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UniProtKB/Swiss-Prot entry Q54KB7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHE3_DICDI
Primary accession number Q54KB7
Secondary accession numbers None
Integrated into Swiss-Prot on April 8, 2008
Sequence was last modified on May 24, 2005 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 27)
Name and origin of the protein
Protein name Glutamate dehydrogenase, mitochondrial [Precursor]
Synonyms GDH
EC 1.4.1.3
Gene name
Name: gluD
ORFNames: DDB_0231438
From
Dictyostelium discoideum (Slime mold) [TaxID: 44689] 
Taxonomy Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
DOI=10.1016/0003-9861(91)90127-5; PubMed=1952936 [NCBI, ExPASy, EBI, Israel, Japan]
Pamula F., Wheldrake J.F.;
"The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum: purification and properties.";
Arch. Biochem. Biophys. 291:225-230(1991).
[3]
ENZYME REGULATION.
PubMed=1402793 [NCBI, ExPASy, EBI, Israel, Japan]
Pamula F., Wheldrake J.F.;
"The effect of AMP on the NAD-dependent glutamate dehydrogenase during activation and morphogenesis in the cellular slime moulds.";
J. Gen. Microbiol. 138:1935-1940(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AAFI02000101; EAL63700.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_637204.1; -.
3D structure databases
ModBase Q54KB7.
Organism-specific databases
dictyBase DDB0231438; gluD.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR006095; 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 of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11606:SF2; GLFV_DH; 1.
Pfam PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000185; Glu_DH; 1.
PRINTS PR00082; GLFDHDRGNASE.
PROSITE PS00074; GLFV_DEHYDROGENASE; 1.
BLOCKS Q54KB7.
Genome annotation databases
GeneID 3388778; -.
KEGG ddi:DDB_0231438; -.
Other
ProtoNet Q54KB7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   502        Glutamate dehydrogenase, mitochondrial. PRO_0000327666
NP_BIND   96    98  3     NAD (By similarity). 
ACT_SITE   138   138        By similarity. 
BINDING   102   102        Substrate (By similarity). 
BINDING   126   126        Substrate (By similarity). 
BINDING   131   131        NAD (By similarity). 
BINDING   394   394        Substrate (By similarity). 
Sequence information
Length: 502 AA [This is the length of the unprocessed precursor] Molecular weight: 55042 Da [This is the MW of the unprocessed precursor] CRC64: D6BB324A859C0528 [This is a checksum on the sequence]
        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 

Q54KB7 in FASTA format

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