ID A8RI49_GIAIN Unreviewed; 335 AA.
AC A8RI49;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:ABS53090.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ABS53090.1};
RN [1] {ECO:0000313|EMBL:ABS53090.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C28 {ECO:0000313|EMBL:ABS53090.1};
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; EF507628; ABS53090.1; -; Genomic_DNA.
DR AlphaFoldDB; A8RI49; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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..335
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:ABS53090.1"
FT NON_TER 335
FT /evidence="ECO:0000313|EMBL:ABS53090.1"
SQ SEQUENCE 335 AA; 36713 MW; DAC0299CF9C817D6 CRC64;
RVIIFRVPWM DDAGRINVNR GFRVQYNSAL GPYKGGLRFH PSVNLSILKF LGFEQILKNS
LTTLPMGGGK GGSDFDPKGK SDNEVMRFCQ SFMTELQRHV GADTDVPAGD IGVGAREIGY
LFGQYKRLRN EFTGVLTGKN IKWGGSLIRP EATGYGAVYF LEEMCKDNNT IIRGKNVLLS
GSGNVAQFAC EKLLQLGAKV LTFSDSNGTI VDKDGFNEEK LTHLKYLKNE KRGRISEFKD
KYPSVTYYEN KKPWECFEGQ VDCIMPCATQ NEVTGDDATR LVGLGLKFVA EGANMPSTAE
AVHIYHAKGV MYGPAKAANA GGVSVSGLEM SQNSV
//