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Database: UniProt
Entry: F2F941_SOLSS
LinkDB: F2F941_SOLSS
Original site: F2F941_SOLSS 
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
//
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