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DHE1_ORYSJ
ID   DHE1_ORYSJ              Reviewed;         411 AA.
AC   Q852M0; A3ANK4;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Glutamate dehydrogenase 1, mitochondrial {ECO:0000305};
DE            Short=OsGDH1;
DE            EC=1.4.1.3 {ECO:0000255|PROSITE-ProRule:PRU10011};
DE   Flags: Precursor;
GN   Name=GDH1;
GN   OrderedLocusNames=LOC_Os03g58040 {ECO:0000312|EMBL:ABF99322.1},
GN   Os03g0794500 {ECO:0000312|EMBL:BAF13454.1};
GN   ORFNames=OSJNBb0060J21.2 {ECO:0000312|EMBL:AAO37984.1},
GN   OSNPB_030794500 {ECO:0000312|EMBL:BAS86820.1};
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].
RA   Yao Q., Peng R., Xiong A.;
RT   "Isolation and characterization of a rice glutamate dehydrogenase.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY INORGANIC
RP   NITROGEN, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Nipponbare; TISSUE=Callus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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).
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, NaNO(3) and NH(4)NO(3)
CC       (PubMed:16120687). Induced in roots after nitrogen (N-deprivation)
CC       deprivation (PubMed:19430792). {ECO:0000269|PubMed:16120687,
CC       ECO:0000269|PubMed:19430792}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAZ28893.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY332470; AAQ01156.1; -; mRNA.
DR   EMBL; AB024962; BAE48296.1; -; mRNA.
DR   EMBL; AC090871; AAO37984.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99322.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99323.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99324.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13454.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS86820.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ28893.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015631051.1; XM_015775565.1.
DR   RefSeq; XP_015631052.1; XM_015775566.1.
DR   AlphaFoldDB; Q852M0; -.
DR   SMR; Q852M0; -.
DR   STRING; 4530.OS03T0794500-01; -.
DR   PaxDb; Q852M0; -.
DR   PRIDE; Q852M0; -.
DR   EnsemblPlants; Os03t0794500-01; Os03t0794500-01; Os03g0794500.
DR   GeneID; 4334405; -.
DR   Gramene; Os03t0794500-01; Os03t0794500-01; Os03g0794500.
DR   KEGG; osa:4334405; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_025763_1_2_1; -.
DR   InParanoid; Q852M0; -.
DR   OMA; WMTYKTA; -.
DR   OrthoDB; 692851at2759; -.
DR   BRENDA; 1.4.1.2; 4460.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
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:1901698; P:response to nitrogen compound; 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 1, mitochondrial"
FT                   /id="PRO_0000437577"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   411 AA;  44342 MW;  883A70259304766E CRC64;
     MNALAATSRN FKQAAKLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS YVGFRVQHDN
     ARGPMKGGIR YHHEVDPDEV NALAQLMTWK TAVANIPYGG AKGGIGCSPG DLSISELERL
     TRVFTQKIHD LIGIHTDVPA PDMGTNSQTM AWILDEYSKF HGYSPAVVTG KPVDLGGSLG
     RDAATGRGVL FATEALLAEH GKGIAGQRFV IQGFGNVGSW AAQLISEAGG KVIAISDVTG
     AVKNSNGLDI AKLMKHSSEN RGIKGFDGGD AIDPRSLLTE ECDVLIPAAL GGVINKDNAN
     EIKAKYIIEA ANHPTDPEAD EILSKKGVLI LPDILANSGG VTVSYFEWVQ NIQGFMWDEE
     KVNNELKTYM TRGFRDVKEM CRSHHCDLRM GAFTLGVNRV ARATVLRGWE A
 
 
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