ID   DHE4_PONPY              Reviewed;         558 AA.
AC   Q64I00;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-MAY-2023, entry version 94.
DE   RecName: Full=Glutamate dehydrogenase 2, mitochondrial;
DE            Short=GDH 2;
DE            EC=1.4.1.3;
DE   Flags: Precursor;
GN   Name=GLUD2;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
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; AY588268; AAU03134.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q64I00; -.
DR   SMR; Q64I00; -.
DR   GO; GO:0005759; C:mitochondrial matrix; 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:amino acid metabolic process; IEA:InterPro.
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; 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_0000007211"
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;  61386 MW;  EF26FEC7089E5D44 CRC64;
     MYRYLGKALL LSRAGPAALG SAANHSAALL GRARGQPAAA SQPGLALASR RHYSELVADR
     EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN RVRGILRIIK PCNHVLSLSF
     PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
     GAKAGVKINP KNYTENELEK ITRRFTMELA KKGFIGPGID VPAPDMNTGE REMSWIADTY
     ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SNVGMTPGFG
     DKTFVVQGFG NVGLHSMRYL HRFGAKCVAV GESDGSIWNP DGIDPKELED FRLQHGSILG
     FPKAKPYEGS ILEADCDILI PAATEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
     NILVIPDVYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
     HGGTIPIVPT AEFRDSISGA SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV
     NAIEKVFKVY SEAGVTFT
//