ID   DHE4_SCHOC              Reviewed;         459 AA.
AC   P29507;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-MAY-2023, entry version 82.
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=GDHA;
OS   Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX   NCBI_TaxID=27300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1934128; DOI=10.1007/bf00326236;
RA   de Zoysa P.A., Connerton I.F., Watson D.C., Johnston J.R.;
RT   "Cloning, sequencing and expression of the Schwanniomyces occidentalis
RT   NADP-dependent glutamate dehydrogenase gene.";
RL   Curr. Genet. 20:219-224(1991).
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; S64476; AAB20267.1; -; Genomic_DNA.
DR   PIR; S17907; S17907.
DR   AlphaFoldDB; P29507; -.
DR   SMR; P29507; -.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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   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..459
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182796"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   459 AA;  49831 MW;  03047D3D1C05B79C CRC64;
     MIKNGLPHEP EFQQAYNELV SALEESTLFT EKPEYKKVIP VVSIPERIIQ FRVAWENDNG
     DVEVNNGFRV QFNSSLGPYK GGLRFHPSVN LSILKFLGFE QIFKNALTGL SMGGGKGGCD
     FNPKGRSDGE IRRFCVAFMR QLARYIGADT DVPAGDIGVG GREIGYLFGA YKQMQNNWYG
     VLTGKGLTWG GSLIRPEATG YVSFTTLKKM IEKATNGKES FKGKRVELSG SGNVAQYAAL
     KVIELGGIVV SLSDSKGSIV SKNGIVPEQV LEIAAAKLKF KSLEEITKES VKLFSGENSV
     EYLAGVRPWA KVGHFDVALP SATQKEVSGE EEAKALVEAG CKYIAEGSNM GSTKEAIDVF
     EANRSNNVWY APGKAANCGG VAVSGLEMAQ NSQRVQWSAE EVDAKLKNIM YTCFDNCYDP
     AIKYSAEKNA DGLPSLLKGA NIASFIKVAD AMFDQGDVY
//