ID   DHE2_SACS2              Reviewed;         420 AA.
AC   P80053;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 3.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Glutamate dehydrogenase 2;
DE            Short=GDH-2;
DE            EC=1.4.1.3;
GN   Name=gdhA-2; Synonyms=gdhA; OrderedLocusNames=SSO1907;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-420, ACETYLATION AT MET-2, AND METHYLATION AT
RP   LYS-254; LYS-260; LYS-372; LYS-391 AND LYS-392.
RC   STRAIN=DSM 5833 / MT-4;
RX   PubMed=1730244; DOI=10.1111/j.1432-1033.1992.tb19831.x;
RA   Maras B., Consalvi V., Chiaraluce R., Politi L., de Rosa M., Bossa F.,
RA   Scandurra R., Barra D.;
RT   "The protein sequence of glutamate dehydrogenase from Sulfolobus
RT   solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-
RT   epsilon-methyllysine related to thermostability?";
RL   Eur. J. Biochem. 203:81-87(1992).
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=1.4.1.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
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=1.4.1.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
CC   -!- SUBUNIT: Homohexamer.
CC   -!- PTM: Methylation of lysine residues may play a role in the thermal
CC       stability of this enzyme.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AE006641; AAK42099.1; -; Genomic_DNA.
DR   PIR; D90355; D90355.
DR   PIR; S20286; S20286.
DR   AlphaFoldDB; P80053; -.
DR   SMR; P80053; -.
DR   STRING; 273057.SSO1907; -.
DR   iPTMnet; P80053; -.
DR   PaxDb; 273057-SSO1907; -.
DR   EnsemblBacteria; AAK42099; AAK42099; SSO1907.
DR   KEGG; sso:SSO1907; -.
DR   PATRIC; fig|273057.12.peg.1968; -.
DR   eggNOG; arCOG01352; Archaea.
DR   HOGENOM; CLU_025763_1_2_2; -.
DR   InParanoid; P80053; -.
DR   BRENDA; 1.4.1.3; 6163.
DR   SABIO-RK; P80053; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
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; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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; Methylation; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   CHAIN           2..420
FT                   /note="Glutamate dehydrogenase 2"
FT                   /id="PRO_0000182761"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   MOD_RES         2
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   MOD_RES         254
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   MOD_RES         260
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   MOD_RES         372
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   MOD_RES         391
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   MOD_RES         392
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:1730244"
FT   CONFLICT        203
FT                   /note="E -> EE (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="K -> KK (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  46031 MW;  D9283C66D305EED5 CRC64;
     MMEEVLSSSL YTQQVKKLYK VGELLGLDNE TLETLSQPER IIQVKIQIRG SDGKLKTFMG
     WRSQHNSALG PYKGGVRYHP NVTQDEVEAL SMIMTWKNSL LLLPYGGGKG GVRVDPKKLT
     REELEQLSRK YIQAIYKYLG SELDIPAPDV NTDSQTMAWF LDEYIKITGK VDFAVFTGKP
     VELGGIGVRL YSTGLGVATI AKEAANKFIG GVEEARVIIQ GFGNVGYYAG KFLSEMGAKI
     VGVSDSKGGV INEKGIDVGK AIEIKEKTGS VINYPEGRKV TNEELLISDC DILIPAALEN
     VINKFNAPKV KAKLIVEGAN GPLTADADEI MRQRGIAVVP DILANAGGVV GSYVEWANNK
     MGEIISDEEA KKLIVDRMNN AFNTLYDYHQ KKLEDHDLRT AAMALAVDRV VRAMKARGIL
//