ID D6YQU5_PANVC Unreviewed; 424 AA.
AC D6YQU5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA {ECO:0000313|EMBL:ADI78378.1};
GN OrderedLocusNames=Pvag_pPag30309 {ECO:0000313|EMBL:ADI78378.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OG Plasmid pPag3 {ECO:0000313|EMBL:ADI78378.1,
OG ECO:0000313|Proteomes:UP000006631}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADI78378.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADI78378.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADI78378.1,
RC ECO:0000313|Proteomes:UP000006631};
RC PLASMID=pPag3 {ECO:0000313|EMBL:ADI78378.1};
RX PubMed=20487014; DOI=10.1111/j.1574-6968.2010.01994.x;
RA Smits T.H., Rezzonico F., Pelludat C., Goesmann A., Frey J.E., Duffy B.;
RT "Genomic and phenotypic characterization of a nonpigmented variant of
RT Pantoea vagans biocontrol strain C9-1 lacking the 530-kb megaplasmid
RT pPag3.";
RL FEMS Microbiol. Lett. 308:48-54(2010).
RN [2] {ECO:0000313|EMBL:ADI78378.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADI78378.1,
RC ECO:0000313|Proteomes:UP000006631};
RC PLASMID=pPag3 {ECO:0000313|EMBL:ADI78378.1};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001463};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; CP001895; ADI78378.1; -; Genomic_DNA.
DR RefSeq; WP_013196280.1; NC_014258.1.
DR AlphaFoldDB; D6YQU5; -.
DR KEGG; pva:Pvag_pPag30309; -.
DR HOGENOM; CLU_025763_1_2_6; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000006631; Plasmid pPag3.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR Gene3D; 1.10.8.1210; -; 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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000185; Glu_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:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185}; Plasmid {ECO:0000313|EMBL:ADI78378.1}.
FT DOMAIN 190..420
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 153
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 424 AA; 46633 MW; E97C851991E855E0 CRC64;
MDKLSYASES STSAWSTYLQ QIDRVAPYLG DLSRWIDTLR HPKRALIVDI PLQMDDGSIR
HFEGYRVQHN LSRGPGKGGI RYHPAVDLNE VMALSAWMTI KCAAVNLPYG GAKGGIRVDP
FKLSEGELER LTRRYTSEIG IIIGPQKDIP APDVGTNSKV MAWMMDTYSM NHGTTITGVV
TGKPIHLGGS LGREKATGRG VFITGREVAR RSGIEIEGAR VAVQGFGNVG SEAARLFDEA
GARVVVIQDH TATIYNSDGL DMAALSEWQI AHKQIAGFPG AQSIDKEAFW TTEMDILIPA
ALEGQITRER AEMLSCKIVL EGANGPTYPD ADDMLATRGI IVVPDVVCNA GGVTVSYFEW
VQDMASFFWS EDEINRRSDK IMTEAMVHIW EKSKEKDCSL RTAAYIVACE RILMARKDRG
IYPG
//
