ID A0A3B0K5C3_DROGU Unreviewed; 548 AA.
AC A0A3B0K5C3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=glutamate dehydrogenase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012889};
DE EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN ORFNames=DGUA_6G004995 {ECO:0000313|EMBL:SPP80141.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP80141.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; OUUW01000005; SPP80141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0K5C3; -.
DR STRING; 7266.A0A3B0K5C3; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
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:SF7; GLUTAMATE DEHYDROGENASE; 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}.
FT DOMAIN 257..544
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 19..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60594 MW; FCD17E3AD73E204D CRC64;
MLRNLTLALF KQRSQAQAQA QAQAHAPVQS QIQSRRHEHK MPEHLKKVAS DKDPEFSAMV
LYYYHQAAQA MESQLVKEMG KYSHMKPEER QARVSAILNL IGSVTTSVEV SFPIIKSDGA
YEIITGYRAH HIRNRLPLKG GIRYAMDVDE NEVKALAAIM TFKCACVSLP YGGSKGGVRI
DPKKYTVGEL QTITRRYTME LLKRNMIGPG IDVPAPDVNT SGREMSWIVD QYSKTFGYKD
INAAAIVTGK PVHIGGINGR NSATGRGVWK AGDLFLQDKD WMDLLKWKTG WEDKKVIVQG
FGNVGSFAAK FVHEAGAKLI GVKELDCQLF NKDGIDINDL IAYKEEKKSI KGYSKAQEAK
GDLLEAECDI LMPCATQKVI TSENAGKIKA KLILEGANGP TTPAGEKILI DKGVLLVPDL
YCNAGGVTVS YFEYLKNINH VSYGKMNSKT TSQLIHEVIN SINESLNRCP DAEFPEIEPN
KRLMRIRDCT KEAEIVDAAL QTVMESAAAG IKATANKFET CNDLRKAAYI YAVFKIFNAV
ESSGISQQ
//