ID   DHE4_HYLLA              Reviewed;         555 AA.
AC   Q64HZ9;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Glutamate dehydrogenase 2, mitochondrial;
DE            Short=GDH 2;
DE            EC=1.4.1.3;
DE   Flags: Precursor;
GN   Name=GLUD2;
OS   Hylobates lar (Common gibbon) (White-handed gibbon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Hylobates.
OX   NCBI_TaxID=9580;
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; AY588269; AAU03135.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q64HZ9; -.
DR   SMR; Q64HZ9; -.
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:cellular amino acid metabolic process; IEA:InterPro.
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; 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   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   3: Inferred from homology;
KW   ADP-ribosylation; Mitochondrion; NADP; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           51..555
FT                   /note="Glutamate dehydrogenase 2, mitochondrial"
FT                   /id="PRO_0000007209"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         169
FT                   /note="ADP-ribosylcysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  60866 MW;  36BF0E321F993A53 CRC64;
     MYCYLGKALL PSGAGPAALG SAGAALLGRA RGQPAAAPQP GLALAAWRHY SEVVADRKDD
     PNFFKMVEGF FDRGASIVED KLVKDLRTRE SEEQKRNRVR GILRIIKPCN HVLSLSFPIR
     RDDGSWEVIE GYRAQHSQHR TPCKGGIRYS ADVSVDEVKA LASLMTYKCA VVDVPFGGAK
     AGVKINPKNY TENELEKITR RFTMELAKKG FIGPGIDVPA PDMNTGEREM SWIADTYAST
     IGHYDINAHA CVTGKPISQG GIHGRISATG RGVFHGIENF INEASYMSIL GMTPGFGDKT
     FVVQGFGNVG LHSMRYLHRF GAKCIAVGES DGSIWNPDGI DPKELEDFKL QHGSILGFPK
     AKPYEGSILE ADCDILIPAA SEKQLTKSNA PRVKAKIIAE GANGPTTPEA DKIFLERNIM
     VIPDLYVNAG GVTVSYFEWL KNLNHVSYGR LTFKYERDSN YHLLMSVQES LERKFGKHGG
     TIPIVPTAEF QDSISGASEK DIVHSALAYT MERSARQIMR TAMKYNLGLD LRTAAYVNAI
     EKVFKVYSEA GVTFT