ID   DHE4_PANTR              Reviewed;         558 AA.
AC   Q64HZ8;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-NOV-2023, entry version 108.
DE   RecName: Full=Glutamate dehydrogenase 2, mitochondrial;
DE            Short=GDH 2;
DE            EC=1.4.1.3;
DE   Flags: Precursor;
GN   Name=GLUD2;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15378063; DOI=10.1038/ng1431;
RA   Burki F., Kaessmann H.;
RT   "Birth and adaptive evolution of a hominoid gene that supports high
RT   neurotransmitter flux.";
RL   Nat. Genet. 36:1061-1063(2004).
CC   -!- FUNCTION: Important for recycling the chief excitatory
CC       neurotransmitter, glutamate, during neurotransmission.
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- PTM: Stoichiometry shows that ADP-ribosylation occurs in one subunit
CC       per catalytically active homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AY588274; AAU03136.1; -; Genomic_DNA.
DR   RefSeq; NP_001009004.1; NM_001009004.1.
DR   AlphaFoldDB; Q64HZ8; -.
DR   SMR; Q64HZ8; -.
DR   STRING; 9598.ENSPTRP00000004734; -.
DR   PaxDb; 9598-ENSPTRP00000004734; -.
DR   GeneID; 449581; -.
DR   KEGG; ptr:449581; -.
DR   CTD; 2747; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   InParanoid; Q64HZ8; -.
DR   OrthoDB; 45283at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   Gene3D; 1.10.287.140; -; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF15; GLUTAMATE DEHYDROGENASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 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.
PE   3: Inferred from homology;
KW   ADP-ribosylation; Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           54..558
FT                   /note="Glutamate dehydrogenase 2, mitochondrial"
FT                   /id="PRO_0000007210"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         172
FT                   /note="ADP-ribosylcysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   558 AA;  61439 MW;  9180BC7CB62C251D CRC64;
     MYRYLAKALL TSRAGPAALG SAANHSAALL GRGPGQPAAA SQPGLALAAR RHYSELVADR
     EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN RVRGILRIIK PCNHVLSLSF
     PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
     GAKAGVKINP KNYTENELEK ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY
     ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR
     DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FRLQHGSLLG
     FPKAKPYEGS ILEIDCDILI PAATEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
     NILVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
     HGGTIPIVPT AEFQDSISGA SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV
     NAIEKVFKVY SEAGVTFT
//