ID   DHE4_SACU7              Reviewed;         454 AA.
AC   Q8TFF6;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=NADP-specific glutamate dehydrogenase 1;
DE            Short=NADP-GDH 1;
DE            EC=1.4.1.4;
DE   AltName: Full=NADP-dependent glutamate dehydrogenase 1;
GN   Name=GDH1;
OS   Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS   / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS   uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=659244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=623-6C / CBS 9787 / CLIB 533;
RA   Nguyen H.V.;
RT   "New S. pastorianus strains and Saccharomyces natural hybrids revealed by
RT   polyphasis identification of CBS strains formerly uncompletely identified
RT   by conventional method.";
RL   Submitted (OCT-2001) 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; AJ418037; CAD10750.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TFF6; -.
DR   SMR; Q8TFF6; -.
DR   IntAct; Q8TFF6; 1.
DR   MINT; Q8TFF6; -.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
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   InterPro; IPR033922; NAD_bind_Glu_DH.
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..454
FT                   /note="NADP-specific glutamate dehydrogenase 1"
FT                   /id="PRO_0000182797"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         174..203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  49425 MW;  98DF52A68BDE0D12 CRC64;
     MSEPEFQQAY DEVVSSLEDS TLFEQHPKYR KVLPIVSVPE RIIQFRVTWE NDKGEQEVAQ
     GYRVQYNSAK GPYKGGLRFH PSVNLSILKF LGFEQIFKNS LTGLDMGGGK GGLCVDLKGR
     SNNEIRRICY AFMRELSRHI GQDTDVPAGD IGVGGREIGY LFGAYRTYKN SWEGVLTGKG
     LNWGGSLIRP EATGYGLVYY TQAMIDYATN GKESFEGKRV TISGSGNVAQ FAALKVIELG
     GTVVSLSDSK GCIISETGIT SEQVADISSA KVNFKSLEQI VGEYSTFTEN KVQYISGARP
     WTHVQKVDIA LPCATQNEVS GDEAKALVAQ GVKFVAEGSN MGSTPEAIAV FETARATAST
     LKESVWYGPP KAANLGGVAV SGLEMAQNSQ RITWSSERVD QELKKIMVNC FNECIDSAKK
     YTKEGNALPS LVKGANIASF IKVSDAMFDQ GDVF
//