ID   DHE4_BOTFU              Reviewed;         450 AA.
AC   O93934;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 77.
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   Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=40559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2850;
RA   Santos M.;
RT   "Cloning and regulation of the gdhA gene from Botrytis cinerea.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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; AF109684; AAC95390.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93934; -.
DR   SMR; O93934; -.
DR   PRIDE; O93934; -.
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..450
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182784"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   450 AA;  49044 MW;  6EDAFAB75B03C93A CRC64;
     MSNLPSEPEF EQAYNELAST LENSTLFEKN PEYRTALKVV SIPERVIQFR VVWEDDKNQV
     QVNRGYRVQF NSALGPYKGG LRFHPTVNLS VLKFLGFEQI FKNALTGLNI GGGKGGADFD
     PKGKSDNEIR RFCVSFMREL SKHIGADTDV PAGDINVGGR EIGFLFGAYK AIQNKWEGVL
     TGKGGSWGGS LIRPEATGYG LVYYVAHMIQ YAGQGSFQGK RVAISGSGNV AQYAALKCIE
     LGATVVSLSD SQGSLIAEGD AYFTPEDVGK IAELKLKRQS LTAFEHGGKY KYIEGSRPWT
     HVKVDVALPC ATQNEVSKEE AESLVASGAR YIAEGSNMGC TQEAIDVFEA ERKEKKDKAI
     WYAPGKAANA GGVAVSGLEM AQNSARISWT QEEVDEKLKD IMKNAFETGL ETPKKYVEAK
     DGEYPSLVAG SNIAGFVKVA SAMHNHGDWW