ID A7GN28_BACCN Unreviewed; 427 AA. AC A7GN28; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 04-NOV-2026, entry version 111. DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185}; GN OrderedLocusNames=Bcer98_1214 {ECO:0000313|EMBL:ABS21536.1}; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21536.1, ECO:0000313|Proteomes:UP000002300}; RN [1] {ECO:0000313|EMBL:ABS21536.1, ECO:0000313|Proteomes:UP000002300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98 RC {ECO:0000313|Proteomes:UP000002300}; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V., RA Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate + NAD(+) + H2O = 2-oxoglutarate + NH4(+) + NADH + CC H(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU10011}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate + NADP(+) + H2O = 2-oxoglutarate + NH4(+) + NADPH CC + H(+); 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=1.4.1.3; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU10011}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000764; ABS21536.1; -; Genomic_DNA. DR RefSeq; WP_011984289.1; NC_009674.1. DR AlphaFoldDB; A7GN28; -. DR STRING; 315749.Bcer98_1214; -. DR PaxDb; 315749-Bcer98_1214; -. DR GeneID; 33896565; -. DR KEGG; bcy:Bcer98_1214; -. DR eggNOG; COG0334; Bacteria. DR HOGENOM; CLU_025763_1_2_9; -. DR OrthoDB; 9803297at2; -. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0004352; F:L-glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-ARBA. DR GO; GO:0006538; P:L-glutamate catabolic process; IEA:TreeGrafter. DR CDD; cd01076; NAD_bind_1_Glu_DH; 1. DR FunFam; 3.40.50.10860:FF:000008; Glutamate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000212; Glutamate dehydrogenase; 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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000185-2}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000185}; KW Reference proteome {ECO:0000313|Proteomes:UP000002300}. FT DOMAIN 196..425 FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan FT dehydrogenase C-terminal" FT /evidence="ECO:0000259|SMART:SM00839" FT ACT_SITE 119 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10011" FT ACT_SITE 119 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 203 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 234 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 361 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT SITE 159 FT /note="Important for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3" SQ SEQUENCE 427 AA; 47336 MW; AE20ACE6EB387B00 CRC64; MVAEKGTQTQ TQQREQHFEL LNSTQIVINE ALEKLGYPNE VYELLKEPVR MMTVKIPVRM DDGTVKIFTG YRAQHNDAVG PTKGGIRFHP NVTENEVKAL SIWMSLKCGI VDLPYGGGKG GIVCDPREMS FRELERLSRG YVRAISQIVG PTKDIPAPDV FTNSQIMAWM MDEYSRIDEF NSPGFITGKP LVLGGSHGRE TATAKGVTIC IREAAKKRGI DIKGARVVVQ GFGNAGSFLA KFMHDAGAKV IAISDAYGAL HDPNGLDIDY LLDRRDSFGT VTKLFNNTIT NKELLELECD ILVPAAIENQ ITEKNAADIK AKIVVEAANG PTTLEATKIL TDRGILLVPD VLASAGGVTV SYFEWVQNNQ GYYWSEEEVE ERLEKVMVKS FESIYETSQV RKVNMRLAAY MVGVRKMAEA SRFRGWV //