ID   DHE4_YEAST              Reviewed;         454 AA.
AC   P07262; D6W368; Q08899;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 208.
DE   RecName: Full=NADP-specific glutamate dehydrogenase 1 {ECO:0000303|PubMed:2932370};
DE            Short=NADP-GDH 1;
DE            EC=1.4.1.4 {ECO:0000269|PubMed:2932370, ECO:0000269|PubMed:2989290};
DE   AltName: Full=NADP-dependent glutamate dehydrogenase 1 {ECO:0000303|PubMed:2989290};
GN   Name=GDH1 {ECO:0000303|PubMed:2989290}; Synonyms=DHE4, URE1;
GN   OrderedLocusNames=YOR375C;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2989290; DOI=10.1016/s0021-9258(17)39500-5;
RA   Moye W.S., Amuro N., Rao J.K.M., Zalkin H.;
RT   "Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine
RT   dinucleotide phosphate-dependent glutamate dehydrogenase.";
RL   J. Biol. Chem. 260:8502-8508(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=2932370; DOI=10.1016/0378-1119(85)90279-3;
RA   Nagasu T., Hall B.D.;
RT   "Nucleotide sequence of the GDH gene coding for the NADP-specific glutamate
RT   dehydrogenase of Saccharomyces cerevisiae.";
RL   Gene 37:247-253(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 79-88; 157-165 AND 236-246.
RC   STRAIN=ATCC 38531 / Y41;
RX   PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA   Norbeck J., Blomberg A.;
RT   "Protein expression during exponential growth in 0.7 M NaCl medium of
RT   Saccharomyces cerevisiae.";
RL   FEMS Microbiol. Lett. 137:1-8(1996).
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-325 AND LYS-371, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
RN   [9]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-325; LYS-371 AND LYS-433, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Catalyzes the incorporation of an ammonium ion into alpha-
CC       ketoglutarate to form L-glutamate, the major route of assimilation of
CC       ammonia into an organic form in yeast. {ECO:0000305|PubMed:2989290}.
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         Evidence={ECO:0000269|PubMed:2932370, ECO:0000269|PubMed:2989290};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11614;
CC         Evidence={ECO:0000269|PubMed:2989290};
CC   -!- SUBUNIT: Homohexamer.
CC   -!- MISCELLANEOUS: Present with 77500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; M11297; AAB03898.1; -; Genomic_DNA.
DR   EMBL; M10590; AAA34642.1; -; Genomic_DNA.
DR   EMBL; Z75283; CAA99706.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11134.1; -; Genomic_DNA.
DR   PIR; S67287; A25275.
DR   RefSeq; NP_015020.3; NM_001183795.3.
DR   AlphaFoldDB; P07262; -.
DR   SMR; P07262; -.
DR   BioGRID; 34758; 120.
DR   DIP; DIP-1329N; -.
DR   IntAct; P07262; 53.
DR   MINT; P07262; -.
DR   STRING; 4932.YOR375C; -.
DR   iPTMnet; P07262; -.
DR   MaxQB; P07262; -.
DR   PaxDb; 4932-YOR375C; -.
DR   PeptideAtlas; P07262; -.
DR   EnsemblFungi; YOR375C_mRNA; YOR375C; YOR375C.
DR   GeneID; 854557; -.
DR   KEGG; sce:YOR375C; -.
DR   AGR; SGD:S000005902; -.
DR   SGD; S000005902; GDH1.
DR   VEuPathDB; FungiDB:YOR375C; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   GeneTree; ENSGT00390000000854; -.
DR   HOGENOM; CLU_025763_2_0_1; -.
DR   InParanoid; P07262; -.
DR   OMA; MIMGWMM; -.
DR   OrthoDB; 45283at2759; -.
DR   BioCyc; MetaCyc:YOR375C-MONOMER; -.
DR   BioCyc; YEAST:YOR375C-MONOMER; -.
DR   BRENDA; 1.4.1.4; 984.
DR   BioGRID-ORCS; 854557; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P07262; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P07262; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IDA:SGD.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IMP:SGD.
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   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Isopeptide bond; NADP;
KW   Oxidoreductase; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..454
FT                   /note="NADP-specific glutamate dehydrogenase 1"
FT                   /id="PRO_0000182798"
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"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CROSSLNK        325
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        371
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        433
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        83
FT                   /note="V -> G (in Ref. 1; AAB03898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="V -> L (in Ref. 1; AAB03898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="S -> L (in Ref. 1; AAB03898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="D -> V (in Ref. 1; AAB03898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358..364
FT                   /note="ATGPSEA -> PLDQAT (in Ref. 2; AAA34642)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  49570 MW;  707F921B6FE5B5B1 CRC64;
     MSEPEFQQAY EEVVSSLEDS TLFEQHPEYR KVLPIVSVPE RIIQFRVTWE NDKGEQEVAQ
     GYRVQYNSAK GPYKGGLRFH PSVNLSILKF LGFEQIFKNS LTGLDMGGGK GGLCVDLKGR
     SNNEIRRICY AFMRELSRHI GQDTDVPAGD IGVGGREIGY LFGAYRSYKN SWEGVLTGKG
     LNWGGSLIRP EATGYGLVYY TQAMIDYATN GKESFEGKRV TISGSGNVAQ YAALKVIELG
     GTVVSLSDSK GCIISETGIT SEQVADISSA KVNFKSLEQI VNEYSTFSEN KVQYIAGARP
     WTHVQKVDIA LPCATQNEVS GEEAKALVAQ GVKFIAEGSN MGSTPEAIAV FETARSTATG
     PSEAVWYGPP KAANLGGVAV SGLEMAQNSQ RITWTSERVD QELKRIMINC FNECIDYAKK
     YTKDGKVLPS LVKGANIASF IKVSDAMFDQ GDVF
//