ID   G9I738_GIAIN            Unreviewed;       141 AA.
AC   G9I738;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
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:AEV23640.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:AEV23640.1};
RN   [1] {ECO:0000313|EMBL:AEV23640.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISSGdA418 {ECO:0000313|EMBL:AEV23632.1}, and ISSGdA482
RC   {ECO:0000313|EMBL:AEV23640.1};
RX   PubMed=22022810; DOI=10.1089/vbz.2011.0751;
RA   Beck R., Sprong H., Pozio E., Caccio S.M.;
RT   "Genotyping Giardia duodenalis Isolates from Dogs: Lessons from a
RT   Multilocus Sequence Typing Study.";
RL   Vector Borne Zoonotic Dis. 12:206-213(2012).
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; JN587370; AEV23632.1; -; Genomic_DNA.
DR   EMBL; JN587378; AEV23640.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9I738; -.
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; 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; 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; 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|RuleBase:RU004417}.
FT   DOMAIN          35..139
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:AEV23640.1"
FT   NON_TER         141
FT                   /evidence="ECO:0000313|EMBL:AEV23640.1"
SQ   SEQUENCE   141 AA;  15752 MW;  948EAA3E9DC7AE81 CRC64;
     GVGAREIGYL YGQYKRLRNE FTGVLTGKNV KWGGSFIRPE ATGYGAVYFL EEMCKDNNTV
     IRGKNVLLSG SGNVAQFACE KLIQLGAKVL TFSDSNGTIV DKDGFNEEKL AHLMYLKNEK
     RGRVSEFKDK YPSVAYYEGK K
//