[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Borges K.M., Diruggiero J., Robb F.T.; "Cloning and sequencing of glutamate dehydrogenases from hyperthermophilic archaea."; Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 2-21, AND SUBCELLULAR LOCATION. STRAIN=DSM 5473; PubMed=8135516 [NCBI, ExPASy, EBI, Israel, Japan] Ma K., Robb F.T., Adams M.W.W.; "Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis."; Appl. Environ. Microbiol. 60:562-568(1994).
[3]	SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1006/jmbi.1999.3205; PubMed=10547290 [NCBI, ExPASy, EBI, Israel, Japan] Britton K.L., Yip K.S.P., Sedelnikova S.E., Stillman T.J., Adams M.W.W., Ma K., Maeder D.L., Robb F.T., Tolliday N., Vetriani C., Rice D.W., Baker P.J.; "Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus."; J. Mol. Biol. 293:1121-1132(1999).

Comments

CATALYTIC ACTIVITY: L-glutamate + H₂O + NAD(P)⁺ = 2-oxoglutarate + NH₃ + NAD(P)H.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8.0;
Temperature dependence: Optimum temperature is above 95 degrees Celsius;
SUBUNIT: Homohexamer.
SUBCELLULAR LOCATION: Cytoplasm.
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

L19995; AAA72393.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1BVU; X-ray; 2.50 A; A/B/C/D/E/F=1-419.

[ExPASy / RCSB / EBI]

PDBsum

1BVU; -.

ModBase

Q56304.

Ontologies

GO:0004353;	Molecular function: glutamate dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from EC).
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.
IPR014362; Glu_DHase.
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.

PIRSF

PIRSF000185; Glu_DH; 1.

PRINTS

PR00082; GLFDHDRGNASE.

PROSITE

PS00074; GLFV_DEHYDROGENASE; 1.

Other

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

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 419`	`418`	`Glutamate dehydrogenase.`	`PRO_0000182762`
`NP_BIND`	`219 225`	`7`	`NAD (Potential).`
`ACT_SITE`	`105 105`		`By similarity.`
`HELIX`	`5 18`	`14`
`HELIX`	`25 30`	`6`
`STRAND`	`35 45`	`11`
`STRAND`	`51 62`	`12`
`STRAND`	`66 69`	`4`
`STRAND`	`72 75`	`4`
`HELIX`	`80 97`	`18`
`STRAND`	`102 110`	`9`
`HELIX`	`112 114`	`3`
`HELIX`	`117 131`	`15`
`HELIX`	`132 134`	`3`
`TURN`	`137 139`	`3`
`HELIX`	`150 164`	`15`
`HELIX`	`170 173`	`4`
`STRAND`	`174 176`	`3`
`HELIX`	`179 181`	`3`
`HELIX`	`190 205`	`16`
`STRAND`	`214 218`	`5`
`HELIX`	`222 235`	`14`
`STRAND`	`238 243`	`6`
`STRAND`	`248 250`	`3`
`HELIX`	`257 267`	`11`
`STRAND`	`268 270`	`3`
`STRAND`	`277 279`	`3`
`HELIX`	`281 286`	`6`
`STRAND`	`290 294`	`5`
`HELIX`	`303 306`	`4`
`STRAND`	`312 315`	`4`
`STRAND`	`318 320`	`3`
`HELIX`	`324 333`	`10`
`STRAND`	`336 338`	`3`
`HELIX`	`340 343`	`4`
`HELIX`	`346 360`	`15`
`HELIX`	`366 391`	`26`
`HELIX`	`395 414`	`20`

Sequence information

Length: 419 AA [This is the length of the unprocessed precursor]

Molecular weight: 46740 Da [This is the MW of the unprocessed precursor]

CRC64: 2768747A590B71F6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEQDPFEIA VKQLERAAQY MDISEEALEF LKRPQRIVEV SIPVEMDDGS VKVFTGFRVQ 

        70         80         90        100        110        120 
YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGVIC NPKEMSDREK 

       130        140        150        160        170        180 
ERLARGYVRA IYDVISPYTD IPAPDVYTNP QIMAWMMDEY ETISRRKDPS FGVITGKPPS 

       190        200        210        220        230        240 
VGGIVARMDA TARGASYTVR EAAKALGMDL KGKTIAIQGY GNAGYYMAKI MSEEYGMKVV 

       250        260        270        280        290        300 
AVSDTKGGIY NPDGLNADEV LAWKKKTGSV KDFPGATNIT NEELLELEVD VLAPSAIEEV 

       310        320        330        340        350        360 
ITKKNADNIK AKIVAELANG PTTPEADEIL YEKGILIIPD FLCNAGGVTV SYFEWVQNIT 

       370        380        390        400        410 
GDYWTVEETR AKLDKKMTKA FWDVYNTHKE KNINMRDAAY VVAVSRVYQA MKDRGWIKK

Q56304 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