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Reviewed, UniProtKB/Swiss-Prot Q99VD0 (DHE2_STAAM)

Last modified January 19, 2010. Version 53. 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:
    NAD-specific glutamate dehydrogenase
      Short name=NAD-GDH
    EC=1.4.1.2
Gene names
Name: gluD
Synonyms: gudB
Ordered Locus Names: SAV0958
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Sequence similarities

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

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular amino 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 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414NAD-specific glutamate dehydrogenase
PRO_0000223327

Sites

Active site1061 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99VD0-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F79290751F6312C7

FASTA41445,760
        10         20         30         40         50         60 
MTENNNLVTS TQGIIKEALH KLGFDEGMYD LIKEPLRMLQ VRIPVRMDDG TVKTFTGYRA 

        70         80         90        100        110        120 
QHNDAVGPTK GGVRFHPDVD EEEVKALSMW MTLKCGIVNL PYGGGKGGIV CDPRQMSIHE 

       130        140        150        160        170        180 
VERLSRGYVR AISQFVGPNK DIPAPDVFTN SQIMAWMMDE YSALDKFNSP GFITGKPIVL 

       190        200        210        220        230        240 
GGSHGRDRST ALGVVIAIEQ AAKRRNMQIE GAKVVIQGFG NAGSFLAKFL YDLGAKIVGI 

       250        260        270        280        290        300 
SDAYGALHDP NGLDIDYLLD RRDSFGTVTN LFEETISNKE LFELDCDILV PAAISNQITE 

       310        320        330        340        350        360 
DNAHDIKASI VVEAANGPTT PEATRILTER GILLVPDVLA SAGGVTVSYF EWVQNNQGYY 

       370        380        390        400        410 
WSEEEVNEKL REKLEAAFDT IYELSQNRKI DMRLAAYIIG IKRTAEAARY RGWA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB57120.1.
RefSeqNP_371482.1.

3D structure databases

SMRQ99VD0. Positions 7-414.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99VD0.

2-D gel databases

World-2DPAGE0002:Q99VD0.

Genome annotation databases

GeneID1120933.
GenomeReviewsGene locus SAV0958 in contig BA000017_GR.
KEGGsav:SAV0958.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHBG590661.
OMAREMAWMM.

Enzyme and pathway databases

BioCycSAUR158878:SAV0958-MONOMER.

Family and domain databases

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]
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.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHE2_STAAM
AccessionPrimary (citable) accession number: Q99VD0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: June 1, 2001
Last modified: January 19, 2010
This is version 53 of the entry and version 1 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