ID   DHE3_ELEEL              Reviewed;          51 AA.
AC   P28270;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
DE   Flags: Fragments;
OS   Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC   Gymnotoidei; Gymnotidae; Electrophorus.
OX   NCBI_TaxID=8005;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=1639763; DOI=10.1093/oxfordjournals.jbchem.a123814;
RA   Tang M.-Q., Ando S., Yamada S., Hayashi S.;
RT   "The trypsin-catalyzed activation of glutamate dehydrogenase purified from
RT   eel liver.";
RL   J. Biochem. 111:655-661(1992).
CC   -!- FUNCTION: Mitochondrial glutamate dehydrogenase that converts L-
CC       glutamate into alpha-ketoglutarate. Plays a key role in glutamine
CC       anaplerosis by producing alpha-ketoglutarate, an important intermediate
CC       in the tricarboxylic acid cycle (By similarity). {ECO:0000250}.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P28270; -.
DR   SMR; P28270; -.
DR   STRING; 8005.ENSEEEP00000036184; -.
DR   Proteomes; UP000314983; Unassembled WGS sequence.
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:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; ISS:UniProtKB.
DR   GO; GO:0006541; P:glutamine metabolic process; ISS:UniProtKB.
DR   GO; GO:0072350; P:tricarboxylic acid metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.10.287.140; -; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..>51
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182744"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        43..44
FT                   /evidence="ECO:0000305"
FT   NON_TER         51
SQ   SEQUENCE   51 AA;  5650 MW;  499A36DF9A05B004 CRC64;
     SEAVAEKEDD PNFFKMVEGF FDKGAAIVEN KLVEDLKTRG SPEVEGNLTF T
//