ID   DHE4_GIBFU              Reviewed;         451 AA.
AC   Q96VJ7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=GDH2;
OS   Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=m567;
RA   Tudzynski B.;
RT   "Cloning and characterization of the NADP-depending glutamate dehydrogenase
RT   gene from Gibberella fujikuroi.";
RL   Submitted (JUL-2001) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ315471; CAC45043.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96VJ7; -.
DR   SMR; Q96VJ7; -.
DR   PRIDE; Q96VJ7; -.
DR   eggNOG; KOG2250; Eukaryota.
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..451
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182787"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   451 AA;  48826 MW;  171867950A9B8E85 CRC64;
     MSHLPQEPEF EQAYGELASA LENSSLFNEH PEYRTALAVA AIPERVIQFR VVWNDDKGNL
     QVNRGYRVQF NGALGPYKGG LRFHPSVNLS ILKFLGFEQI FKNALTGLNM GGGKGGADFD
     PKGKSDAEIR RFCQAFMTEL SKHIGAETDV PAGDIGVGGR EIGYLFGAYR KFANRWEGVL
     TGKGLSWGGS LIRPEATGYG LVYYVEYMLK HANRGTFEGK RVALSGSGNV AQYAALKIIE
     LGGSVVSLSD SKGALVAKEG SSFTPEQIHN IAALKIKHQA LTTFEHDGQF TWIEGARPWV
     HVGKVDIALP SATQNEVSKE EAQALVDAGA FIVAEGSNMG CTAEAIDVFE AHRKEKGAEA
     LWYAPGKASN CGGVAVSGLE MAQNSQRIQW TEKEVDDRLK AIMKDAFVAG LETAQKYVEA
     KEGELPSLIA GSNIAGFIKV AEAMHDQGDW F