ID A0A5M8BSG7_CLOSY Unreviewed; 450 AA. AC A0A5M8BSG7; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 08-NOV-2023, entry version 14. DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185}; GN ORFNames=F2P57_03865 {ECO:0000313|EMBL:KAA6138967.1}; OS Clostridium symbiosum (Bacteroides symbiosus). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae. OX NCBI_TaxID=1512 {ECO:0000313|EMBL:KAA6138967.1, ECO:0000313|Proteomes:UP000325100}; RN [1] {ECO:0000313|EMBL:KAA6138967.1, ECO:0000313|Proteomes:UP000325100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT0011 {ECO:0000313|EMBL:KAA6138967.1, RC ECO:0000313|Proteomes:UP000325100}; RA Hanson B.T., Loy A.; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA6138967.1}. 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; VWSY01000001; KAA6138967.1; -; Genomic_DNA. DR RefSeq; WP_003497202.1; NZ_VWSY01000001.1. DR AlphaFoldDB; A0A5M8BSG7; -. DR SMR; A0A5M8BSG7; -. DR GeneID; 57967689; -. DR Proteomes; UP000325100; Unassembled WGS sequence. DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR CDD; cd05313; NAD_bind_2_Glu_DH; 1. DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2. 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; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1. DR PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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|PIRNR:PIRNR000185, KW ECO:0000256|RuleBase:RU004417}. FT DOMAIN 203..447 FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan FT dehydrogenase C-terminal" FT /evidence="ECO:0000259|SMART:SM00839" FT ACT_SITE 126 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1" FT BINDING 90 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 210 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 241 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 381 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT SITE 166 FT /note="Important for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3" SQ SEQUENCE 450 AA; 49310 MW; 4FE0DBA5E4F8BDD7 CRC64; MSKYVDRVIA EVEKKYADEP EFVQTVEEVL SSLGPVVDAH PEYEEVALLE RMVIPERVIE FRVPWEDDNG KVHVNTGYRV QFNGAIGPYK GGLRFAPSVN LSIMKFLGFE QAFKDSLTTL PMGGAKGGSD FDPNGKSDRE VMRFCQAFMT ELYRHIGPDI DVPAGDLGVG AREIGYMYGQ YRKIVGGFYN GVLTGKARSF GGSLVRPEAT GYGSVYYVEA VMKHENDTLV GKTVALAGFG NVAWGAAKKL AELGAKAVTL SGPDGYIYDP EGITTEEKIN YMLEMRASGR NKVQDYADKF GVQFFPGEKP WGQKVDIIMP CATQNDVDLE QAKKIVANNI KYYIEVANMP TTNEALRFLM QQPNMVVAPS KAVNAGGVLV SGFEMSQNSE RLSWTAEEVD SKLHQVMTDI HDGSAAAAER YGLGYNLVAG ANIVGFQKIA DAMMAQGIAW //