NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-448, AND CHARACTERIZATION.
PubMed=10601858 [NCBI, ExPASy, EBI, Israel, Japan]
Di Fraia R., Wilquet V., Ciardiello M.A., Carratore V., Antignani A., Camardella L., Glansdorff N., Di Prisco G.;
"NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases.";
Eur. J. Biochem. 267:121-131(2000).

Comments

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

AJ010746; CAB54142.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P24295; 1AUP. [HSSP ENTRY / PDB]

ModBase

Q9S1F9.

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

Q9S1F9.

UniRef

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

Keywords

Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 448`	`447`	`NADP-specific glutamate dehydrogenase.`	`PRO_0000182774`
`ACT_SITE`	`124 124`		`By similarity.`

Sequence information

Length: 448 AA [This is the length of the unprocessed precursor]

Molecular weight: 49448 Da [This is the MW of the unprocessed precursor]

CRC64: EE24FEA463DCB660 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSISKAIEKV EARYAHQPEF IQAVKEVAIT IKPLYDAHPE YDKLKVFERL VEPDRVFGFR 

        70         80         90        100        110        120 
VNWEDDNGEI QINRGWRVQF SNALGPYKGG LRFHPTVNQS VLKFLGFEQI FKNALTGLPI 

       130        140        150        160        170        180 
GGGKGGSDFD PKGKTDSEIR RFCYAFMREL HHYVNKDMDV PAGDIGVGGR EVSYMFAMYK 

       190        200        210        220        230        240 
NLTRESTGVI TGKGVGFGGS LMRTEATGYG AVYFLQNMLA AQNESIEGKK VLVSGAGNVS 

       250        260        270        280        290        300 
LHAAEKATLI GAIVLTVSDS KGTIYDAKGL NQEKIDWLKV QKDQHKPLAD YVEVFGGEWM 

       310        320        330        340        350        360 
ADQKPWSIKA DIAIPSATQN EINEEDAKLL VDNGVKYIVE GANMPLTAEA IDYIRLHRVH 

       370        380        390        400        410        420 
YAPGKAANAG GVAVSALEMS QNSVRQYQTF EQVDERLQGI MKDIHDSSAQ ASEMYGQTDE 

       430        440 
GYIDYMSGAN MVGFKRVADA LVAFGILN

Q9S1F9 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