ID A0A3B7DMR8_9ACTN Unreviewed; 364 AA.
AC A0A3B7DMR8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Valine dehydrogenase {ECO:0000313|EMBL:AXT86928.1};
GN ORFNames=C6I20_13735 {ECO:0000313|EMBL:AXT86928.1};
OS Aeromicrobium sp. A1-2.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2107713 {ECO:0000313|EMBL:AXT86928.1, ECO:0000313|Proteomes:UP000257855};
RN [1] {ECO:0000313|EMBL:AXT86928.1, ECO:0000313|Proteomes:UP000257855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1-2 {ECO:0000313|EMBL:AXT86928.1,
RC ECO:0000313|Proteomes:UP000257855};
RA Liao L., Chen B.;
RT "Complete genome of Aeromicrobium sp. A1-2.";
RL Submitted (MAR-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP027482; AXT86928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7DMR8; -.
DR KEGG; aeb:C6I20_13735; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000257855; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257855}.
FT DOMAIN 149..358
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 85
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 185..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 364 AA; 38617 MW; 75C413F6A9D6857B CRC64;
MTTQHTSNAP SVFGSRHEQV VFCHDEASGL KAIIGIYSTA LGPALGGTRF YPYGSEQAAL
TDVLNLSQGM AYKNALAGLD LGGGKAVIIG DPATLKTEAL LRAYGRFVQT LGGRYYTACD
VGTFSPDMDL IARECDFVTG RTVEHGGAGD SSVLTAFGVY QGMRASAQHL WGDTSLAGKR
VGVAGVGKVG KHLVRHLVEE DAQVVVTDPY APAVAALIET YPTVTAVADT ETLIREPLDI
YAPCALGGAL NDESIEVLTA TIVCGAANNQ LAHEGIEKRL EERGITYAPD YCVNAGGVIQ
VADELEGFDF DRAKMRATTI YDTTLGVLER AKAEGVPPSI AADRMAEQRM REVGRLRSVW
LPSS
//
