ID A0A286CWG3_9GAMM Unreviewed; 366 AA.
AC A0A286CWG3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:SOD50704.1};
GN ORFNames=SAMN06296416_101291 {ECO:0000313|EMBL:SOD50704.1};
OS Pseudoxanthomonas wuyuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1073196 {ECO:0000313|EMBL:SOD50704.1, ECO:0000313|Proteomes:UP000219374};
RN [1] {ECO:0000313|EMBL:SOD50704.1, ECO:0000313|Proteomes:UP000219374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10978 {ECO:0000313|EMBL:SOD50704.1,
RC ECO:0000313|Proteomes:UP000219374};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OCND01000001; SOD50704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286CWG3; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000219374; Unassembled WGS sequence.
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|ARBA:ARBA00023027, 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:UP000219374}.
FT DOMAIN 143..349
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 79
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 179..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 366 AA; 39814 MW; 4E69A8F4824CDE84 CRC64;
MIFETLDTSG HEQVVFCHNP DAGLKAIIAI HSTVLGPALG GVRMRQYADS NLALTDALRL
SRTMTYKNAL AGLSVGGGKA VIIGDCDQDK SEVLFRSFGR YVDSLGGRYI TAEDVGTDVN
DMENVYRETE YVVGVHQVHG GSGDPAPFTA YGALQGLMAT LNRKFGHEEV GKTSIAVQGL
GHIGMEFVKL LKERGAKLFV TDLNPRLVAH AVEEFGAEAV KPDEIYDLPV DVFAPCALEY
AINAETLPRL KARIICGTAN NQMSHVTGDE AAKRGILYAP DYAVNAGGVM NVSLEIDGYN
RERAMRMMRT IYHTVGKIFE LADRENITPQ YAADRMAEAR IGSIGKLKLP LGRTAPRFMG
HLRGEH
//