ID A0A0S7XLX9_9BACT Unreviewed; 206 AA.
AC A0A0S7XLX9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KPJ63490.1};
DE Flags: Fragment;
GN ORFNames=AMK68_03890 {ECO:0000313|EMBL:KPJ63490.1};
OS candidate division KD3-62 bacterium DG_56.
OC Bacteria; candidate division KD3-62.
OX NCBI_TaxID=1704032 {ECO:0000313|EMBL:KPJ63490.1, ECO:0000313|Proteomes:UP000052020};
RN [1] {ECO:0000313|EMBL:KPJ63490.1, ECO:0000313|Proteomes:UP000052020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_56 {ECO:0000313|EMBL:KPJ63490.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {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:KPJ63490.1}.
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DR EMBL; LIZY01000083; KPJ63490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XLX9; -.
DR Proteomes; UP000052020; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
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 PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 1..206
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:KPJ63490.1"
SQ SEQUENCE 206 AA; 22029 MW; 857B2148DE84C4B4 CRC64;
LEGATVAVQG YGNAGSNFAQ LVHEQDGCRI VAVSDSKGGI HDPHGLDPTS VLEHKKSHGT
VVGYPGADVI TNDQLLEVDC DILAPSALEN VITDVNADKL RCSIIVELAN GPTTPSADDI
LHTRGVVVLP DILANAGGVT VSCYEWQQNL ARQKWSAEKV DSMLEKTMHT NTLSVFETTQ
GYAVTPRVGA YILAIGRIAE KLRDQR
//
