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Database: UniProt
Entry: A0A286CWG3_9GAMM
LinkDB: A0A286CWG3_9GAMM
Original site: A0A286CWG3_9GAMM 
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
//
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