ID   DHE4_NEUSI              Reviewed;         454 AA.
AC   Q9HGU3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 72.
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 sitophila (Chrysonilia sitophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=40126;
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}.
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DR   EMBL; AF285428; AAG01159.1; -; mRNA.
DR   AlphaFoldDB; Q9HGU3; -.
DR   SMR; Q9HGU3; -.
DR   PRIDE; Q9HGU3; -.
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_0000182792"
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;  48835 MW;  5F1DEBDCC9799AEC CRC64;
     MSNLPSEPEF EQAYKELAYT LENSSLFQKH PEYRTALAVA SIPERVIQFR VVWEDDNGNV
     QVNRGYRVQF NSALGPYKGG LRLHPSVNLS ILKFLGFEQI FKNALTGLSM GGGKGGADFD
     PKGKSDAEIR RFCCAFMAEL HKHIGADTDV PAGDIGVGGR EIGYMFGAYR KAANRFEGVL
     TGKGLSWGGS LIRPEATGYG LVYYVGHMLE YSGAGSYAGK RVALSGSGNV AQYAALKLIE
     LGATVVSLSD SKGALVATGE SGITVEDINA IMAIKEARQS LTTFQHAGHV KWIEGARPWL
     HVGKVDIALP CATQNEVSKE EAEGLLAAGC KFVAEGSNMG CTLEAIEVFE NNRKEKKGEA
     VWYAPGKAAN CGGVAVSGLE MAQNSQRLNW TQAEVDEKLK DIMKNAFFNG LNTAKTYAEA
     AEGELPSLVA GSNIAGFVKV PQAMHDQGDW WSKN