ID   DHE4_TUBBO              Reviewed;         457 AA.
AC   Q9HFR6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-MAY-2023, entry version 74.
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=GDH;
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND23280867; DOI=10.1046/j.1469-8137.2002.00409.x;
RA   Vallorani L., Polidori E., Sacconi C., Agostini D., Pierleoni R.,
RA   Piccoli G., Zeppa S., Stocchi V.;
RT   "Biochemical and molecular characterization of NADP-glutamate dehydrogenase
RT   from the ectomycorrhizal fungus Tuber borchii.";
RL   New Phytol. 154:779-790(2002).
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; AF309087; AAG28788.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HFR6; -.
DR   SMR; Q9HFR6; -.
DR   BRENDA; 1.4.1.4; 7423.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
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; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
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   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 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.
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_0000182795"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   457 AA;  50155 MW;  C32DE331D01DF612 CRC64;
     MSNLAPEPEF QQAYNELVHS LRDQNSSRLP QILRLLCLSS PPERVIQFRV TWEDDKGNFQ
     VNRGYRVQFN SALGPYKGGL RFHPTVNLSI LKFLGFEQTF KNALTGLNMG GGKGGSDFDP
     KGKSDNEIRR FCYSFMRELS KHIGQFTDVP AGDIGVGGRE IGYLFGAYES YKNQFEGVLT
     GKGITWGGSL IRPEATGYGL VYYVAHMISY ASGGKETFAG KRVAISGSGN VAQYAALKVL
     ELGGKVITLS DSKGALIATG EEGFNETDIE LIAKLKLDRG YLTQLHAAED SFKSRFKYLP
     GERPWCHVDK VDVALPSATQ NEVSEQEAKE LIASGCKFLA EGSNMGSTQE AINVYEEDRK
     SRKADGLWYG PAKAANCGGV AVSGLEMAQN SQRLTWTSEQ VDKELAGIME RCFWNCLNPA
     KEYFDIAEGE LPSLVAGANI AGYVKVVNAM KAQGDWW
//