ID   C8Z6Q4_YEAS8            Unreviewed;      1092 AA.
AC   C8Z6Q4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   ORFNames=EC1118_1D22_0397g {ECO:0000313|EMBL:CAY79070.1};
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY79070.1, ECO:0000313|Proteomes:UP000000286};
RN   [1] {ECO:0000313|EMBL:CAY79070.1, ECO:0000313|Proteomes:UP000000286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse
RC   {ECO:0000313|Proteomes:UP000000286};
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA   Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC       glutamate to ammonia and alpha-ketoglutarate.
CC       {ECO:0000256|PIRNR:PIRNR000184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN393064; CAY79070.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z6Q4; -.
DR   HOGENOM; CLU_005220_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D22.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016210; NAD-GDH_euk.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   PIRSF; PIRSF000184; GDH_NAD; 1.
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   NAD {ECO:0000256|PIRNR:PIRNR000184};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184}.
FT   DOMAIN          715..986
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   1092 AA;  124318 MW;  10352D08041410B4 CRC64;
     MLFDNKNRGA LNSLNTPDIA SLSISSMSDY HVFDFPGKDL QREEVIDLLD QQGFIPDDLI
     EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF FAKSKFNGIQ PRLFSIKNKI
     ITNDNHAIFM ESNTGVSISD SQQKNFKFAS EAVGNDTLEH GKDTIKKNRI EMDDSCPPYE
     LDSEIDDLFL DNKSQKNCRL VSFWAPESEL KLTFVYESVY PNDDPAGVDI SSQDLLKGDI
     ESISDKTMYK VSSNENKKLY GLLLKLVKER EGPVIKTTRS VENKDEIRLL VAYKRFTTKR
     YYSALNSLFH YYKLKPSKFY LESFNVKDDD IIIFSVYLNE NQQLEDVLLH DVEAALKQVE
     REASLLYAIP NNSFHEVYQR RQFSPKEAIY AHIGAIFINH FVNRLGSDYQ NLLSQITIKR
     NDTTLLEIVE NLKRKLRNET LTQQTIINIM SKHYTIISKL YKNFAQIHYY HNSTKDMEKT
     LSFQRLEKVE PFKNEQEFEA YLNKFIPNDS PDLLILKTLN IFNKSILKTN FYITRKVAIS
     FRLDPSLVMT KFEYPETPYG IFFVVGNTFK GFHIRFRDIA RGGIRIVCSR NQDIYDLNSK
     NVIDENYQLA STQQRKNKDI PEGGSKGVIL LNPGLVEHDQ TFVAFSQYVD AMIDILINDP
     LKENYVNLLP KEEILFFGPD EGTAGFVDWA TNHARVRNCP WWKSFLTGKS PSLGGIPHDE
     YGMTSLGVRA YVNKIYETLN LTNSTVYKFQ TGGPDGDLGS NEILLSSPNE CYLAILDGSG
     VLCDPKGLDK DELCRLAHAR KMISDFDTSK LSNNGFFVSV DAMDIMLPNG TIVANGTTFR
     NTFHTQIFKF VDHVDIFVPC GGRPNSITLN NLHYFVDEKT GKCKIPYIVE GANLFITQPA
     KNALEEHGCI LFKDASANKG GVTSSSMEVL ASLALNDNDF VHKFIGDVSG ERSALYKSYV
     VEVQSRIQKN AELEFGQLWN LNQLNGTHIS EISNQLSFTI NKLNDDLVAS QELWLNDLKL
     RNYLLLDKII PKILIDVAGP QSVLENIPES YLKVLLSSYL SSTFVYQNGI DVNIGKFLEF
     IGGLKREAEA SA
//