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Q8RQP4 (DHE4_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADP-specific glutamate dehydrogenase

Short name=NADP-GDH
EC=1.4.1.4
Gene names
Name:gdh
Ordered Locus Names:CE1982
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia By similarity.

Catalytic activity

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

Subunit structure

Homohexamer By similarity.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Sequence caution

The sequence BAC18792.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamate biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutamate dehydrogenase (NADP+) activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447NADP-specific glutamate dehydrogenase
PRO_0000182767

Sites

Active site1281Proton donor By similarity
Binding site921Substrate By similarity
Binding site1131Substrate By similarity
Binding site1161Substrate By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Binding site2121NADP By similarity
Binding site2431NADP By similarity
Binding site3791Substrate By similarity
Site1681Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RQP4 [UniParc].

Last modified November 1, 2002. Version 2.
Checksum: B2B320AAE3EA70A3

FASTA44748,962
        10         20         30         40         50         60 
MTVDEQVSNY YDMLLKRNAG EPEFHQAVAE VLESLKIVLE KDPHYADYGL IQRLCEPERQ 

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

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

       190        200        210        220        230        240 
GHYRRLANQH ESGVLTGKGL TWGGSLVRTE ATGFGTVYFV QEMIKAEGET LEGKKVIVSG 

       250        260        270        280        290        300 
SGNVATYAIQ KVQELGAVVV GFSDSSGWVS TPNGVDVAKL REIKEVRRAR VSSYADEVEG 

       310        320        330        340        350        360 
AEYHTDGSIW DLTADIALPC ATQNELDGDN ARTLADNGCR FVAEGANMPS TPEAIDVFRE 

       370        380        390        400        410        420 
RGVLFGPGKA ANAGGVATSA LEMQQNASRD SWSFEYTDER LHRIMKNIFK SCADTAKEYG 

       430        440 
HEKNYVVGAN IAGFKKVADA MLAQGVI 

« Hide

References

« Hide 'large scale' references
[1]"Corynebacterium efficiens gdh gene encoding glutamate dehydrogenase NADP dependent."
Matsuzaki Y., Kimura E., Nakamura K., Kawahara Y., Sugimoto S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.
[2]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB082375 Genomic DNA. Translation: BAB86838.1.
BA000035 Genomic DNA. Translation: BAC18792.1. Different initiation.
RefSeqNP_738592.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8RQP4.
SMRQ8RQP4. Positions 3-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE1982.

Proteomic databases

PRIDEQ8RQP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18792; BAC18792; BAC18792.
GeneID1032052.
KEGGcef:CE1982.
PATRIC21490097. VBICorEff9312_1963.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000243799.
KOK00262.
OrthoDBEOG65XN4D.
ProtClustDBPRK09414.

Enzyme and pathway databases

BioCycCEFF196164:GJW8-2018-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHE4_COREF
AccessionPrimary (citable) accession number: Q8RQP4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: November 13, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families