[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=2850; Santos M.; "Cloning and regulation of the gdhA gene from Botrytis cinerea."; Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.

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

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Cross-references

Sequence databases

EMBL

AF109684; AAC95390.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P24295; 1AUP. [HSSP ENTRY / PDB]

ModBase

O93934.

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

O93934.

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`	`1 450`	`450`	`NADP-specific glutamate dehydrogenase.`	`PRO_0000182784`
`ACT_SITE`	`114 114`		`By similarity.`

Sequence information

Length: 450 AA [This is the length of the unprocessed precursor]

Molecular weight: 49044 Da [This is the MW of the unprocessed precursor]

CRC64: 6EDAFAB75B03C93A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNLPSEPEF EQAYNELAST LENSTLFEKN PEYRTALKVV SIPERVIQFR VVWEDDKNQV 

        70         80         90        100        110        120 
QVNRGYRVQF NSALGPYKGG LRFHPTVNLS VLKFLGFEQI FKNALTGLNI GGGKGGADFD 

       130        140        150        160        170        180 
PKGKSDNEIR RFCVSFMREL SKHIGADTDV PAGDINVGGR EIGFLFGAYK AIQNKWEGVL 

       190        200        210        220        230        240 
TGKGGSWGGS LIRPEATGYG LVYYVAHMIQ YAGQGSFQGK RVAISGSGNV AQYAALKCIE 

       250        260        270        280        290        300 
LGATVVSLSD SQGSLIAEGD AYFTPEDVGK IAELKLKRQS LTAFEHGGKY KYIEGSRPWT 

       310        320        330        340        350        360 
HVKVDVALPC ATQNEVSKEE AESLVASGAR YIAEGSNMGC TQEAIDVFEA ERKEKKDKAI 

       370        380        390        400        410        420 
WYAPGKAANA GGVAVSGLEM AQNSARISWT QEEVDEKLKD IMKNAFETGL ETPKKYVEAK 

       430        440        450 
DGEYPSLVAG SNIAGFVKVA SAMHNHGDWW

O93934 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