ID   DHE4_NEUIN              Reviewed;         454 AA.
AC   Q9HGU4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 70.
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   Neurospora intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5142;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang F., Tien P.;
RT   "The Neurospora GDH gene can increase the nitrogen assimilation in
RT   transgene tobacco.";
RL   Submitted (JUL-2000) 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; AF285427; AAG01158.1; -; mRNA.
DR   AlphaFoldDB; Q9HGU4; -.
DR   SMR; Q9HGU4; -.
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   2: Evidence at transcript level;
KW   Acetylation; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..454
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182791"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  48888 MW;  71D5C8DFD849CF39 CRC64;
     MSNLPSEPEF EQAYKELAYT LENSSLFQKH PEYRTALTVA SIPERVIQFR VVWEDDNGNV
     QVNRGYRVQF NSALGPYKGG LRLHPSVNLS ILKFLGFEQI FKNALTGLSM GGGKGGADFD
     PKGKSDAEIR RFCCAFMAEL HKHIGADTDV PAGDIGVGGR EIGYMFGAYR KAANRFEGVL
     TGKGLSWGGS LIRPEATGYG LVYYVGHMLE YSGAGSYAGK RVALSGSGNV AQYAALKLIE
     LGATVVSLSD SKGALVATGE SGITVEDINA VMAIKEARQS LTSFQHAGHL KWIEGARPWL
     HVGKVDIALP CATQNEVSKE EAEGLLAAGC KFVAEGSNMG CTLEAIEVFE NHRKEKKGEA
     VWYAPGKAAN CGGVAVSGLE MAQNSQRLNW TQAEVDEKLK DIMKNAFFNG LNTAKIYVEA
     AEGELPSLVA GSNIAGFVKV AQAMHDQGDW WSKN