DHE3_DICDI
ID DHE3_DICDI Reviewed; 502 AA.
AC Q54KB7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutamate dehydrogenase, mitochondrial;
DE Short=GDH;
DE EC=1.4.1.3;
DE Flags: Precursor;
GN Name=gluD; ORFNames=DDB_G0287469;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=1952936; DOI=10.1016/0003-9861(91)90127-5;
RA Pamula F., Wheldrake J.F.;
RT "The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum:
RT purification and properties.";
RL Arch. Biochem. Biophys. 291:225-230(1991).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=1402793; DOI=10.1099/00221287-138-9-1935;
RA Pamula F., Wheldrake J.F.;
RT "The effect of AMP on the NAD-dependent glutamate dehydrogenase during
RT activation and morphogenesis in the cellular slime moulds.";
RL J. Gen. Microbiol. 138:1935-1940(1992).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
CC -!- ACTIVITY REGULATION: Subject to allosteric regulation. Activated by AMP
CC and ADP. {ECO:0000269|PubMed:1402793, ECO:0000269|PubMed:1952936}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.36 mM for alpha-ketoglutarate {ECO:0000269|PubMed:1952936};
CC KM=16 uM for NADH {ECO:0000269|PubMed:1952936};
CC KM=34.5 mM for NH(3) {ECO:0000269|PubMed:1952936};
CC pH dependence:
CC Optimum pH is 7.25 to 7.5. {ECO:0000269|PubMed:1952936};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:1952936}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- MISCELLANEOUS: ADP can occupy the NADH binding site and activate the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000101; EAL63700.1; -; Genomic_DNA.
DR RefSeq; XP_637204.1; XM_632112.1.
DR AlphaFoldDB; Q54KB7; -.
DR SMR; Q54KB7; -.
DR STRING; 44689.DDB0231438; -.
DR PaxDb; Q54KB7; -.
DR EnsemblProtists; EAL63700; EAL63700; DDB_G0287469.
DR GeneID; 8626141; -.
DR KEGG; ddi:DDB_G0287469; -.
DR dictyBase; DDB_G0287469; glud1.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; Q54KB7; -.
DR OMA; WLQNRNG; -.
DR PhylomeDB; Q54KB7; -.
DR Reactome; R-DDI-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; Q54KB7; -.
DR PRO; PR:Q54KB7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:dictyBase.
DR GO; GO:0006538; P:glutamate catabolic process; ISS:dictyBase.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000185; Glu_DH; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..502
FT /note="Glutamate dehydrogenase, mitochondrial"
FT /id="PRO_0000327666"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 96..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 55042 MW; D6BB324A859C0528 CRC64;
MQSLARLSRT SLVQKGLVPQ TIKNYSSVSQ AEIDNEPRFL ECFKTFFDKA AGLTNLKPGV
LNNMKECNVA LRVEFPIKNE HGDVDIIAGY RAQHSHHRLP CKGGIRFSEE VDLQEVMALA
SLMTYKCAVV DVPFGGAKGG VRIDPKKYTV AQREKITRAY TLLLCQKNFI GPGVDVPAPD
MGTGEQEMAW IRDTYQAFNT NDVDSMACVT GKPISSGGIR GRTEATGLGV FYGIREFLSY
EEVLKKTGLT PGIKGKSIVI QGFGNVGYFA AKFFEQAGAK VIAVAEHNGA VYNADGLNID
ALNKYKLQHG TFIDFPGATN IVDSVKALEI PCDILIPAAL EKQIHIGNVA DIQAKLIGEA
ANGPMTPRAD QILLNRGHVI IPDLLLNAGG VTVSYFEWLK NLSHVRFGRL NKKWEESSKK
LLLEFVESTV NKKLSEAERS LIIHGADEID IVRSGLEDTM QNACAETRKT ANEKNTDYRS
AALYNAIMKI KAVYESSGNV FS
