ID   E9M2I4_GIAIN            Unreviewed;       209 AA.
AC   E9M2I4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:ADW95173.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ADW95173.1};
RN   [1] {ECO:0000313|EMBL:ADW95173.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wielinga C.M., Ryan U., Thompson A., Monis P.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADW95173.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21176781; DOI=10.1016/j.ijpara.2010.11.007;
RA   Wielinga C., Ryan U., Andrew Thompson R.C., Monis P.;
RT   "Multi-locus analysis of Giardia duodenalis intra-Assemblage B substitution
RT   patterns in cloned culture isolates suggests sub-Assemblage B analyses will
RT   require multi-locus genotyping with conserved and variable genes.";
RL   Int. J. Parasitol. 41:495-503(2011).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; HQ179611; ADW95173.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9M2I4; -.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
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   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          2..209
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:ADW95173.1"
FT   NON_TER         209
FT                   /evidence="ECO:0000313|EMBL:ADW95173.1"
SQ   SEQUENCE   209 AA;  22767 MW;  CC923CF800D4B3C9 CRC64;
     NVLLSGSGNV AQFACEKLIQ LGAKVLTFSD SNGTIVDKDG FNEEKLAHLM YLKNEKRGRV
     SEFKDKYPSV VYYEGKKPWE CFEGQVDCIM PCATQNEVSG DDATRLVGLG LKFVAEGANM
     PSTAEAVHVY HAKGVMYGPA KASNAGGVSV SGLEMSQNSV RLQWTAEEVD QKLRGIMRGI
     FVACRDTAKK YGHPKNYQMG ANIAGFLKV
//