[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1917850 [NCBI, ExPASy, EBI, Israel, Japan] Snedecor B., Chu H., Chen E.Y.; "Selection, expression, and nucleotide sequencing of the glutamate dehydrogenase gene of Peptostreptococcus asaccharolyticus."; J. Bacteriol. 173:6162-6167(1991).

Comments

CATALYTIC ACTIVITY: L-glutamate + H₂O + NAD⁺ = 2-oxoglutarate + NH₃ + NADH.
PATHWAY: Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 1/5 .
SUBUNIT: Homohexamer.
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

M76403; AAA25611.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A38168; A38168.

3D structure databases

HSSP

O74024; 1EUZ. [HSSP ENTRY / PDB]

ModBase

P28997.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-1161; -.

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

NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 421`	`421`	`NAD-specific glutamate dehydrogenase.`	`PRO_0000182739`
`ACT_SITE`	`106 106`		`By similarity.`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 46514 Da [This is the MW of the unprocessed precursor]

CRC64: DDA64241C027422C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDTLNPLVA AQEKVRIACE KLGCDPAVYE LLKEPQRVIE ISIPVKMDDG TVKVFKGWRS 

        70         80         90        100        110        120 
AHSSAVGPSK GGVRFHPNVN MDEVKALSLW MTFKGGALGL PYGGGKGGIC VDPAELSERE 

       130        140        150        160        170        180 
LEQLSRGWVR GLYKYLGDRI DIPAPDVNTN GQIMSWFVDE YVKLNGERMD IGTFTGKPVA 

       190        200        210        220        230        240 
FGGSEGRNEA TGFGVAVVVR ESAKRFGIKM EDAKIAVQGF GNVGTFTVKN IERQGGKVCA 

       250        260        270        280        290        300 
IAEWDRNEGN YALYNENGID FKELLAYKEA NKTLIGFPGA ERITDEEFWT KEYDIIVPAA 

       310        320        330        340        350        360 
LENVITGERA KTINAKLVCE AANGPTTPEG DKVLTERGIN LTPDILTNSG GVLVSYYEWV 

       370        380        390        400        410        420 
QNQYGYYWTE AEVEEKQEAD MMKAIKGVFA VADEYNVTLR EAVYMYAIKS IDVAMKLRGW 


Y

P28997 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