine; alternate Ref.7
Modified residue3651N6-acetyllysine; alternate
Modified residue3651N6-succinyllysine; alternate By similarity
Modified residue3861N6-acetyllysine Ref.7
Modified residue3901N6-acetyllysine; alternate By similarity
Modified residue3901N6-succinyllysine; alternate By similarity
Modified residue3991N6-acetyllysine Ref.7
Modified residue4151N6-acetyllysine; alternate Ref.7
Modified residue4151N6-succinyllysine; alternate Ref.7
Modified residue4571N6-acetyllysine; alternate Ref.7
Modified residue4571N6-malonyllysine; alternate Ref.7
Modified residue4571N6-succinyllysine; alternate Ref.7
Modified residue4771N6-acetyllysine; alternate By similarity
Modified residue4771N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine; alternate
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue5031N6-acetyllysine; alternate Ref.7
Modified residue5031N6-malonyllysine; alternate Ref.7
Modified residue5031N6-succinyllysine; alternate Ref.7
Modified residue5271N6-acetyllysine; alternate Ref.7
Modified residue5271N6-malonyllysine; alternate Ref.7
Modified residue5271N6-succinyllysine; alternate Ref.7
Modified residue5451N6-acetyllysine; alternate Ref.7
Modified residue5451N6-succinyllysine; alternate Ref.7

Experimental info

Sequence conflict41Y → C in AAI03337. Ref.2
Sequence conflict141A → I in AAI03337. Ref.2
Sequence conflict22 – 232AS → VA in AAI03337. Ref.2
Sequence conflict281A → V in AAI03337. Ref.2
Sequence conflict321W → R in AAI03337. Ref.2
Sequence conflict37 – 382PA → AAAAV in AAI03337. Ref.2
Sequence conflict93 – 953ETE → QTQ AA sequence Ref.3
Sequence conflict1041S → G in AAI03337. Ref.2
Sequence conflict1041S → G AA sequence Ref.3
Sequence conflict141 – 1422QH → HQ AA sequence Ref.3
Sequence conflict196 – 1972NE → ED AA sequence Ref.3
Sequence conflict2251D → N AA sequence Ref.3
Sequence conflict257 – 2593GKP → KPG AA sequence Ref.3
Sequence conflict278 – 2792HG → GH AA sequence Ref.3
Sequence conflict3051V → A in AAI03337. Ref.2
Sequence conflict3051V → A AA sequence Ref.3
Sequence conflict3281I → V in AAI03337. Ref.2
Sequence conflict3281I → V AA sequence Ref.3
Sequence conflict3291T → A in AAI03337. Ref.2
Sequence conflict3891T → P in AAP55683. Ref.1
Sequence conflict4121E → Q AA sequence Ref.3
Sequence conflict441 – 4422EW → QI AA sequence Ref.3
Sequence conflict4441N → K in AAI03337. Ref.2
Sequence conflict4441N → K AA sequence Ref.3

Secondary structure

............................................................................................ 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00366 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: 194D74A33F2310E7

FASTA55861,512
        10         20         30         40         50         60 
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLVPPAR RHYSEAAADR 

        70         80         90        100        110        120 
EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRETEEQKRN RVRSILRIIK PCNHVLSLSF 

       130        140        150        160        170        180 
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG 

       190        200        210        220        230        240 
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGVD VPAPDMSTGE REMSWIADTY 

       250        260        270        280        290        300 
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 

       310        320        330        340        350        360 
DKTFVVQGFG NVGLHSMRYL HRFGAKCITV GESDGSIWNP DGIDPKELED FKLQHGTILG 

       370        380        390        400        410        420 
FPKAKIYEGS ILEVDCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER 

       430        440        450        460        470        480 
NIMVIPDLYL NAGGVTVSYF EWLNNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK 

       490        500        510        520        530        540 
HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV 

       550 
NAIEKVFRVY NEAGVTFT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase."
Kim D.W., Eum W.S., Jang S.H., Yoon C.S., Kim Y.H., Choi S.H., Choi H.S., Kim S.Y., Kwon H.Y., Kang J.H., Kwon O.-S., Cho S.-W., Park J., Choi S.Y.
J. Biochem. Mol. Biol. 36:545-551(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ALLOSTERIC REGULATION.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Sequence of bovine liver glutamate dehydrogenase. 8. Peptides produced by specific chemical cleavages; the complete sequence of the protein."
Moon K., Smith E.L.
J. Biol. Chem. 248:3082-3088(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-558.
Tissue: Liver.
[4]"Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme."
Julliard J.H., Smith E.L.
J. Biol. Chem. 254:3427-3438(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 440-441.
[5]"Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues."
Witzemann V., Koberstein R., Sund H., Rasched I., Joernvall H., Noack K.
Eur. J. Biochem. 43:319-325(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Studies of glutamate dehydrogenase. Identification of an amino group involved in the substrate binding."
Rasched I., Joernvall H., Sund H.
Eur. J. Biochem. 41:603-606(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY STUDIES OF SUBSTRATE-BINDING SITE.
[7]"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-84; LYS-90; LYS-110; LYS-162; LYS-183; LYS-191; LYS-363; LYS-365; LYS-386; LYS-399; LYS-415; LYS-457; LYS-480; LYS-503; LYS-527 AND LYS-545, MALONYLATION AT LYS-457; LYS-503 AND LYS-527, SUCCINYLATION AT LYS-84; LYS-110; LYS-162; LYS-363; LYS-415; LYS-457; LYS-503; LYS-527 AND LYS-545.
[8]"The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery."
Peterson P.E., Smith T.J.
Structure 7:769-782(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558.
Tissue: Liver.
[9]"Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation."
Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.
J. Mol. Biol. 307:707-720(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558 IN COMPLEX WITH SUBSTRATE; NADH AND GTP, FUNCTION.
[10]"Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation."
Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.
Biochemistry 42:3446-3456(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-520 ALONE AND IN COMPLEX WITH ADP, HOMOHEXAMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY138843 mRNA. Translation: AAN15276.1.
AY256856 mRNA. Translation: AAP55683.1.
BC103336 mRNA. Translation: AAI03337.1.
PIRDEBOE. A92129.
RefSeqNP_872593.1. NM_182652.1.
UniGeneBt.107155.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HWYX-ray3.20A/B/C/D/E/F58-558[»]
1HWZX-ray2.80A/B/C/D/E/F58-558[»]
1NQTX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
1NR7X-ray3.30A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
3ETDX-ray2.50A/B/C/D/E/F58-558[»]
3ETEX-ray3.00A/B/C/D/E/F58-558[»]
3ETGX-ray2.50A/B/C/D/E/F58-558[»]
3MVOX-ray3.23A/B/C/D/E/F58-558[»]
3MVQX-ray2.94A/B/C/D/E/F58-558[»]
3MW9X-ray2.50A/B/C/D/E/F58-558[»]
3QMUX-ray3.62A/B/C/D/E/F/G/H/I/J/K/L58-558[»]
ProteinModelPortalP00366.
SMRP00366. Positions 63-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-39002N.
IntActP00366. 1 interaction.

Chemistry

BindingDBP00366.
ChEMBLCHEMBL4628.

Proteomic databases

PaxDbP00366.
PRIDEP00366.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000009923; ENSBTAP00000009923; ENSBTAG00000007540.
GeneID281785.
KEGGbta:281785.

Organism-specific databases

CTD2746.

Phylogenomic databases

eggNOGCOG0334.
GeneTreeENSGT00390000000854.
HOGENOMHOG000243801.
HOVERGENHBG005479.
InParanoidP00366.
KOK00261.
OrthoDBEOG73NG50.
TreeFamTF313945.

Enzyme and pathway databases

SABIO-RKP00366.

Gene expression databases

ArrayExpressP00366.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. 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]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00366.
NextBio20805698.

Entry information

Entry nameDHE3_BOVIN
AccessionPrimary (citable) accession number: P00366
Secondary accession number(s): Q3SYY0, Q7YS29, Q8HZ49
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2004
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references