ID   A0A3B4GT15_9CICH        Unreviewed;       546 AA.
AC   A0A3B4GT15;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glutamate dehydrogenase 1, mitochondrial {ECO:0000256|ARBA:ARBA00040147};
DE            EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN   Name=glud1 {ECO:0000313|RefSeq:XP_005743603.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000026140.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000026140.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005743603.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023525};
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:0000256|ARBA:ARBA00023549};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR   RefSeq; XP_005743603.1; XM_005743546.2.
DR   AlphaFoldDB; A0A3B4GT15; -.
DR   STRING; 303518.ENSPNYP00000026140; -.
DR   Ensembl; ENSPNYT00000026778.1; ENSPNYP00000026140.1; ENSPNYG00000019695.1.
DR   GeneID; 102210269; -.
DR   CTD; 2746; -.
DR   GeneTree; ENSGT00390000000854; -.
DR   OrthoDB; 45283at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; Unplaced.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
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:SF13; GLUTAMATE DEHYDROGENASE 1, 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000695023}.
FT   DOMAIN          253..542
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   546 AA;  59953 MW;  C32E239D5E598573 CRC64;
     MYRYFGELLT RGAGGVLASG YPAAAADSVL PASASLLRHR GYSQAVDPAD DPNFFTMVEG
     FFDKGAAIVE DKLVEDLKTR ETAEQKRSRV RGILRIIKPC NHVLSVSFPI KRDSGEWEVI
     EGYRAQHSQH RTPCKGGIRY STEVSVDEVK ALASLMTYKC AVVDVPFGGA KAGVKINPKK
     YSDNELEKIT RRFTIELAKK GFIGPGIDVP APDMSTGERE MSWIADTFAT VMGHNDINAH
     ACVTGKPISQ GGIHGRISAT GRGVFHGIEN FINEASYMSQ LGMYPGFQDK TFVIQGFGNV
     GLHSMRYLHR FGARCVGVGE LDGSIWNPEG INPKELEDYK LANGTIVGFP DSTPYEGSIL
     EADCDILIPA ASEKQLTKSN AHKIKAKIIA EGANGPTTPE ADQIFLERNI LVIPDMYLNA
     GGVTVSYFEW LKNLNHVSYG RLTFKYERDS NYHLLMSVQE SLERKFGKHG GSVPVVPTSE
     FQARIAGASE KDIVHSGLAY TMERSARQIM RTANKYDLGL DLRTAAYVNA IEKVFKVYSE
     AGLIIT
//