ID I3USL8_PSEPU Unreviewed; 339 AA.
AC I3USL8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:AFK68489.1};
GN ORFNames=YSA_03174 {ECO:0000313|EMBL:AFK68489.1};
OS Pseudomonas putida ND6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK68489.1, ECO:0000313|Proteomes:UP000005268};
RN [1] {ECO:0000313|EMBL:AFK68489.1, ECO:0000313|Proteomes:UP000005268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND6 {ECO:0000313|EMBL:AFK68489.1,
RC ECO:0000313|Proteomes:UP000005268};
RX PubMed=22933774; DOI=10.1128/JB.01190-12;
RA Li S., Zhao H., Li Y., Niu S., Cai B.;
RT "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT Strain ND6.";
RL J. Bacteriol. 194:5154-5155(2012).
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; CP003588; AFK68489.1; -; Genomic_DNA.
DR RefSeq; WP_003251677.1; NC_017986.1.
DR AlphaFoldDB; I3USL8; -.
DR KEGG; ppi:YSA_03174; -.
DR PATRIC; fig|231023.4.peg.1543; -.
DR HOGENOM; CLU_025763_0_0_6; -.
DR Proteomes; UP000005268; 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}.
FT DOMAIN 138..339
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 339 AA; 35885 MW; BE32FFF7E19413A5 CRC64;
MFALMQSTRT QSLHLFNDPP TGLKAVVAIH SEHLGPAMGG CRYLPYADDE SAMTDAIRLA
QGMSYKAALA GLPMGGGKAV IMRNPHVENR AALFEAFGRF IDTLHGRFII AVDSGTSTLD
MDCIAHSTPY VTSTTASGDP SPHAAMGVFA GIRATTSFRL GSDDLRGLRV AVQGLGNVGY
ALAEQLHAVG AELLVSDLDP GRVRLAMEQF DAKPVTNDAL ISTPCDIFAP CGVGPVLNGQ
SVMQLRCAAV AGAANNQLTT LQVADQLESR GILYAPDYVI NAGGLIYVAL THRGEDQGTI
TAHLARIPSR LTEVFGHAQA EKRSPARVAQ MLAERLLYG
//
