ID   DHE4_AGABI              Reviewed;         457 AA.
AC   P54387;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
DE   AltName: Full=NADP-dependent glutamate dehydrogenase;
GN   Name=gdhA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Horst H39;
RX   PubMed=8602149; DOI=10.1007/bf02174392;
RA   Schaap P.J., Mueller Y., Baars J.J.P., Op den Camp H.J.M.,
RA   Sonnenberg A.S.M., van Griensven L.J.L.D., Visser J.;
RT   "Nucleotide sequence and expression of the gene encoding NADP+-dependent
RT   glutamate dehydrogenase (gdhA) from Agaricus bisporus.";
RL   Mol. Gen. Genet. 250:339-347(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; X83393; CAA58312.1; -; Genomic_DNA.
DR   PIR; S63608; S63608.
DR   AlphaFoldDB; P54387; -.
DR   SMR; P54387; -.
DR   PRIDE; P54387; -.
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   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..457
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182783"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   457 AA;  49557 MW;  1BF0E97F67078AC4 CRC64;
     MVLPHEPEFE QALHELETSL QPFLTTNPQY KKALEIIQVP ERVLQFRVTW EDDQGKPQVN
     RGFRVQYNSA LGPYKGGLRL HPTVNLSILK FLGFEQTFKN ALTGLSMGGG KGGSDFDPKG
     KSDNEIRRFC VAFMSELFRH IGQDTDVPAG DIGTGAREIG FLFGAYRRLK NEFTGMLTGK
     GINWGGSFIR PEATGYGLIY YVEHMIAHAC PEYSLDRPST LVAISGSGNV SQFTALKVIE
     LGATVLSLSD SKGSLISEKG YTKEAIEKIA ELKLKGGALE AIVDDLGAGY TYHAGKRPWT
     LLPQVHIALP GATQNEVSQE EAEALVKAGT RIVAEGSNMG CTEEAIAIFE NSRRASRAGV
     WYAPGKASNC GGVAVSGLEM AQNSQRLAWS TQEVDAKLKS IMAECYQICY TAGSRWSGEK
     VAEGVAEGEA LPSLLSGANL AGFIKVADAM KEQGDWW