[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CCM 2090 / JCM 9120; DOI=10.1007/BF00280290; PubMed=1766432 [NCBI, ExPASy, EBI, Israel, Japan] Benachenhou N., Baldacci G.; "The gene for a halophilic glutamate dehydrogenase: sequence, transcription analysis and phylogenetic implications."; Mol. Gen. Genet. 230:345-352(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NRC-36014; DOI=10.1016/j.gene.2005.01.011; PubMed=15780999 [NCBI, ExPASy, EBI, Israel, Japan] Ingoldsby L.M., Geoghegan K.F., Hayden B.M., Engel P.C.; "The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum."; Gene 349:237-244(2005).
[3]	PROTEIN SEQUENCE OF 119-128; 184-193 AND 268-276, AND CHARACTERIZATION. DOI=10.1111/j.1574-6968.2002.tb11200.x; PubMed=12052548 [NCBI, ExPASy, EBI, Israel, Japan] Hayden B.M., Bonete M.J., Brown P.E., Moir A.J., Engel P.C.; "Glutamate dehydrogenase of Halobacterium salinarum: evidence that the gene sequence currently assigned to the NADP+-dependent enzyme is in fact that of the NAD+-dependent glutamate dehydrogenase."; FEMS Microbiol. Lett. 211:37-41(2002).

Comments

CATALYTIC ACTIVITY: L-glutamate + H₂O + NAD⁺ = 2-oxoglutarate + NH₃ + NADH.
SUBUNIT: Homohexamer (By similarity).
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

X63837; CAA45327.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY840088; AAW19068.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18609; S18609.

3D structure databases

HSSP

P96110; 1B26. [HSSP ENTRY / PDB]

ModBase

P29051.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-741; -.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004352;	Molecular function: glutamate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0006520;	Biological process: amino acid metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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

Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 435`	`435`	`NAD-specific glutamate dehydrogenase A.`	`PRO_0000182779`
`ACT_SITE`	`126 126`		`By similarity.`

Sequence information

Length: 435 AA [This is the length of the unprocessed precursor]

Molecular weight: 47459 Da [This is the MW of the unprocessed precursor]

CRC64: 0E4E940D2FF8B9D2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTMASKSDST HDESGDEAAD STEPESALET ARRQLYHAAS YLDIDQNIVE RLKYPKKVHE 

        70         80         90        100        110        120 
VTIPIERDDG TVEVFTGYRA QHDSVRGPYK GGLRYHPDVT RDECVGLGMW MTWKCAVMDL 

       130        140        150        160        170        180 
PFGGAKGGVA VNPKELSPEE KERLTRRFTQ EIRDVIGPNQ DIPAPDMGTD PQTMAWLMDA 

       190        200        210        220        230        240 
YSMQEGETTP GVVTGKPPVV GGSEGREEAP GRSVAIITQL VCEYYDQPLD ETTVAVQGYG 

       250        260        270        280        290        300 
SVGANAARLL DKWGATIVAI SDVNGAMYEP DGIDTASVPS HDEEPEAVTT YADTVISNEE 

       310        320        330        340        350        360 
LLTLDVDVLI PAALGNVITK ENAEAIAADL VVEGANGPTT STADSILADR DVAVIPDILA 

       370        380        390        400        410        420 
NAGGVTVSYF EWLQDINRRA WSLERVNDEL EAEMQAAWRA VKDEYENRDV TWRDAAYIVA 

       430 
LSRIAEAHEA RGLWP

P29051 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