ID   A0A0G1YK49_9BACT        Unreviewed;       363 AA.
AC   A0A0G1YK49;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=UY55_C0001G0141 {ECO:0000313|EMBL:KKW15387.1};
OS   Candidatus Jorgensenbacteria bacterium GW2011_GWB1_50_10.
OC   Bacteria; Candidatus Jorgensenbacteria.
OX   NCBI_TaxID=1618665 {ECO:0000313|EMBL:KKW15387.1, ECO:0000313|Proteomes:UP000034224};
RN   [1] {ECO:0000313|EMBL:KKW15387.1, ECO:0000313|Proteomes:UP000034224}
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|PIRNR:PIRNR000185,
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:KKW15387.1}.
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DR   EMBL; LCQK01000001; KKW15387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1YK49; -.
DR   STRING; 1618665.UY55_C0001G0141; -.
DR   Proteomes; UP000034224; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   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   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   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185}.
FT   DOMAIN          141..361
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        74
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            111
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   363 AA;  39079 MW;  1AE8F295C48D92DF CRC64;
     MEIKSDKFGP ENVIEVYEPE IGMKGFLVID NTVLGPGKGG IRMTPNVTKE EVWRLARTMT
     WKNALADIPF GGAKAGIVWQ GGDGAQKKQF VQSFAKRIKD FMPDRYIAGP DVSTGEREMR
     WFVEATGDPR SATGKPESFG GLPHELGSTG FGVAEAAAVA AEIGGVNIKN ASVAIEGFGN
     VGKFAAKHLV GKGAKIVAVA DSEGMIYDPR GLDVLKLIEI KSGGCAVCEY PGGEKLPRGD
     VFGLEVDILI PASVTDVINE KNEKSIKSKI IVEGANIPMT EEIEKELWQR NVLVVPDMVA
     NAGGVISSYA EYMGYGPDKM FGLVEEKIRK SVGAVLRLSL EQKRNPREVA LEIARAKIEA
     KVL
//