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
//
