ID C9EHI3_GIAIN Unreviewed; 275 AA.
AC C9EHI3;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=glutamate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012907};
DE EC=1.4.1.4 {ECO:0000256|ARBA:ARBA00012907};
DE Flags: Fragment;
GN Name=gdh {ECO:0000313|EMBL:ACV92725.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ACV92725.1};
RN [1] {ECO:0000313|EMBL:ACV92725.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C928 {ECO:0000313|EMBL:ACV92725.1};
RA Fernandes L.N., Dropa M., Araujo R.S., Matte G.R., Matte M.H.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; GQ503128; ACV92725.1; -; Genomic_DNA.
DR AlphaFoldDB; C9EHI3; -.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 56..275
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV92725.1"
FT NON_TER 275
FT /evidence="ECO:0000313|EMBL:ACV92725.1"
SQ SEQUENCE 275 AA; 29843 MW; 62DE94FB2F222EA0 CRC64;
SFMTELQRHV GADTDVPAGD IGVGAREIGY LYGQYKRLGN EFTGVLTGKN VKWGGSFIRP
EATGYGAVYF LEEMCKDNNT VIRGKNVLLS GSGNVAQFAC EKLIQLGAKV LTSSDSNGTI
VDKDGFNEEK LAHLMYLKNE KRGRVSELKD KYPSVVYYEG KKPWECFEGQ VDCIMPCATQ
NEVSGDDATR LVGLGHKFVA EGANMPSTAE AVHVYPAKGV MYGPAKASNA GGVSVSGLEM
SQNSVRLQWT AEEVDQKLRG IMRGIFAACR DTAKK
//
