ID   DHE2_YEAST              Reviewed;        1092 AA.
AC   P33327; D6VRD9;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
GN   Name=GDH2; OrderedLocusNames=YDL215C; ORFNames=D0892;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EBY23;
RX   PubMed=7901008; DOI=10.1111/j.1432-1033.1993.tb18266.x;
RA   Boles E., Lehnert W., Zimmermann F.K.;
RT   "The role of the NAD-dependent glutamate dehydrogenase in restoring growth
RT   on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant.";
RL   Eur. J. Biochem. 217:469-477(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
RX   PubMed=1682801; DOI=10.1128/mcb.11.12.6229-6247.1991;
RA   Miller S.M., Magasanik B.;
RT   "Role of the complex upstream region of the GDH2 gene in nitrogen
RT   regulation of the NAD-linked glutamate dehydrogenase in Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 11:6229-6247(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 848-1092.
RA   Rasmussen S.W.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   INTERACTION WITH NNK1, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
RX   PubMed=20489023; DOI=10.1126/science.1176495;
RA   Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA   Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA   Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA   Nesvizhskii A.I., Tyers M.;
RT   "A global protein kinase and phosphatase interaction network in yeast.";
RL   Science 328:1043-1046(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC       glutamate to ammonia and alpha-ketoglutarate.
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   -!- SUBUNIT: Homotetramer. Interacts with NNK1.
CC       {ECO:0000269|PubMed:20489023}.
CC   -!- INTERACTION:
CC       P33327; P36003: NNK1; NbExp=3; IntAct=EBI-5815, EBI-9796;
CC   -!- PTM: Phosphorylated by a complex containing the NNK1 kinase.
CC       {ECO:0000269|PubMed:20489023}.
CC   -!- DISRUPTION PHENOTYPE: Leads to rapamycin resistance when grown on
CC       glutamate as the sole nitrogen source. {ECO:0000269|PubMed:20489023}.
CC   -!- MISCELLANEOUS: Present with 7400 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; S66436; AAB20327.1; -; Genomic_DNA.
DR   EMBL; X99000; CAA67475.1; -; Genomic_DNA.
DR   EMBL; Z74263; CAA98793.1; -; Genomic_DNA.
DR   EMBL; X72015; CAA50894.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11649.1; -; Genomic_DNA.
DR   PIR; S37676; S37676.
DR   RefSeq; NP_010066.1; NM_001180275.1.
DR   AlphaFoldDB; P33327; -.
DR   SMR; P33327; -.
DR   BioGRID; 31830; 147.
DR   DIP; DIP-1689N; -.
DR   IntAct; P33327; 19.
DR   MINT; P33327; -.
DR   STRING; 4932.YDL215C; -.
DR   iPTMnet; P33327; -.
DR   MaxQB; P33327; -.
DR   PaxDb; P33327; -.
DR   PRIDE; P33327; -.
DR   EnsemblFungi; YDL215C_mRNA; YDL215C; YDL215C.
DR   GeneID; 851311; -.
DR   KEGG; sce:YDL215C; -.
DR   SGD; S000002374; GDH2.
DR   VEuPathDB; FungiDB:YDL215C; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   GeneTree; ENSGT00390000000854; -.
DR   HOGENOM; CLU_005220_0_0_1; -.
DR   InParanoid; P33327; -.
DR   OMA; LYCLPQN; -.
DR   BioCyc; MetaCyc:YDL215C-MON; -.
DR   BioCyc; YEAST:YDL215C-MON; -.
DR   BRENDA; 1.4.1.2; 984.
DR   PRO; PR:P33327; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P33327; protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IMP:SGD.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IMP:SGD.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016210; NAD-GDH_euk.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   PIRSF; PIRSF000184; GDH_NAD; 1.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1092
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182733"
FT   ACT_SITE        626
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   1092 AA;  124332 MW;  DF8358D831E4545F CRC64;
     MLFDNKNRGA LNSLNTPDIA SLSISSMSDY HVFDFPGKDL QREEVIDLLD QQGFIPDDLI
     EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF FAKSKFNGIQ PRLFSIKNKI
     ITNDNHAIFM ESNTGVSISD SQQKNFKFAS DAVGNDTLEH 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 PFKNDQEFEA YLNKFIPNDS PDLLILKTLN IFNKSILKTN FFITRKVAIS
     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 DELCRLAHER 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