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Reviewed, UniProtKB/Swiss-Prot P00366 (DHE3_BOVIN)

Last modified November 25, 2008. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutamate dehydrogenase 1, mitochondrial
      Short name=GDH
    EC=1.4.1.3
Gene names
Name: GLUD1
Synonyms: GLUD
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

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

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General annotation (Comments)

Function

May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate By similarity.

Catalytic activity

L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + 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.

Subcellular location

Mitochondrion matrix.

Sequence similarities

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5757Mitochondrion
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 residue841N6-acetyllysine By similarity
Modified residue1351Phosphotyrosine By similarity
Modified residue2271Phosphoserine By similarity
Modified residue5031N6-acetyllysine By similarity
Modified residue5121Phosphotyrosine By similarity
Modified residue5271N6-acetyllysine By similarity

Experimental info

Sequence conflict93 – 953ETE → QTQ AA sequence Ref.2
Sequence conflict1041S → G AA sequence Ref.2
Sequence conflict141 – 1422QH → HQ AA sequence Ref.2
Sequence conflict196 – 1972NE → ED AA sequence Ref.2
Sequence conflict2251D → N AA sequence Ref.2
Sequence conflict257 – 2593GKP → KPG AA sequence Ref.2
Sequence conflict278 – 2792HG → GH AA sequence Ref.2
Sequence conflict3051V → A AA sequence Ref.2
Sequence conflict3281I → V AA sequence Ref.2
Sequence conflict3891T → P in AAP55683. Ref.1
Sequence conflict4121E → Q AA sequence Ref.2
Sequence conflict441 – 4444EWLN → QILK AA sequence Ref.2

Secondary structure

1 ................................................................................. 558
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00366-1 [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

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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: 14659072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ALLOSTERIC REGULATION.
Tissue: Brain.
[2]"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: 4735572] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-558.
Tissue: Liver.
[3]"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: 429360] [Abstract]
Cited for: SEQUENCE REVISION TO 440-441.
[4]"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: 4365183] [Abstract]
Cited for: CHARACTERIZATION.
[5]"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: 4856315] [Abstract]
Cited for: PRELIMINARY STUDIES OF SUBSTRATE-BINDING SITE.
[6]"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: 10425679] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558.
Tissue: Liver.
[7]"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: 11254391] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558 IN COMPLEX WITH SUBSTRATE; NADH AND GTP, CHARACTERIZATION.
[8]"Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation."
Banerjee S.,