[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; PubMed=1552846 [NCBI, ExPASy, EBI, Israel, Japan] Boermann E.R., Eikmanns B.J., Sahm H.; "Molecular analysis of the Corynebacterium glutamicum gdh gene encoding glutamate dehydrogenase."; Mol. Microbiol. 6:317-326(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Guyonvarch A., David F., Leblon G.; Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).

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

X59404; CAA42048.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X72855; CAA51376.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB99472.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927154; CAF20415.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S32227; S32227.

RefSeq

NP_601279.1; -.
YP_226316.1; -.

3D structure databases

HSSP

P24295; 1AUP. [HSSP ENTRY / PDB]

ModBase

P31026.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG2280-MON; -.

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.

BLOCKS

P31026.

Genome annotation databases

GeneID

1020031; -.
3343980; -.

GenomeReviews

BX927147_GR; cg2280.
BA000036_GR; Cgl2079.

KEGG

cgb:cg2280; -.
cgl:NCgl1999; -.

Phylogenomic databases

HOGENOM

P31026; -.

Genome annotation databases

CMR

P31026; Cgl2079.

Other

ProtoNet

P31026.

UniRef

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

Keywords

Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 447`	`447`	`NADP-specific glutamate dehydrogenase.`	`PRO_0000182768`
`ACT_SITE`	`128 128`		`By similarity.`
`CONFLICT`	`37 37`		`I -> L (in Ref. 1; CAA42048).`
`CONFLICT`	`371 410`		`ANAGGVATSALEMQQNASRDSWSFEYTDERLQVIMKNIFK -> TPEAVEVFRERDIRFGPGKAVNVGGVATSALEMQQNASRE (in Ref. 1).`

Sequence information

Length: 447 AA [This is the length of the unprocessed precursor]

Molecular weight: 48988 Da [This is the MW of the unprocessed precursor]

CRC64: 0338926EA7080E35 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVDEQVSNY YDMLLKRNAG EPEFHQAVAE VLESLKIVLE KDPHYADYGL IQRLCEPERQ 

        70         80         90        100        110        120 
LIFRVPWVDD QGQVHVNRGF RVQFNSALGP YKGGLRFHPS VNLGIVKFLG FEQIFKNSLT 

       130        140        150        160        170        180 
GLPIGGGKGG SDFDPKGKSD LEIMRFCQSF MTELHRHIGE YRDVPAGDIG VGGREIGYLF 

       190        200        210        220        230        240 
GHYRRMANQH ESGVLTGKGL TWGGSLVRTE ATGYGCVYFV SEMIKAKGES ISGQKIIVSG 

       250        260        270        280        290        300 
SGNVATYAIE KAQELGATVI GFSDSSGWVH TPNGVDVAKL REIKEVRRAR VSVYADEVEG 

       310        320        330        340        350        360 
ATYHTDGSIW DLKCDIALPC ATQNELNGEN AKTLADNGCR FVAEGANMPS TPEAVEVFRE 

       370        380        390        400        410        420 
RDIRFGPGKA ANAGGVATSA LEMQQNASRD SWSFEYTDER LQVIMKNIFK TCAETAAEYG 

       430        440 
HENDYVVGAN IAGFKKVADA MLAQGVI

P31026 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