ID   A0A1Q9NZI4_9ARCH        Unreviewed;       310 AA.
AC   A0A1Q9NZI4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=NAD(P)-specific glutamate dehydrogenase {ECO:0000313|EMBL:OLS27431.1};
DE            EC=1.4.1.2 {ECO:0000313|EMBL:OLS27431.1};
DE   Flags: Fragment;
GN   Name=gdhA {ECO:0000313|EMBL:OLS27431.1};
GN   ORFNames=HeimC3_04300 {ECO:0000313|EMBL:OLS27431.1};
OS   Candidatus Heimdallarchaeota archaeon LC_3.
OC   Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX   NCBI_TaxID=1841598 {ECO:0000313|EMBL:OLS27431.1, ECO:0000313|Proteomes:UP000186063};
RN   [1] {ECO:0000313|EMBL:OLS27431.1, ECO:0000313|Proteomes:UP000186063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC_3 {ECO:0000313|EMBL:OLS27431.1};
RX   PubMed=28077874; DOI=10.1038/nature21031;
RA   Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA   Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA   Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA   Baker B.J., Spang A., Ettema T.J.G.;
RT   "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL   Nature 541:353-358(2017).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLS27431.1}.
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DR   EMBL; MDVS01000007; OLS27431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9NZI4; -.
DR   Proteomes; UP000186063; Unassembled WGS sequence.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_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; 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   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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          62..308
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OLS27431.1"
SQ   SEQUENCE   310 AA;  33818 MW;  330372192670BFF6 CRC64;
     VMRFCQSFMG ELFRHIGANT DVPAGDIGVG GREIGYMFGI YKKIKNIFEG VLTGKGLEYG
     GSLIRPEATG YGCVYFTREM LLARGVNDGF KNKNVTISGS GNVAQYSTEK VLELGGKVLT
     LSDSSGSIYD PDGIDKDKLA WVMELKNVRR GRIKEYVDKF TNAQYFAGKR PWMLGKFDIA
     LPSATQNEIN LEEATYLVNN GVLAVGEGAN MPTEPDAMDH FIENGVSFGL GKAANAGGVA
     VSGLEMSQNS LRYSWTREEV DQRLHNIMKS IHKNAYETSE RFGVKGNYVV GANIAGFLKI
     ARAMTAQGVV
//