[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ALLOSTERIC REGULATION. TISSUE=Brain; PubMed=14659072 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase."; J. Biochem. Mol. Biol. 36:545-551(2003).
[2]	PROTEIN SEQUENCE OF 58-558. TISSUE=Liver; PubMed=4735572 [NCBI, ExPASy, EBI, Israel, Japan] Moon K., Smith E.L.; "Sequence of bovine liver glutamate dehydrogenase. 8. Peptides produced by specific chemical cleavages; the complete sequence of the protein."; J. Biol. Chem. 248:3082-3088(1973).
[3]	SEQUENCE REVISION TO 440-441. PubMed=429360 [NCBI, ExPASy, EBI, Israel, Japan] Julliard J.H., Smith E.L.; "Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme."; J. Biol. Chem. 254:3427-3438(1979).
[4]	CHARACTERIZATION. PubMed=4365183 [NCBI, ExPASy, EBI, Israel, Japan] Witzemann V., Koberstein R., Sund H., Rasched I., Joernvall H., Noack K.; "Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues."; Eur. J. Biochem. 43:319-325(1974).
[5]	PRELIMINARY STUDIES OF SUBSTRATE-BINDING SITE. PubMed=4856315 [NCBI, ExPASy, EBI, Israel, Japan] Rasched I., Joernvall H., Sund H.; "Studies of glutamate dehydrogenase. Identification of an amino group involved in the substrate binding."; Eur. J. Biochem. 41:603-606(1974).
[6]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558. TISSUE=Liver; DOI=10.1016/S0969-2126(99)80101-4; PubMed=10425679 [NCBI, ExPASy, EBI, Israel, Japan] Peterson P.E., Smith T.J.; "The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery."; Structure 7:769-782(1999).
[7]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558 IN COMPLEX WITH SUBSTRATE; NADH AND GTP, AND CHARACTERIZATION. DOI=10.1006/jmbi.2001.4499; PubMed=11254391 [NCBI, ExPASy, EBI, Israel, Japan] Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.; "Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation."; J. Mol. Biol. 307:707-720(2001).
[8]	X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-520 ALONE AND IN COMPLEX WITH ADP, AND HOMOHEXAMERIZATION. DOI=10.1021/bi0206917; PubMed=12653548 [NCBI, ExPASy, EBI, Israel, Japan] Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.; "Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation."; Biochemistry 42:3446-3456(2003).

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 + 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: Homohexamer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY138843; AAN15276.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY256856; AAP55683.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A92129; DEBOE.

NP_872593.1; -.

3D structure databases

PDB

1HWX; X-ray; 2.50 A; A/B/C/D/E/F=58-558.	[ExPASy / RCSB / EBI]
1HWY; X-ray; 3.20 A; A/B/C/D/E/F=58-558.	[ExPASy / RCSB / EBI]
1HWZ; X-ray; 2.80 A; A/B/C/D/E/F=58-558.	[ExPASy / RCSB / EBI]
1NQT; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=63-558.	[ExPASy / RCSB / EBI]
1NR7; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=63-558.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1HWX; -.
1HWY; -.
1HWZ; -.
1NQT; -.
1NR7; -.

ModBase

P00366.

Protein-protein interaction databases

IntAct

P00366; -.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from sequence or structural similarity from AgBase).
GO:0004353;	Molecular function: glutamate dehydrogenase [NAD(P)+] activity (inferred from sequence or structural similarity from AgBase).
GO:0004352;	Molecular function: glutamate dehydrogenase activity (inferred from sequence or structural similarity from AgBase).
GO:0006538;	Biological process: glutamate catabolic process (inferred from sequence or structural similarity from AgBase).
QuickGo view.

Family and domain databases

InterPro

IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR11606:SF2; GLFV_DH; 1.

Pfam

PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00082; GLFDHDRGNASE.

PROSITE

PS00074; GLFV_DEHYDROGENASE; 1.

BLOCKS

P00366.

Genome annotation databases

Ensembl

ENSBTAG00000007540; Bos taurus. [Contig view]

GeneID

281785; -.

KEGG

bta:281785; -.

Phylogenomic databases

HOVERGEN

P00366; -.

Other

P00366; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; ATP-binding; Direct protein sequencing; GTP-binding; Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase; Phosphoprotein; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 57`	`57`	`Mitochondrion.`
`CHAIN`	`58 558`	`501`	`Glutamate dehydrogenase 1, mitochondrial.`	`PRO_0000007205`
`NP_BIND`	`141 143`	`3`	`NAD.`
`ACT_SITE`	`183 183`
`BINDING`	`147 147`		`Substrate.`
`BINDING`	`171 171`		`Substrate.`
`BINDING`	`176 176`		`NAD.`
`BINDING`	`252 252`		`NAD.`
`BINDING`	`266 266`		`GTP.`
`BINDING`	`270 270`		`GTP.`
`BINDING`	`319 319`		`GTP.`
`BINDING`	`322 322`		`GTP.`
`BINDING`	`438 438`		`Substrate.`
`BINDING`	`444 444`		`NAD.`
`BINDING`	`450 450`		`ADP.`
`BINDING`	`516 516`		`ADP.`
`MOD_RES`	`84 84`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`135 135`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`227 227`		`Phosphoserine (By similarity).`
`MOD_RES`	`503 503`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`512 512`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`527 527`		`N6-acetyllysine (By similarity).`
`CONFLICT`	`93 95`		`ETE -> QTQ (in Ref. 2; AA sequence).`
`CONFLICT`	`104 104`		`S -> G (in Ref. 2; AA sequence).`
`CONFLICT`	`141 142`		`QH -> HQ (in Ref. 2; AA sequence).`
`CONFLICT`	`196 197`		`NE -> ED (in Ref. 2; AA sequence).`
`CONFLICT`	`225 225`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`257 259`		`GKP -> KPG (in Ref. 2; AA sequence).`
`CONFLICT`	`278 279`		`HG -> GH (in Ref. 2; AA sequence).`
`CONFLICT`	`305 305`		`V -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`328 328`		`I -> V (in Ref. 2; AA sequence).`
`CONFLICT`	`389 389`		`T -> P (in Ref. 1; AAP55683).`
`CONFLICT`	`412 412`		`E -> Q (in Ref. 2; AA sequence).`
`CONFLICT`	`441 444`		`EWLN -> QILK (in Ref. 2; AA sequence).`
`HELIX`	`66 87`	`22`
`HELIX`	`97 109`	`13`
`STRAND`	`113 123`	`11`
`STRAND`	`125 127`	`3`
`STRAND`	`129 138`	`10`
`STRAND`	`142 152`	`11`
`HELIX`	`158 174`	`17`
`STRAND`	`180 186`	`7`
`HELIX`	`190 192`	`3`
`HELIX`	`195 211`	`17`
`TURN`	`217 219`	`3`
`STRAND`	`220 223`	`4`
`HELIX`	`230 241`	`12`
`HELIX`	`244 247`	`4`
`HELIX`	`251 254`	`4`
`HELIX`	`260 262`	`3`
`HELIX`	`268 284`	`17`
`HELIX`	`287 293`	`7`
`STRAND`	`297 299`	`3`
`STRAND`	`303 307`	`5`
`HELIX`	`311 322`	`12`
`STRAND`	`326 332`	`7`
`STRAND`	`335 337`	`3`
`HELIX`	`345 353`	`9`
`STRAND`	`356 358`	`3`
`HELIX`	`371 373`	`3`
`STRAND`	`377 381`	`5`
`STRAND`	`383 386`	`4`
`TURN`	`390 392`	`3`
`HELIX`	`393 395`	`3`
`STRAND`	`399 402`	`4`
`STRAND`	`405 407`	`3`
`HELIX`	`411 419`	`9`
`STRAND`	`423 425`	`3`
`HELIX`	`427 430`	`4`
`HELIX`	`433 447`	`15`
`TURN`	`451 455`	`5`
`HELIX`	`456 477`	`22`
`TURN`	`478 482`	`5`
`HELIX`	`491 496`	`6`
`HELIX`	`502 527`	`26`
`HELIX`	`534 552`	`19`

Sequence information

Length: 558 AA [This is the length of the unprocessed precursor]

Molecular weight: 61512 Da [This is the MW of the unprocessed precursor]

CRC64: 194D74A33F2310E7 [This is a checksum on the sequence]

        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

P00366 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools