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Q54KB7 (DHE3_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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, mitochondrial
Short name=GDH
EC=1.4.1.3
Gene names
Name:gluD
ORF Names:DDB_G0287469
OrganismDictyostelium discoideum (Slime mold)
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Subject to allosteric regulation. Activated by AMP and ADP. Ref.2 Ref.3

Subunit structure

Homohexamer. Ref.2

Subcellular location

Mitochondrion matrix By similarity.

Miscellaneous

ADP can occupy the NADH binding site and activate the enzyme By similarity.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.36 mM for alpha-ketoglutarate Ref.2

KM=16 µM for NADH

KM=34.5 mM for NH3

pH dependence:

Optimum pH is 7.25 to 7.5.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
NAD
Nucleotide-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglutamate catabolic process

Inferred from sequence or structural similarity. Source: dictyBase

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle

Inferred from direct assay. Source: dictyBase

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate dehydrogenase [NAD(P)+] activity

Inferred from sequence or structural similarity. Source: dictyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 502Glutamate dehydrogenase, mitochondrialPRO_0000327666

Regions

Nucleotide binding96 – 983NAD By similarity

Sites

Active site1381 By similarity
Binding site1021Substrate By similarity
Binding site1261Substrate By similarity
Binding site1311NAD By similarity
Binding site3941Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q54KB7 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: D6BB324A859C0528

FASTA50255,042
        10         20         30         40         50         60 
MQSLARLSRT SLVQKGLVPQ TIKNYSSVSQ AEIDNEPRFL ECFKTFFDKA AGLTNLKPGV 

        70         80         90        100        110        120 
LNNMKECNVA LRVEFPIKNE HGDVDIIAGY RAQHSHHRLP CKGGIRFSEE VDLQEVMALA 

       130        140        150        160        170        180 
SLMTYKCAVV DVPFGGAKGG VRIDPKKYTV AQREKITRAY TLLLCQKNFI GPGVDVPAPD 

       190        200        210        220        230        240 
MGTGEQEMAW IRDTYQAFNT NDVDSMACVT GKPISSGGIR GRTEATGLGV FYGIREFLSY 

       250        260        270        280        290        300 
EEVLKKTGLT PGIKGKSIVI QGFGNVGYFA AKFFEQAGAK VIAVAEHNGA VYNADGLNID 

       310        320        330        340        350        360 
ALNKYKLQHG TFIDFPGATN IVDSVKALEI PCDILIPAAL EKQIHIGNVA DIQAKLIGEA 

       370        380        390        400        410        420 
ANGPMTPRAD QILLNRGHVI IPDLLLNAGG VTVSYFEWLK NLSHVRFGRL NKKWEESSKK 

       430        440        450        460        470        480 
LLLEFVESTV NKKLSEAERS LIIHGADEID IVRSGLEDTM QNACAETRKT ANEKNTDYRS 

       490        500 
AALYNAIMKI KAVYESSGNV FS

« Hide

References

« Hide 'large scale' references
[1]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed: 15875012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum: purification and properties."
Pamula F., Wheldrake J.F.
Arch. Biochem. Biophys. 291:225-230(1991) [PubMed: 1952936] [Abstract]
Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[3]"The effect of AMP on the NAD-dependent glutamate dehydrogenase during activation and morphogenesis in the cellular slime moulds."
Pamula F., Wheldrake J.F.
J. Gen. Microbiol. 138:1935-1940(1992) [PubMed: 1402793] [Abstract]
Cited for: ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAFI02000101 Genomic DNA. Translation: EAL63700.1.
RefSeqXP_637204.1. XM_632112.1.

3D structure databases

HSSPHSSP built from PDB template 1L1F based on UniProtKB P00367.
ProteinModelPortalQ54KB7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ54KB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0231438; DDB0231438; DDB_G0287469.
GeneID8626141.
GenomeReviewsGene locus gluD in contig CM000154_GR.
KEGGddi:DDB_G0287469.

Organism-specific databases

dictyBaseDDB_G0287469. glud1.

Phylogenomic databases

eggNOGKOG2250.
GeneTreeEPrGT00050000005333.
HOGENOMHBG590661.
OMAKNIENTE.
PhylomeDBQ54KB7.
ProtClustDBCLSZ2429993.

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.
KOK00261.
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_DICDI
AccessionPrimary (citable) accession number: Q54KB7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

SIMILARITY comments

Index of protein domains and families

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