ID DHE2_ORYSJ Reviewed; 411 AA.
AC Q33E23; B9FGE7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Glutamate dehydrogenase 2, mitochondrial {ECO:0000305};
DE Short=OsGDH2;
DE EC=1.4.1.3 {ECO:0000255|PROSITE-ProRule:PRU10011};
DE Flags: Precursor;
GN Name=GDH2;
GN OrderedLocusNames=LOC_Os04g45970 {ECO:0000305},
GN Os04g0543900 {ECO:0000312|EMBL:BAS90319.1};
GN ORFNames=OSNPB_040543900 {ECO:0000312|EMBL:BAS90319.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY INORGANIC
RP NITROGEN, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Sasanishiki; TISSUE=Root;
RX PubMed=16120687; DOI=10.1093/pcp/pci188;
RA Abiko T., Obara M., Ushioda A., Hayakawa T., Hodges M., Yamaya T.;
RT "Localization of NAD-isocitrate dehydrogenase and glutamate dehydrogenase
RT in rice roots: candidates for providing carbon skeletons to NADH-glutamate
RT synthase.";
RL Plant Cell Physiol. 46:1724-1734(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY NITROGEN DEPRIVATION.
RX PubMed=19430792; DOI=10.1007/s00299-009-0709-z;
RA Qiu X., Xie W., Lian X., Zhang Q.;
RT "Molecular analyses of the rice glutamate dehydrogenase gene family and
RT their response to nitrogen and phosphorous deprivation.";
RL Plant Cell Rep. 28:1115-1126(2009).
RN [6]
RP INDUCTION BY SALT STRESS.
RX PubMed=23082824; DOI=10.1186/1471-2229-12-194;
RA Wang H., Zhang M., Guo R., Shi D., Liu B., Lin X., Yang C.;
RT "Effects of salt stress on ion balance and nitrogen metabolism of old and
RT young leaves in rice (Oryza sativa L.).";
RL BMC Plant Biol. 12:194-194(2012).
RN [7]
RP INDUCTION BY ALKALI STRESS.
RX PubMed=22655071; DOI=10.1371/journal.pone.0037817;
RA Wang H., Wu Z., Han J., Zheng W., Yang C.;
RT "Comparison of ion balance and nitrogen metabolism in old and young leaves
RT of alkali-stressed rice plants.";
RL PLoS ONE 7:E37817-E37817(2012).
RN [8]
RP INDUCTION BY IDD10.
RX PubMed=23278238; DOI=10.1111/nph.12075;
RA Xuan Y.H., Priatama R.A., Huang J., Je B.I., Liu J.M., Park S.J.,
RA Piao H.L., Son D.Y., Lee J.J., Park S.H., Jung K.H., Kim T.H., Han C.D.;
RT "Indeterminate domain 10 regulates ammonium-mediated gene expression in
RT rice roots.";
RL New Phytol. 197:791-804(2013).
RN [9]
RP INDUCTION BY IDD10.
RX PubMed=23470720; DOI=10.4161/psb.24139;
RA Xuan Y.H., Priatama R.A., Kumar V., Han C.D.;
RT "Regulatory role of indeterminate domain 10 (IDD10) in ammonium-dependent
RT gene expression in rice roots.";
RL Plant Signal. Behav. 8:E24139-E24139(2013).
RN [10]
RP INDUCTION BY COLD.
RX PubMed=26230579; DOI=10.1371/journal.pone.0132100;
RA Bevilacqua C.B., Basu S., Pereira A., Tseng T.-M., Zimmer P.D.,
RA Burgos N.R.;
RT "Analysis of stress-responsive gene expression in cultivated and weedy rice
RT differing in cold stress tolerance.";
RL PLoS ONE 10:E0132100-E0132100(2015).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots (PubMed:16120687). Expressed
CC ubiquitously in various tissues (PubMed:19430792).
CC {ECO:0000269|PubMed:16120687, ECO:0000269|PubMed:19430792}.
CC -!- DEVELOPMENTAL STAGE: Detected in the region of the apical meristem and
CC cortical cells in the tip region and elongation zone of the roots.
CC {ECO:0000269|PubMed:16120687}.
CC -!- INDUCTION: Slightly induced by NH(4)Cl and NH(4)NO(3)
CC (PubMed:16120687). Induced in shoots after nitrogen (N-deprivation)
CC deprivation. In roots, first transiently repressed but later induced by
CC N-deprivation (PubMed:19430792). Induced by alkali stress
CC (PubMed:22655071). Up-regulated by salt stress in old leaves
CC (PubMed:23082824). Activated by IDD10 in the presence of NH(4)+ ions
CC (PubMed:23278238, PubMed:23470720). Induced by cold stress (i.e. 10
CC degrees Celsius) (PubMed:26230579). {ECO:0000269|PubMed:16120687,
CC ECO:0000269|PubMed:19430792, ECO:0000269|PubMed:22655071,
CC ECO:0000269|PubMed:23082824, ECO:0000269|PubMed:23278238,
CC ECO:0000269|PubMed:23470720, ECO:0000269|PubMed:26230579}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; AB189166; BAE48298.1; -; mRNA.
DR EMBL; AP014960; BAS90319.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61431.1; -; Genomic_DNA.
DR RefSeq; XP_015637000.1; XM_015781514.1.
DR AlphaFoldDB; Q33E23; -.
DR SMR; Q33E23; -.
DR STRING; 39947.Q33E23; -.
DR PaxDb; 39947-Q33E23; -.
DR EnsemblPlants; Os04t0543900-02; Os04t0543900-02; Os04g0543900.
DR GeneID; 4336554; -.
DR Gramene; Os04t0543900-02; Os04t0543900-02; Os04g0543900.
DR KEGG; osa:4336554; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_2_1; -.
DR InParanoid; Q33E23; -.
DR OMA; WMVYKCA; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q33E23; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006995; P:cellular response to nitrogen starvation; IEP:UniProtKB.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR GO; GO:0010446; P:response to alkaline pH; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:1901698; P:response to nitrogen compound; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF24; GLUTAMATE DEHYDROGENASE 2; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; NAD; NADP; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..411
FT /note="Glutamate dehydrogenase 2, mitochondrial"
FT /id="PRO_0000437579"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT CONFLICT 15
FT /note="A -> P (in Ref. 4; EEE61431)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="D -> E (in Ref. 4; EEE61431)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="R -> P (in Ref. 4; EEE61431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 44551 MW; A240E3AB15A0C7BB CRC64;
MNALAATSRN FRQAARLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS FIGFRVQHDN
ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVAAIPYGG AKGGIGCAPG ELSTSELERL
TRVFTQKIHD LIGAHTDVPA PDMGTNSQTM AWILDEYSKF HGHSPAVVTG KPIDLGGSLG
RDAATGRGVM YATEALLAEH GKSISGSTFV IQGFGNVGSW AARIIHEKGG KVIALGDVTG
SIRNKNGLDI PALMKHRNEG GALKDFHDAE VMDSSELLVH ECDVLIPCAL GGVLNRENAP
DVKAKFIIEA ANHPTDPEAD EILAKKGVTI LPDIYANSGG VIVSYFEWVQ NIQGFMWDEE
KVNMELHKYM NNSFQHIKAM CKSHDCNLRM GAFTLGVNRV ARATLLRGWE A
//
