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P94598 (DHE3_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. 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:
Glutamate dehydrogenase

Short name=GDH
EC=1.4.1.3
Alternative name(s):
NAD(P)H-utilizing glutamate dehydrogenase
Gene names
Name:gdhA
Ordered Locus Names:BT_1970
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

Sequence caution

The sequence AAB40143.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglutamate dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Glutamate dehydrogenase
PRO_0000182766

Sites

Active site1241 By similarity

Sequences

Sequence LengthMass (Da)Tools
P94598 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 6563EB81F0746095

FASTA44449,017
        10         20         30         40         50         60 
MNAAKVLDDL KRRFPNEPEY HQAVEEVLST IEEEYNKHPE FDKANLIERL CIPDRVFQFR 

        70         80         90        100        110        120 
VTWMDDKGNI QTNMGYRVQH NNAIGPYKGG IRFHASVNLS ILKFLAFEQT FKNSLTTLPM 

       130        140        150        160        170        180 
GGGKGGSDFS PRGKSNAEVM RFVQAFMLEL WRHIGPETDV PAGDIGVGGR EVGFMFGMYK 

       190        200        210        220        230        240 
KLAHEFTGTF TGKGREFGGS LIRPEATGYG NIYFLMEMLK TKGTDLKGKV CLVSGSGNVA 

       250        260        270        280        290        300 
QYTIEKVIEL GGKVVTCSDS DGYIYDPDGI DREKLDYIME LKNLYRGRIR EYAEKYGCKY 

       310        320        330        340        350        360 
VEGAKPWGEK CDIALPSATQ NELNGDHARQ LVANGCIAVS EGANMPSTPE AVRVFQDAKI 

       370        380        390        400        410        420 
LYAPGKAANA GGVSVSGLEM TQNSIKLSWS AEEVDEKLKS IMKNIHEACV QYGTEADGYV 

       430        440 
NYVKGANVAG FMKVAKAMMA QGIV 

« Hide

References

« Hide 'large scale' references
[1]"The NAD(P)H-utilizing glutamate dehydrogenase of Bacteroides thetaiotaomicron belongs to enzyme family I, and its activity is affected by trans-acting gene(s) positioned downstream of gdhA."
Baggio L., Morrison M.
J. Bacteriol. 178:7212-7220(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[2]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82241 Genomic DNA. Translation: AAB40143.1. Different initiation.
AE015928 Genomic DNA. Translation: AAO77077.1.
RefSeqNP_810883.1. NC_004663.1.

3D structure databases

ProteinModelPortalP94598.
SMRP94598. Positions 4-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_1970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO77077; AAO77077; BT_1970.
GeneID1076144.
KEGGbth:BT_1970.
PATRIC21058859. VBIBacThe70966_2018.

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHOG000243799.
KOK00262.
OMATANEYEV.
OrthoDBEOG65XN4D.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-2009-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 nameDHE3_BACTN
AccessionPrimary (citable) accession number: P94598
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 94 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