NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 76518 / CBS 7001 / NCYC 623 / NRRL Y-11845;
Nguyen H.V.;
"New S. pastorianus strains and Saccharomyces natural hybrids revealed by polyphasis identification of CBS strains formerly uncompletely identified by conventional method.";
Submitted (OCT-2001) 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

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ418037; CAD10750.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P24295; 1AUP. [HSSP ENTRY / PDB]

ModBase

Q8TFF6.

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.

ProtoNet

Q8TFF6.

Other

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`	`1 454`	`454`	`NADP-specific glutamate dehydrogenase 1.`	`PRO_0000182797`
`NP_BIND`	`174 203`	`30`	`NAD (By similarity).`
`ACT_SITE`	`110 110`		`By similarity.`

Sequence information

Length: 454 AA [This is the length of the unprocessed precursor]

Molecular weight: 49425 Da [This is the MW of the unprocessed precursor]

CRC64: 98DF52A68BDE0D12 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEPEFQQAY DEVVSSLEDS TLFEQHPKYR KVLPIVSVPE RIIQFRVTWE NDKGEQEVAQ 

        70         80         90        100        110        120 
GYRVQYNSAK GPYKGGLRFH PSVNLSILKF LGFEQIFKNS LTGLDMGGGK GGLCVDLKGR 

       130        140        150        160        170        180 
SNNEIRRICY AFMRELSRHI GQDTDVPAGD IGVGGREIGY LFGAYRTYKN SWEGVLTGKG 

       190        200        210        220        230        240 
LNWGGSLIRP EATGYGLVYY TQAMIDYATN GKESFEGKRV TISGSGNVAQ FAALKVIELG 

       250        260        270        280        290        300 
GTVVSLSDSK GCIISETGIT SEQVADISSA KVNFKSLEQI VGEYSTFTEN KVQYISGARP 

       310        320        330        340        350        360 
WTHVQKVDIA LPCATQNEVS GDEAKALVAQ GVKFVAEGSN MGSTPEAIAV FETARATAST 

       370        380        390        400        410        420 
LKESVWYGPP KAANLGGVAV SGLEMAQNSQ RITWSSERVD QELKKIMVNC FNECIDSAKK 

       430        440        450 
YTKEGNALPS LVKGANIASF IKVSDAMFDQ GDVF

Q8TFF6 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