NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Horst H39;
DOI=10.1007/s004380050084; PubMed=8602149 [NCBI, ExPASy, EBI, Israel, Japan]
Schaap P.J., Mueller Y., Baars J.J.P., Op den Camp H.J.M., Sonnenberg A.S.M., van Griensven L.J.L.D., Visser J.;
"Nucleotide sequence and expression of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) from Agaricus bisporus.";
Mol. Gen. Genet. 250:339-347(1996).

Comments

CATALYTIC ACTIVITY: L-glutamate + H₂O + NADP⁺ = 2-oxoglutarate + NH₃ + NADPH.
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

X83393; CAA58312.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S63608; S63608.

3D structure databases

HSSP

P24295; 1AUP. [HSSP ENTRY / PDB]

ModBase

P54387.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004354;	Molecular function: glutamate dehydrogenase (NADP+) 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

ProtoNet

P54387.

UniRef

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

Keywords

NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 457`	`457`	`NADP-specific glutamate dehydrogenase.`	`PRO_0000182783`
`ACT_SITE`	`111 111`		`By similarity.`

Sequence information

Length: 457 AA [This is the length of the unprocessed precursor]

Molecular weight: 49557 Da [This is the MW of the unprocessed precursor]

CRC64: 1BF0E97F67078AC4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLPHEPEFE QALHELETSL QPFLTTNPQY KKALEIIQVP ERVLQFRVTW EDDQGKPQVN 

        70         80         90        100        110        120 
RGFRVQYNSA LGPYKGGLRL HPTVNLSILK FLGFEQTFKN ALTGLSMGGG KGGSDFDPKG 

       130        140        150        160        170        180 
KSDNEIRRFC VAFMSELFRH IGQDTDVPAG DIGTGAREIG FLFGAYRRLK NEFTGMLTGK 

       190        200        210        220        230        240 
GINWGGSFIR PEATGYGLIY YVEHMIAHAC PEYSLDRPST LVAISGSGNV SQFTALKVIE 

       250        260        270        280        290        300 
LGATVLSLSD SKGSLISEKG YTKEAIEKIA ELKLKGGALE AIVDDLGAGY TYHAGKRPWT 

       310        320        330        340        350        360 
LLPQVHIALP GATQNEVSQE EAEALVKAGT RIVAEGSNMG CTEEAIAIFE NSRRASRAGV 

       370        380        390        400        410        420 
WYAPGKASNC GGVAVSGLEM AQNSQRLAWS TQEVDAKLKS IMAECYQICY TAGSRWSGEK 

       430        440        450 
VAEGVAEGEA LPSLLSGANL AGFIKVADAM KEQGDWW

P54387 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