ID   A8RII7_GIAIN            Unreviewed;       332 AA.
AC   A8RII7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:ABS53117.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ABS53117.1};
RN   [1] {ECO:0000313|EMBL:ABS53117.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H11 {ECO:0000313|EMBL:ABS53117.1}, and H31
RC   {ECO:0000313|EMBL:ABS53135.1};
RX   PubMed=17900812; DOI=10.1016/j.vetpar.2007.08.019;
RA   Souza S.L., Gennari S.M., Richtzenhain L.J., Pena H.F., Funada M.R.,
RA   Cortez A., Gregori F., Soares R.M.;
RT   "Molecular identification of Giardia duodenalis isolates from humans, dogs,
RT   cats and cattle from the state of Sao Paulo, Brazil, by sequence analysis
RT   of fragments of glutamate dehydrogenase (gdh) coding gene.";
RL   Vet. Parasitol. 149:258-264(2007).
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; EF507655; ABS53117.1; -; Genomic_DNA.
DR   EMBL; EF507673; ABS53135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8RII7; -.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          146..332
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:ABS53117.1"
FT   NON_TER         332
FT                   /evidence="ECO:0000313|EMBL:ABS53117.1"
SQ   SEQUENCE   332 AA;  36322 MW;  0D79891DC379D659 CRC64;
     RVIIFRVPWM DDAGRINVNR GFRVQYNSAL GPYKGGLRFH PSVNLSILKF LGFEQILKNS
     LTTLPMGGGK GGSDFDPKGK SDNEVMRFCQ SFMTELQRHV GADTDVPAGD IGVGAREIGY
     LYGQYKRLRN EFTGVLTGKN VKWGGSFIRP EATGYGAVYF LEEMCKDNNT VIRGKNVLLS
     GSGNVAQFAC EKLIQLGAKV LTFSDSNGTI VDKDGFNEEK LAHLMYLKNE KRGRVSEFKD
     KYPSVVYYEG KKPWECFEGQ VDCIMPCATQ NEVSGDDATR LVGLGLKFVA EGANMPSTAE
     AVHVYHAKGV MYGPAKASNA GGVSVSGLEM SQ
//