DHE2_ORYSI
ID DHE2_ORYSI Reviewed; 411 AA.
AC A2XW22;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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; ORFNames=OsI_16842 {ECO:0000312|EMBL:EAY95032.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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 -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; CM000129; EAY95032.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XW22; -.
DR SMR; A2XW22; -.
DR STRING; 39946.A2XW22; -.
DR EnsemblPlants; BGIOSGA016863-TA; BGIOSGA016863-PA; BGIOSGA016863.
DR Gramene; BGIOSGA016863-TA; BGIOSGA016863-PA; BGIOSGA016863.
DR HOGENOM; CLU_025763_1_2_1; -.
DR OMA; WLQNRNG; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblPlants.
DR GO; GO:0010446; P:response to alkaline pH; IEA:EnsemblPlants.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:1901698; P:response to nitrogen compound; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
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; 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.
PE 3: Inferred from homology;
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_0000437580"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
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