ID A0A1H1VEB2_9PSED Unreviewed; 340 AA.
AC A0A1H1VEB2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:SDS83114.1};
GN ORFNames=SAMN05216221_2746 {ECO:0000313|EMBL:SDS83114.1};
OS Pseudomonas oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1392877 {ECO:0000313|EMBL:SDS83114.1, ECO:0000313|Proteomes:UP000243359};
RN [1] {ECO:0000313|Proteomes:UP000243359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32247 {ECO:0000313|Proteomes:UP000243359};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
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; LT629751; SDS83114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1VEB2; -.
DR STRING; 1392877.SAMN05216221_2746; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000243359; Chromosome i.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
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:UP000243359}.
FT DOMAIN 138..340
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 78
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 174..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 340 AA; 35340 MW; 5D1EAD07D8CE1779 CRC64;
MFATLEAVRV EELHLACDPQ TGLHAIVAIH NTNLGPALGG CRYLPYPDEE SAVRDAARLA
RGMSYKAALA GLALGGGKAV IIRPPHLTSR AALFEAFGRF IDKLGGRYIT AVDSGTSGAD
MDCIAQYTRH VTSTTAGGDP SPHTALGVFA GIRATARARL GSDSLDGLCV AVQGLGHVGF
ALAEHLAVAG ARLIVSDIDE GRLELAVEQL GAQPVAADAL LTVPCDILAP CGLGGVINPQ
SIGKLRCAAI AGAANNQLDS PEMGDELAAR GILYAPDYVI NSGGLIFVAL QHQGHSHAEI
TAHLAKIGHR LEEIYTEAHA EQRSPARVAD SLAERLIYGS
//
