ID A0A0J1FEG5_9FIRM Unreviewed; 364 AA.
AC A0A0J1FEG5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:KLU61810.1};
DE EC=1.4.1.9 {ECO:0000313|EMBL:KLU61810.1};
GN Name=ldh_1 {ECO:0000313|EMBL:KLU61810.1};
GN ORFNames=CEB3_c17280 {ECO:0000313|EMBL:KLU61810.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU61810.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU61810.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU61810.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU61810.1}.
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DR EMBL; LDXJ01000051; KLU61810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FEG5; -.
DR STRING; 999898.CEB3_c17280; -.
DR PATRIC; fig|999898.3.peg.1955; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000035957; Unassembled WGS sequence.
DR GO; GO:0050049; F:leucine dehydrogenase activity; IEA:UniProtKB-EC.
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; 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; 1.
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.
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:UP000035957}.
FT DOMAIN 154..360
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 364 AA; 39526 MW; 657E7EEF43DA65B1 CRC64;
MSDKETAFKS IFDQMAEYGH EQVIFNYDKA TGLKAIIAIH DTTLGPALGG CRMWNYETEQ
DALTDALRLS RGMTYKCAVS GAIHGGGKTV IIGDPKTEKS DELFQALGTF VETLKGRYYT
GTDVGTVGMD FVSAGKQTKY VVGVPEEYGG SGNSAIITAF GVYRGMKATA LEAFGSDSLS
GLTIAVQGLG KVGYDLVGRL YQDGAKLIVT DIEENNVRRA KEEYPGITTV KPDEIFGVEC
DIFSPNALGA IINDETIPQF KCKAICGAAN NQLKEPRHGD LLKEKGILYA PDYVANAGGL
IQVADELQGY NKERAFKNAS LIYDILLRIF AVAKKENIST AQAADVMLDR KIETTGRVQR
KYTR
//
