DHE5_YEAST
ID DHE5_YEAST Reviewed; 457 AA.
AC P39708; D6VPF7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NADP-specific glutamate dehydrogenase 2;
DE Short=NADP-GDH 2;
DE EC=1.4.1.4;
DE AltName: Full=NADP-dependent glutamate dehydrogenase 2;
GN Name=GDH3; OrderedLocusNames=YAL062W; ORFNames=FUN51;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
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).
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; U12980; AAC04972.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06927.1; -; Genomic_DNA.
DR PIR; S51960; S51960.
DR RefSeq; NP_009339.1; NM_001178204.1.
DR AlphaFoldDB; P39708; -.
DR SMR; P39708; -.
DR BioGRID; 31768; 59.
DR DIP; DIP-4325N; -.
DR IntAct; P39708; 2.
DR MINT; P39708; -.
DR STRING; 4932.YAL062W; -.
DR iPTMnet; P39708; -.
DR MaxQB; P39708; -.
DR PaxDb; P39708; -.
DR PRIDE; P39708; -.
DR EnsemblFungi; YAL062W_mRNA; YAL062W; YAL062W.
DR GeneID; 851237; -.
DR KEGG; sce:YAL062W; -.
DR SGD; S000000058; GDH3.
DR VEuPathDB; FungiDB:YAL062W; -.
DR eggNOG; KOG2250; Eukaryota.
DR GeneTree; ENSGT00390000000854; -.
DR HOGENOM; CLU_025763_2_1_1; -.
DR InParanoid; P39708; -.
DR OMA; HEPEFIQ; -.
DR BioCyc; MetaCyc:YAL062W-MON; -.
DR BioCyc; YEAST:YAL062W-MON; -.
DR PRO; PR:P39708; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39708; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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 InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Isopeptide bond; NADP; Oxidoreductase; Reference proteome; Ubl conjugation.
FT CHAIN 1..457
FT /note="NADP-specific glutamate dehydrogenase 2"
FT /id="PRO_0000182799"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 175..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P07262"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P07262"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P07262"
SQ SEQUENCE 457 AA; 49627 MW; 81B30625038B1888 CRC64;
MTSEPEFQQA YDEIVSSVED SKIFEKFPQY KKVLPIVSVP ERIIQFRVTW ENDNGEQEVA
QGYRVQFNSA KGPYKGGLRF HPSVNLSILK FLGFEQIFKN ALTGLDMGGG KGGLCVDLKG
KSDNEIRRIC YAFMRELSRH IGKDTDVPAG DIGVGGREIG YLFGAYRSYK NSWEGVLTGK
GLNWGGSLIR PEATGFGLVY YTQAMIDYAT NGKESFEGKR VTISGSGNVA QYAALKVIEL
GGIVVSLSDS KGCIISETGI TSEQIHDIAS AKIRFKSLEE IVDEYSTFSE SKMKYVAGAR
PWTHVSNVDI ALPCATQNEV SGDEAKALVA SGVKFVAEGA NMGSTPEAIS VFETARSTAT
NAKDAVWFGP PKAANLGGVA VSGLEMAQNS QKVTWTAERV DQELKKIMIN CFNDCIQAAQ
EYSTEKNTNT LPSLVKGANI ASFVMVADAM LDQGDVF