ID A0A1H1ZX87_9BACL Unreviewed; 382 AA.
AC A0A1H1ZX87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN05444162_4063 {ECO:0000313|EMBL:SDT38324.1};
OS Paenibacillaceae bacterium GAS479.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae.
OX NCBI_TaxID=1882832 {ECO:0000313|EMBL:SDT38324.1, ECO:0000313|Proteomes:UP000198637};
RN [1] {ECO:0000313|EMBL:SDT38324.1, ECO:0000313|Proteomes:UP000198637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS479 {ECO:0000313|EMBL:SDT38324.1,
RC ECO:0000313|Proteomes:UP000198637};
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}.
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DR EMBL; LT629764; SDT38324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1ZX87; -.
DR STRING; 1882832.SAMN05444162_4063; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000198637; Chromosome i.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198637}.
FT DOMAIN 158..379
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 70
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 106
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 382 AA; 42536 MW; EEEA2B25DFDB5E30 CRC64;
MQNEPYLIVE WNDTETEAKG WLCVYNFVNH YAGGGTRMHP TVTKEEVVRL AKTMAYKYKA
CESITTGGCK GGIAYDYKAP DAKDVLRRYL IAMSPYLKAG VSLGGDLGVD YGEVLRFFDE
TGIGLPQTKE MRDNPRIQQG IQDHDDMVSM KYDDFLMYDM VTGYGIGYSA DEAWKFKGGH
SGARVVVQGF GCAGASCALL MTKLGYKVVG IADANGMVVC ERGLDVKKLI DTKLPKGEMN
PDYFDSDYRI IPNTEWLDVD CDILIPVALE DVINASNAHR VRAQLVVEGA NIPVSVEGER
ILAKREVDIV TDFVANLGAI RFYDVIIFGL VEKSPQAVVD DIEQLCRRNT RKIFELAKLR
GLTQREVAFD IFAPDQSDHP DF
//
