ID Q8GR86_THETH Unreviewed; 419 AA.
AC Q8GR86;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA-1 {ECO:0000313|EMBL:BAC21185.1};
OS Thermus thermophilus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274 {ECO:0000313|EMBL:BAC21185.1};
RN [1] {ECO:0000313|EMBL:BAC21185.1}
RP NUCLEOTIDE SEQUENCE.
RA Miyazaki T., Miyazaki J., Nishiyama M., Yamane H.;
RT "Evolutionary and functional implication of two glutamate dehydrogenases
RT that are tandem manner in an extreme thermophilic bacterium, Thermus
RT thermophilus HB27.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; AB086412; BAC21185.1; -; Genomic_DNA.
DR RefSeq; WP_011173619.1; NZ_CP053287.1.
DR AlphaFoldDB; Q8GR86; -.
DR SMR; Q8GR86; -.
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:amino acid metabolic process; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185}.
FT DOMAIN 190..416
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT SITE 153
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 419 AA; 44568 MW; BEFCCEB1199EF6F7 CRC64;
MPLKAYRPPE DPGLWDTYLE WLERALKVAG VHPTTLEYLA HPKRLVTLSL PVVMDDGKVR
IFQGYRVVHD IARGPAKGGV RLDPGVTLGQ TAGLAAWMTL KAAVYDLPFG GAAGGIAVDP
KGLSPQELER LVRRYTAELV GLIGPDSDIL GPDLGADQQV MAWIMDTYSM TVGSTVPGVV
TGKPHALGGS EGRDDAAGLG ALLVLEALAK RRGLDLRGAR VVVQGLGQVG AAVALHAERL
GMRVVAVATS MGGMYAPEGL DVAEVLSAYE ATGSLPRLDL APEEVFGLEA EVLVLAAREG
ALDGDRARQV QAQAVVEVAN FGLNPEAEAY LLGKGALVVP DLLSGGGGLL ASYLEWVQDL
NMFFWSPEEV RERFETRVAR VVDAVCRRAE RGGLDLRMGA LALALERLDE ATRLRGVYP
//
