ID   DHE4_GIAIN              Reviewed;         449 AA.
AC   P28724; Q24961;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
DE   AltName: Full=NADP-dependent glutamate dehydrogenase;
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1559991; DOI=10.1016/s0021-9258(18)42550-1;
RA   Yee J., Dennis P.P.;
RT   "Isolation and characterization of a NADP-dependent glutamate dehydrogenase
RT   gene from the primitive eucaryote Giardia lamblia.";
RL   J. Biol. Chem. 267:7539-7544(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-261.
RX   PubMed=8587793; DOI=10.1017/s0031182000065021;
RA   Monis P.T., Mayrhofer G., Andrews R.H., Homan W.L., Limper L., Ey P.L.;
RT   "Molecular genetic analysis of Giardia intestinalis isolates at the
RT   glutamate dehydrogenase locus.";
RL   Parasitology 112:1-12(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; M84604; AAA29155.1; -; mRNA.
DR   EMBL; U47632; AAB05400.1; -; Genomic_DNA.
DR   PIR; A42489; A42489.
DR   AlphaFoldDB; P28724; -.
DR   SMR; P28724; -.
DR   PRIDE; P28724; -.
DR   VEuPathDB; GiardiaDB:DHA2_21942; -.
DR   VEuPathDB; GiardiaDB:GL50581_4496; -.
DR   VEuPathDB; GiardiaDB:GL50803_0021942; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   BRENDA; 1.4.1.4; 2401.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..449
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182786"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        249
FT                   /note="I -> L (in Ref. 2; AAB05400)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   449 AA;  49766 MW;  5497B35209B549F6 CRC64;
     MPAQTIEELI AVIKQRDGHM TEFRQAVEEV VDSLKVIFER EPKYIPIFER MLEPERVIIF
     RVPWMDDAGR INVNRGFRVQ YNSALGPYKG GLRFHPSVNL SILKFLGFEQ ILKNSLTTLP
     MGGGKGGSDF DPKGKSDNEV MRFCQSFMTE LQRHVGADTD VPAGDIGVGA REIGYLYGQY
     KRLRNEFTGV LTGKNVKWGG SFIRPEATGY GAVYFLEEMC KDNNTVIRGK NVLLSGSGNV
     AQFACEKLIQ LGAKVLTFSD SNGTIVDKDG FNEEKLAHLM YLKNEKRGRV SEFKDKYPSV
     AYYEGKKPWE CFEGQMDCIM PCATQNEVSG DDATRLVGLG LKFVAEGANM PSTAEAVHVY
     HAKGVMYGPA KASNAGGVSV SGLEMSQNSV RLQWTAEEVD QKLRGIMRGI FVACRDTAKK
     YGHPKNYQMG ANIAGFLKVA DSMIEQGCV