DHE3_ORYSJ
ID DHE3_ORYSJ Reviewed; 411 AA.
AC Q6H3Y7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutamate dehydrogenase 3, mitochondrial {ECO:0000305};
DE Short=OsGDH3;
DE EC=1.4.1.3 {ECO:0000255|PROSITE-ProRule:PRU10011};
DE Flags: Precursor;
GN Name=GDH3;
GN OrderedLocusNames=LOC_Os02g43470 {ECO:0000305},
GN Os02g0650900 {ECO:0000312|EMBL:BAF09503.1};
GN ORFNames=OsJ_07745 {ECO:0000312|EMBL:EAZ24022.1},
GN OSJNBb0012J10.18 {ECO:0000312|EMBL:BAD26562.1},
GN OSNPB_020650900 {ECO:0000312|EMBL:BAS80054.1};
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], AND TISSUE SPECIFICITY.
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=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION BY NITROGEN AND PHOSPHORUS 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 [8]
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 [9]
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).
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: Barely expressed in leaves, spikelets and roots
CC (PubMed:16120687). Glumes and stamens specific accumulation
CC (PubMed:19430792). {ECO:0000269|PubMed:16120687,
CC ECO:0000269|PubMed:19430792}.
CC -!- INDUCTION: Induced in shoots and roots after nitrogen (N-deprivation)
CC and phosphorus (P-deprivation) deprivations (PubMed:19430792). Induced
CC by alkali stress (PubMed:22655071). Up-regulated by salt stress in old
CC leaves (PubMed:23082824). {ECO:0000269|PubMed:19430792,
CC ECO:0000269|PubMed:22655071, ECO:0000269|PubMed:23082824}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; AB035927; BAE48297.1; -; mRNA.
DR EMBL; AP007203; BAD26562.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09503.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80054.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ24022.1; -; Genomic_DNA.
DR EMBL; AK103028; BAG95846.1; -; mRNA.
DR RefSeq; XP_015622776.1; XM_015767290.1.
DR AlphaFoldDB; Q6H3Y7; -.
DR SMR; Q6H3Y7; -.
DR STRING; 4530.OS02T0650900-01; -.
DR PaxDb; Q6H3Y7; -.
DR PRIDE; Q6H3Y7; -.
DR EnsemblPlants; Os02t0650900-01; Os02t0650900-01; Os02g0650900.
DR GeneID; 4330164; -.
DR Gramene; Os02t0650900-01; Os02t0650900-01; Os02g0650900.
DR KEGG; osa:4330164; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_2_1; -.
DR InParanoid; Q6H3Y7; -.
DR OMA; TVPIERD; -.
DR OrthoDB; 692851at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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:0009651; P:response to salt stress; IEP:UniProtKB.
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 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 3, mitochondrial"
FT /id="PRO_0000437581"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ SEQUENCE 411 AA; 44454 MW; 9ACE70BFFB31874B CRC64;
MNALAATSRN FRQAARLLGL DSKLQKSLLI PLREIKVECT IPKDDGTLAT FVGFRVQHDN
SRGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVAAVPYGG AKGGIGCTPG ELSRSELERL
TRVFTQKIHD LIGINTDVPA PDMGTNAQTM AWILDEYSKF HGHSPAVVTG KPIDLGGSLG
RDAATGRGVM YATEALLTEY SESISGSTFV IQGLGNVGSW AAKLIHQKGG KIVAVGDVTG
AIRNKSGIDI PALLKHRSEG GSLEDFYGAE VMDAAELLVH ECDVLVPCAL GGVLNRENAA
EVKARFIIEG ANHPTDTEAD EILAKKGVIV LPDIYANSGG VVVSYFEWVQ NIQGFMWDEE
KVNRELQKYM KNAFQNIKDM CKSQNCNLRM GAFTLGVNRV AKATLLRGWE A
