ID F2F941_SOLSS Unreviewed; 364 AA.
AC F2F941;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase {ECO:0000313|EMBL:BAK16136.1};
GN OrderedLocusNames=SSIL_1713 {ECO:0000313|EMBL:BAK16136.1};
OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK16136.1, ECO:0000313|Proteomes:UP000006691};
RN [1] {ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA Morohoshi T., Someya N., Ikeda T.;
RT "Genome sequence of Solibacillus silvestris StLB046.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAK16136.1, ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK16136.1,
RC ECO:0000313|Proteomes:UP000006691};
RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT "Complete genome sequence and characterization of the N-acylhomoserine
RT lactone-degrading gene of the potato leaf-associated Solibacillus
RT silvestris.";
RL J. Biosci. Bioeng. 113:20-25(2012).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR EMBL; AP012157; BAK16136.1; -; Genomic_DNA.
DR RefSeq; WP_014823491.1; NC_018065.1.
DR AlphaFoldDB; F2F941; -.
DR STRING; 1002809.SSIL_1713; -.
DR KEGG; siv:SSIL_1713; -.
DR PATRIC; fig|1002809.3.peg.1732; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_0_0_9; -.
DR Proteomes; UP000006691; Chromosome.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01075; NAD_bind_Leu_Phe_Val_DH; 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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 2.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000006691}.
FT DOMAIN 144..351
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 364 AA; 39477 MW; 0DA4739A37AF3A05 CRC64;
MEIFKYMQKY DFEQVVFCQD EASGLKAVIA IHDTTLGPAL GGSRMWTYAS EEAAIEDALR
LARGMTYKNA AAGLNLGGGK TVIIGDPFKD KNEEMFRALG RFIQGLNGRY ITAEDVGTTV
ADMDLIHEET NYVTGISPAF GSSGNPSPIT AYGVFLGMKA AAKEAFGDDS LAGRKVAVQG
LGNVAYTLCE YLYNEGAKLI VTDINQQAID RVVADFGAVA VAPDAIYEQD VDIFSPCALG
AIVNDQTIPT LKAKVIAGSA NNQLAESRHG KVLHDLGIVY APDYVINAGG VINVADELYG
YNRERAMKRV ETIYTSLEKI FAISKEEDIP TYLAANRLAE ERIARVAKSR SQFLQNEKNI
LNGR
//