ID   A0A0G1U384_9BACT        Unreviewed;       500 AA.
AC   A0A0G1U384;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KKU60803.1};
GN   ORFNames=UX85_C0007G0090 {ECO:0000313|EMBL:KKU60803.1};
OS   Candidatus Beckwithbacteria bacterium GW2011_GWB1_47_15.
OC   Bacteria; Candidatus Beckwithbacteria.
OX   NCBI_TaxID=1618371 {ECO:0000313|EMBL:KKU60803.1, ECO:0000313|Proteomes:UP000033860};
RN   [1] {ECO:0000313|EMBL:KKU60803.1, ECO:0000313|Proteomes:UP000033860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKU60803.1}.
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DR   EMBL; LCNT01000007; KKU60803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1U384; -.
DR   Proteomes; UP000033860; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
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; 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|RuleBase:RU004417}.
FT   DOMAIN          262..499
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   500 AA;  54385 MW;  4CB6BE17BBC94E89 CRC64;
     MLAKTLTDLK KQAEQSFLAG AQFRVLKALT QIARDDKKIK LNQAVTSRIL YPSFTAELSF
     PVTFKGVTYM IMGLRSWFDD AKPFKPGQIV KGGIRYLGVE GLGDKVKTIK DIDAARQLAL
     DDVFALGLEM LVKNSGVNFS KVLKHSGFTK KHPRAKGLAV RGGSKGVLIG PRSSYLPDHN
     QFVWKVLAEF GYQLGLKGVV GWDRDVPAGD IATTGKVAGH SVMDGFVDGY ARAVKDLKLK
     MPRNLVVGVI TGKTPDRKYL GNKARAAATG FGTAVALKAW MEDKKIKPSE LKVVFDGAGN
     AALPAASLLV SQGIQVLGLT DSRSVILKPD GLTVKDLAQI GQTKAKRGSL SDWAKTQKGK
     VKVLAGKEKL WSQSGMNVLF VSSQERVVNR HNVKFLPRNL LIVDGANGPV TPLAEEILPK
     MGIDHLTGSF ANSGGVAGSL IEWAANVART SVNQKDSQTM IEWSIRTTYK QMRQLIKKGT
     VNSLADAFYY LAVKRIIERY
//