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Database: UniProt
Entry: A0A1G7CID0_9DEIN
LinkDB: A0A1G7CID0_9DEIN
Original site: A0A1G7CID0_9DEIN 
ID   A0A1G7CID0_9DEIN        Unreviewed;       419 AA.
AC   A0A1G7CID0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=SAMN04488243_10141 {ECO:0000313|EMBL:SDE39118.1};
OS   Thermus arciformis.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=482827 {ECO:0000313|EMBL:SDE39118.1, ECO:0000313|Proteomes:UP000199446};
RN   [1] {ECO:0000313|EMBL:SDE39118.1, ECO:0000313|Proteomes:UP000199446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6992 {ECO:0000313|EMBL:SDE39118.1,
RC   ECO:0000313|Proteomes:UP000199446};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNBC01000001; SDE39118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7CID0; -.
DR   STRING; 482827.SAMN04488243_10141; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000199446; Unassembled WGS sequence.
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; 1.10.8.1210; -; 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;  44620 MW;  0241727CAD5F783C CRC64;
     MSLSAYRPPE DPGLWEAFLE RLERTLKVAQ VHPTTLEYLA HPKRLVTVSL PVVMDDGKVR
     VFQGFRVVHD IARGPAKGGV RLHPSVTLGQ TAGLAAWMTL KAAVYDLPFG GAAGGIAADP
     KALSPRELER LVRRYTAELV NLIGPDMDIL GPDLGTDQRV MAWIMDTYSM TVGSTVPGVV
     TGKPHALGGT EGRDDAAGLG VALVLKELAR RQGLPLEGAK VAVQGFGQVG GSFALHAQRM
     GLKVVAVSTG RGAIFQEEGL PVEEILVHYE ATGELPRYDL APEELFALPV DYLVLAALEG
     ALDGEVAKGV RAKAVLEAAN FGLTLEAEAY LLGKGVLVVP DLLTGGGGLL ASYLEWVQDL
     NMFFWSEEEV RRSFAKSVAK AVAEVCGKAE ALAADLRTGA LALALERVNE ATRLRGVYP
//
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