ID A0A1H1BSW0_9ACTN Unreviewed; 388 AA.
AC A0A1H1BSW0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Valine dehydrogenase (NAD+) {ECO:0000313|EMBL:SDQ55035.1};
GN ORFNames=SAMN04489764_1108 {ECO:0000313|EMBL:SDQ55035.1};
OS Thermostaphylospora chromogena.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermostaphylospora.
OX NCBI_TaxID=35622 {ECO:0000313|EMBL:SDQ55035.1, ECO:0000313|Proteomes:UP000217103};
RN [1] {ECO:0000313|EMBL:SDQ55035.1, ECO:0000313|Proteomes:UP000217103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43794 {ECO:0000313|EMBL:SDQ55035.1,
RC ECO:0000313|Proteomes:UP000217103};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNKK01000002; SDQ55035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1BSW0; -.
DR STRING; 35622.SAMN04489764_1108; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000217103; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000217103}.
FT DOMAIN 174..379
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 110
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 210..215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 388 AA; 41224 MW; D5BAAF3CBB23CCE0 CRC64;
MDTLRVISAA KGQWTGPGVT TVTDVFGLSH KGTSPSSEQG THEQVVFCAD ERSGLRAIIA
IYSTALGPSL GGTRFYPYDS EQEALADVLK LSRAMAYKNA LAGLDLGGGK AVIIGDPERD
KTEPLLRAYG RFVASLGGRY ITACDVGTYS EDMDVIAREC PHVVGRTRAY GGAGDSSVLT
AFGVFQGMRA AAQHVYGSPT LRGRRVGVEG VGKVGHRLVD HLIEDGAEVV ICDVSERAVE
RVRERHPQVE VVADRDALVA ADIDVLAPCA LGGTLNDDTV ALLRAKIVCG AANNQLAHAG
VEKQLAERGI LYAPDYVVNS GGVIQVADEI GGFDMERARA KAAQIFNTTA KIFEMAEEEG
VPPAVAADRL AERRMSEVGR ISTIWLGR
//
