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Reviewed, UniProtKB/Swiss-Prot P94598 (DHE3_BACTN)

Last modified November 25, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H.

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

Ontologies

Keywords

   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processamino acid metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glutamate dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: 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
P94598-1 [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: 8955404] [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: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

U82241 Genomic DNA. Translation: AAB40143.1. Different initiation.
AE015928 Genomic DNA. Translation: AAO77077.1.
RefSeqNP_810883.1.

3D structure databases

HSSPHSSP built from PDB template 1AUP based on UniProtKB P24295.
ModBaseSearch...

Genome annotation databases

GeneID1076144.
GenomeReviewsGene locus BT_1970 in contig AE015928_GR.
KEGGbth:BT_1970.
NMPDRfig|226186.1.peg.1970.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP94598.

Enzyme and pathway databases

BioCycBTHE226186:BT_1970-MON.

Family and domain databases

InterProIPR006095. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11606:SF2. GLFV_DH. 1 hit.
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
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: November 25, 2008
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents