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P95544 (DHE4_PRERU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 63. 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:
NAD(P)-specific glutamate dehydrogenase

Short name=NAD(P)-GDH
EC=1.4.1.2
EC=1.4.1.3
Alternative name(s):
NAD(P)H-dependent glutamate dehydrogenase
Gene names
Name:gdhA
OrganismPrevotella ruminicola (Bacteroides ruminicola)
Taxonomic identifier839 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPrevotellaceaePrevotella

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. P.ruminicola possess both NADP(H)- and NAD(H)-dependent activities on the same enzyme, suggesting that both anabolic and catabolic forms of the enzyme might occur. Ref.1

Catalytic activity

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.

L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

Ontologies

Keywords
   LigandNAD
NADP
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processglutamate biosynthetic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutamate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamate dehydrogenase [NAD(P)+] activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444NAD(P)-specific glutamate dehydrogenase
PRO_0000182773

Sites

Active site1241Proton donor By similarity
Binding site881Substrate By similarity
Binding site1091Substrate By similarity
Binding site1121Substrate By similarity
Binding site1631Substrate; via carbonyl oxygen By similarity
Binding site2071NADP By similarity
Binding site2381NADP By similarity
Binding site3761Substrate By similarity
Site1641Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P95544 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 32CAD7F278CF06A9

FASTA44448,878
        10         20         30         40         50         60 
MKATEVIEKL KAKFPGQPEY IQAVSQVLGT IEEEYNKHPE FEKANLIERL CVPDRILQFR 

        70         80         90        100        110        120 
VSWVDDNGNV QTNLGYRVQH NNAIGPYKGG LRFHKSVNAS ILKFLAFEQT FKNSLTTLPM 

       130        140        150        160        170        180 
GGAKGGSDFD PHGKSDMEVM RFCQAFMNEL YRLIGPDEDV PAGDIGVGGR EVGYMFGQYK 

       190        200        210        220        230        240 
KLTHQFQGIL TGKGLEFGGS LIRPEATGYG NVYFLEDMLK TRGESLEGKT VLVSGSGNVA 

       250        260        270        280        290        300 
QYTIEKLLQL GAKPVTCSDS NGYIYDPDGI DAEKLAFIME LKNVKRGRIK EYAEKYGVKY 

       310        320        330        340        350        360 
VENARPWGEK ADIATPCATQ DEINEAEAKT LIANGVFAVS EGANMPTEPA AIKVFQDAKI 

       370        380        390        400        410        420 
LYCPGKASNA GGVATSGLEM SQNSERLSWT REEVDTKLHN IMDEIHANCV KYGTEPDGYI 

       430        440 
NYVKGANVAG FMKVAKAMMA QGIY 

« Hide

References

[1]"The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella ruminicola B(1)4 can be attributed to one enzyme (GdhA), and gdhA expression is regulated in response to the nitrogen source available for growth."
Wen Z., Morrison M.
Appl. Environ. Microbiol. 62:3826-3833(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GLUTAMATE DEHYDROGENASE, SUBSTRATE SPECIFICITY.
Strain: B14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82240 Genomic DNA. Translation: AAB40142.1.
PIRT10487.

3D structure databases

ProteinModelPortalP95544.
SMRP95544. Positions 3-444.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP95544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PRERU
AccessionPrimary (citable) accession number: P95544
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: October 16, 2013
This is version 63 of the entry and version 1 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