ID   DHE_HALSI               Reviewed;         416 AA.
AC   F2Z610;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Glutamate dehydrogenase A2;
DE            EC=1.4.1.-;
GN   Name=gdhA2;
OS   Halobacterium salinarum (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=2242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=NRC-36014;
RX   PubMed=15780999; DOI=10.1016/j.gene.2005.01.011;
RA   Ingoldsby L.M., Geoghegan K.F., Hayden B.M., Engel P.C.;
RT   "The discovery of four distinct glutamate dehydrogenase genes in a strain
RT   of Halobacterium salinarum.";
RL   Gene 349:237-244(2005).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Strain NRC-36014 contains 4 distinct glutamate
CC       dehydrogenases while strain NRC-1 contains only 3.
CC       {ECO:0000305|PubMed:15780999}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AY840086; AAW19066.1; -; Genomic_DNA.
DR   PIR; B84276; B84276.
DR   RefSeq; WP_010902870.1; NZ_CP038631.1.
DR   AlphaFoldDB; F2Z610; -.
DR   SMR; F2Z610; -.
DR   GeneID; 5952864; -.
DR   GeneID; 62884561; -.
DR   OMA; TNAWWWW; -.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..416
FT                   /note="Glutamate dehydrogenase A2"
FT                   /id="PRO_0000428790"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   416 AA;  45332 MW;  11DA56F6C24BEB74 CRC64;
     MTESGPLENM LAQMEQAREY VDIDDGIYER LKSPERTLSV SLPVRMDDGS VEVFDAYRCQ
     FDSARGPYKG GIRYHPTVSE EEVSALAGWM TWKTALVDLP FGGAKGGIVC NPKELSDNEI
     EQLTRRYTEG IRRMIGPETD IPAPDMNTDP RTMAWVMDTY SVYQGYAVPE VVTGKPPEIG
     GTDGRVEATG RGVSIITEET FEYFDTDIQD ADVAIQGFGN VGSVTADLLS ERGANIVAVS
     DVTGAIHDPT GLDIADVQAY ADANGGRLEG YDAEPISNDD LLTLDVDALI PAAIEDVITV
     DVAERLAADV IVEAANGPTT FDAAQVLSDR GVPVVPDILA NAGGVIVSYL EWVQNSQQYS
     WDVEEVNRDL RQRLTGAFDE MLVAYEDRNI PTLRTAAYTI ALERSADAHE FRGLFP