DHE4_TUBBO
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 25-MAY-2022, entry version 71.
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 PRIDE; 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: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_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