ID   DHE4_PENCH              Reviewed;         461 AA.
AC   Q9URS1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10499259; DOI=10.1007/s002530051509;
RA   Diez B., Mellado E., Rodriguez M., Bernasconi E., Barredo J.L.;
RT   "The NADP-dependent glutamate dehydrogenase gene from Penicillium
RT   chrysogenum and the construction of expression vectors for filamentous
RT   fungi.";
RL   Appl. Microbiol. Biotechnol. 52:196-207(1999).
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; AF056974; AAF00006.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9URS1; -.
DR   SMR; Q9URS1; -.
DR   PRIDE; Q9URS1; -.
DR   PhylomeDB; Q9URS1; -.
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..461
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182793"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   461 AA;  49832 MW;  76A014A29150B4DE CRC64;
     MMQNLPFEPE FEQAYKELAS TLENSTLFQK KPEYRKALQV VSVPERVIQF RVVWEDDKGQ
     VQINRGYRVQ FNSALGPYKG GLRFHPTVNL SILKFLGFEQ IFKNALTGLN MGGGKGGSDF
     DPKGKTDNEI RRFCVSFMTE LCKHIGADTD VPAGDIGVTG REVGFMFGQY KKIRNQWEGV
     LTGKGGSWGG SLIRPEATGY GVVYYVEHMI QHASGGKESF AGKRVAISGS GNVAQYAALK
     VIELGGSVIS LSDSQGALVL NGEEGSFTAE EINTIAEIKV QRKQIAELAT QDAFSSKFKY
     IPGARPWTNI AGRIDVALPS ATQNEVSGDE AKALIAAGCK FIAEGSNMGS TQEAIDVFEA
     HRDANPGAAA IWYAPGKAAN AGGVAVSGLE MAQNSARVNW SREEVDSRLK KIMEDCFNNG
     LSTAKEYVTP AEGVLPSLVA GSNIAGFTKV AEAMKEHGDW W