Reviewed, UniProtKB/Swiss-Prot Q54KB7 (DHE3_DICDI)

Names and origin

Protein names

Recommended name:
    Glutamate dehydrogenase, mitochondrial
      Short name=GDH
    EC=1.4.1.3

Gene names

Name:	gluD
ORF Names:	DDB_G0287469

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 KM=16 µM for NADH KM=34.5 mM for NH3 pH dependence: Optimum pH is 7.25 to 7.5.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 502		Glutamate dehydrogenase, mitochondrial		PRO_0000327666
Regions
	Nucleotide binding	96 – 98	3	NAD By similarity
Sites
	Active site	138	1	By similarity
	Binding site	102	1	Substrate By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	131	1	NAD By similarity
	Binding site	394	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54KB7-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: D6BB324A859C0528	FASTA	502	55,042
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000101 Genomic DNA. Translation: EAL63700.1.
RefSeq	XP_637204.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3388778.
KEGG	ddi:DDB_0231438.
Organism-specific databases
dictyBase	DDB_G0287469. gluD.
Phylogenomic databases
OMA	Q54KB7. MERSAQG.
Enzyme and pathway databases
BRENDA	1.4.1.3. 424.
Family and domain databases
InterPro	IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR006097. Glu/Leu/Phe/Val_DH_dimer. IPR014362. Glu_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11606:SF2. GLFV_DH. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view]
PIRSF	PIRSF000185. Glu_DH. 1 hit.
PRINTS	PR00082. GLFDHDRGNASE.
PROSITE	PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHE3_DICDI

Accession

Primary (citable) accession number: Q54KB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)