ID   A8RIP5_GIAIN            Unreviewed;       329 AA.
AC   A8RIP5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 51.
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:ABS53134.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ABS53134.1};
RN   [1] {ECO:0000313|EMBL:ABS53134.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H30 {ECO:0000313|EMBL:ABS53134.1};
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; EF507672; ABS53134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8RIP5; -.
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          144..329
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:ABS53134.1"
FT   NON_TER         329
FT                   /evidence="ECO:0000313|EMBL:ABS53134.1"
SQ   SEQUENCE   329 AA;  35938 MW;  F3CCCA745A06837B CRC64;
     IMFRVPWMDD AGRINVNRGF RIQYNSALGP YKGGLRFHPS VNLSILKFLG FEQILKNSLT
     TLPMGGGKGG SDFDPKGKSD NEVMRFCQSF MTELQRHVGA DTDVPAGDIG VGGREIGYLF
     GQYKRLRNEF TGVLTGKNIK WGGSLIRPEA TGYGAVYFLE EMCKDNNTVI RGKNVLLSGS
     GNVAQYACEK LLQLGAKVLT FSDSNGTIVD KDGFNEEKLA HLMHLKNEKR GRIAEFKEKY
     PSVVYHENKK PWECFDGQVD CIMPCATQNE VTGDDATRLV GLGLKFVAEG ANMPSTAEAV
     HVYHAKGVMY GPAKAANAGG VSVSGLEMS
//