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Reviewed, UniProtKB/Swiss-Prot P41755 (DHE2_ACHKL)

Last modified November 4, 2008. Version 30. 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
OrganismAchlya klebsiana
Taxonomic identifier4767 [NCBI]
Taxonomic lineageEukaryotastramenopilesOomycetesSaprolegnialesSaprolegniaceaeAchlya

Protein attributes

Sequence length1063 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(+) = 2-oxoglutarate + NH(3) + NADH.

Enzyme regulation

Allosterically activated by NADP(+).

Subunit structure

Homotetramer.

Sequence similarities

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

Ontologies

Keywords

   LigandNAD
   Molecular functionOxidoreductase
   Technical termAllosteric enzyme

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglutamate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10631063NAD-specific glutamate dehydrogenase
PRO_0000182731

Sequences

Sequence LengthMass (Da)Tools
P41755-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4EAC1E2C36674860

FASTA1,063118,741
        10         20         30         40         50         60 
MLLCIVLFLI FHILINQAGI VHVLYNASFV ASSSRFILFC EELFKATPQY WQWGNSIVQN 

        70         80         90        100        110        120 
GDASIASTLY LTMRTFIKHW KYTLLIMINQ SISYSCYSTN EASHLLFTNL PKVAPYTLGP 

       130        140        150        160        170        180 
LNFECCLLSS HHIRHIVLMF YGANIDHGLT KYELYTVCRP SSDEKLCNKI LNSPRLHTHN 

       190        200        210        220        230        240 
RYLYLTEVRI VGAFYLIKQV GARMVGLLVH LAFMVLQNLP KLIWPLDLVH VRQKGTCTAH 

       250        260        270        280        290        300 
IAYHPLAQKH FPPYFTHFYL NVTIYAVVKN ILDNISSSFT LQSNRVRPRP DVAGFDFFHR 

       310        320        330        340        350        360 
FDAFEQSLTY GGDTGITSSN EKVALCFEAT YTDIFFTVEI IDSTSVDSGA IMLPILVDAY 

       370        380        390        400        410        420 
TAVARNFCSV SMVISPLVTL VVYDIYTCSF IGLCTQRRTI NCTRILDAIS SVGNSHTFLP 

       430        440        450        460        470        480 
RYKSPRELTT RQPSGSSVIL LIFLLLGFEF FLFSGLVVVE PVNDVGDLVV NDLLVAFIDL 

       490        500        510        520        530        540 
ALELFVVEGV AEVVGVVFKT VLGFNADVVG FIFRLVLFSF LHHAFNIILG EATLVVGNGN 

       550        560        570        580        590        600 
LVFFTSRLFD GRHVQDTVGI NVEGDINLWN TTRHWRNTIE GELPEQVVVT GHRTLTFKHL 

       610        620        630        640        650        660 
NQHTRLVVSV GGESLRLLGW HSSVTLDEGS HDTTSSFQTK RERSDIKKQQ VLELFRRVVT 

       670        680        690        700        710        720 
AQNGSLDCGT ESNSFIRVDR LAWFLAVEEV RKQLLDLWDT GGTTDKDDFM DLALGELRVT 

       730        740        750        760        770        780 
EDLFNRFHSL AEVVTAHVFE TGTGDGGVEI NTIEERVDFN VSLGRRRKST LGTFTSGTKT 

       790        800        810        820        830        840 
AKGTLVLGHI LAVLALEFSG KVVDEAVIEI FTTQVGITSS SLDFEDTFFN GQKRHIEGTT 

       850        860        870        880        890        900 
TKIENENIAF TTLLVKTVGN GGTSRFVNDT KDVKTSNGTS ILGSLTLRVV EISWDGNDSV 

       910        920        930        940        950        960 
VNSSTNEGFS NFLHLDQNHR GNFFRLESLS FTLEFDGDLW LVTSTRGNLE WPVLNIGLSS 

       970        980        990       1000       1010       1020 
WVVEFTTDQT LSIEHSVGRV HGNLVLSGIT NKTFAVSESN VRWGGTVTLI VGNNFNTIVL 

      1030       1040       1050       1060 
PDTDTRISRT EIDTDGSSLD TRHACSKFKN EVDSPPHLTS AFI 

« Hide

References

[1]"Molecular characterization of an NAD-specific glutamate dehydrogenase gene inducible by L-glutamine. Antisense gene pair arrangement with L-glutamine-inducible heat shock 70-like protein gene."
Lejohn H.B., Cameron L.E., Yang B., Rennie S.L.
J. Biol. Chem. 269:4523-4531(1994) [PubMed: 8308022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

U02505 Unassigned DNA. Translation: AAA17563.1.
PIRA53164.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR006095. Glu/Leu/Phe/Val_DHase.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHE2_ACHKL
AccessionPrimary (citable) accession number: P41755
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 4, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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