ID   DHE2_ARATH              Reviewed;         411 AA.
AC   Q38946;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Glutamate dehydrogenase 2;
DE            Short=GDH 2;
DE            EC=1.4.1.3;
GN   Name=GDH2; OrderedLocusNames=At5g07440; ORFNames=T2I1_150;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Turano F.J., Thakkar S.S., Weisemann J.M.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   PROTEIN SEQUENCE OF 232-243 AND 391-399, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf, and Stem;
RX   PubMed=11743114; DOI=10.1104/pp.127.4.1694;
RA   Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT   "Proteomic approach to identify novel mitochondrial proteins in
RT   Arabidopsis.";
RL   Plant Physiol. 127:1694-1710(2001).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
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:0000269|PubMed:11743114,
CC       ECO:0000269|PubMed:14671022}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q38946-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; U56635; AAB01222.1; -; mRNA.
DR   EMBL; AL163912; CAB87933.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91157.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91158.1; -; Genomic_DNA.
DR   PIR; T49883; T49883.
DR   RefSeq; NP_001119183.1; NM_001125711.2. [Q38946-1]
DR   RefSeq; NP_196361.1; NM_120826.3. [Q38946-1]
DR   PDB; 8OWM; X-ray; 1.70 A; A/B/C/D/E/F=1-411.
DR   PDB; 8OWN; EM; 3.26 A; A/B/C/D/E/F=1-411.
DR   PDBsum; 8OWM; -.
DR   PDBsum; 8OWN; -.
DR   AlphaFoldDB; Q38946; -.
DR   EMDB; EMD-17240; -.
DR   SMR; Q38946; -.
DR   BioGRID; 15914; 6.
DR   IntAct; Q38946; 1.
DR   STRING; 3702.Q38946; -.
DR   iPTMnet; Q38946; -.
DR   SwissPalm; Q38946; -.
DR   PaxDb; 3702-AT5G07440-1; -.
DR   ProteomicsDB; 224161; -. [Q38946-1]
DR   EnsemblPlants; AT5G07440.1; AT5G07440.1; AT5G07440. [Q38946-1]
DR   EnsemblPlants; AT5G07440.2; AT5G07440.2; AT5G07440. [Q38946-1]
DR   GeneID; 830635; -.
DR   Gramene; AT5G07440.1; AT5G07440.1; AT5G07440. [Q38946-1]
DR   Gramene; AT5G07440.2; AT5G07440.2; AT5G07440. [Q38946-1]
DR   KEGG; ath:AT5G07440; -.
DR   Araport; AT5G07440; -.
DR   TAIR; AT5G07440; GDH2.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_025763_1_2_1; -.
DR   InParanoid; Q38946; -.
DR   OMA; WMVYKCA; -.
DR   OrthoDB; 45283at2759; -.
DR   PhylomeDB; Q38946; -.
DR   BioCyc; ARA:AT5G07440-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G07440-MONOMER; -.
DR   BRENDA; 1.4.1.3; 399.
DR   PRO; PR:Q38946; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q38946; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:TAIR.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
DR   Genevisible; Q38946; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..411
FT                   /note="Glutamate dehydrogenase 2"
FT                   /id="PRO_0000182746"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        232
FT                   /note="V -> I (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242..243
FT                   /note="IR -> LK (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   411 AA;  44699 MW;  91267768215A15CF CRC64;
     MNALAATNRN FRHASRILGL DSKIERSLMI PFREIKVECT IPKDDGTLVS YIGFRVQHDN
     ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVADIPYGG AKGGIGCSPR DLSLSELERL
     TRVFTQKIHD LIGIHTDVPA PDMGTNAQTM AWILDEYSKF HGHSPAVVTG KPIDLGGSLG
     REAATGRGVV FATEALLAEY GKSIQGLTFV IQGFGNVGTW AAKLIHEKGG KVVAVSDITG
     AIRNPEGIDI NALIKHKDAT GSLNDFNGGD AMNSDELLIH ECDVLIPCAL GGVLNKENAG
     DVKAKFIVEA ANHPTDPDAD EILSKKGVII LPDIYANAGG VTVSYFEWVQ NIQGFMWEEE
     KVNLELQKYM TRAFHNIKTM CHTHSCNLRM GAFTLGVNRV ARATQLRGWE A
//