DHE2_SACS2
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 25-MAY-2022, entry version 129.
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; Crenarchaeota; 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}.
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; 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 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 OMA; WLQNRNG; -.
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 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 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
