ID A0A2C1YTA7_9BACI Unreviewed; 379 AA.
AC A0A2C1YTA7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:PGV48309.1};
GN ORFNames=COD92_27120 {ECO:0000313|EMBL:PGV48309.1};
OS Bacillus sp. AFS037270.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV48309.1, ECO:0000313|Proteomes:UP000225442};
RN [1] {ECO:0000313|EMBL:PGV48309.1, ECO:0000313|Proteomes:UP000225442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS037270 {ECO:0000313|EMBL:PGV48309.1,
RC ECO:0000313|Proteomes:UP000225442};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PGV48309.1}.
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DR EMBL; NUNF01000073; PGV48309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1YTA7; -.
DR Proteomes; UP000225442; Unassembled WGS sequence.
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; 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.
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}.
FT DOMAIN 156..365
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 189..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 379 AA; 41249 MW; 3D0E7E0F3CF8B1A4 CRC64;
MNVLEHSVQT TESVIEKMHE HEQIVFCNDP TTGLKAIIAI HNTTLGPALG GCRMRPYRTM
DEALEDVLRL SKGMTYKCAA ADVDFGGGKA VIFGDPATDK TPAMFRALGQ FVDSLNGRFY
TGTDMGTSMD DFIHASKETN CIVGIPEAYG GGGDSSIPTA IGVIYGLKAT NKVVFGTDDL
SGKTFTIQGL GKVGYKVAEQ LLESGADLYV SDINEEAVKA IQEHAKQLGS IARAVSGNDV
YAAEADVFVP CAFGGIINDE TIDLLKVKAV AGSANNQLLT EKHGEVLKQK GILYAPDYIV
NAGGLIQVAD ELYGYNKERV LSKTRSIYTS LLEVYRQAEL DDITTIQAAN RLCEKRIEDR
KKQNSFFTHT KRPKWDIRN
//
