ID E0E269_9FIRM Unreviewed; 417 AA.
AC E0E269;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN Name=gluD {ECO:0000313|EMBL:EFM65016.1};
GN ORFNames=HMPREF0634_1400 {ECO:0000313|EMBL:EFM65016.1};
OS Peptostreptococcus stomatis DSM 17678.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM65016.1, ECO:0000313|Proteomes:UP000003244};
RN [1] {ECO:0000313|EMBL:EFM65016.1, ECO:0000313|Proteomes:UP000003244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM65016.1,
RC ECO:0000313|Proteomes:UP000003244};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFM65016.1}.
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DR EMBL; ADGQ01000032; EFM65016.1; -; Genomic_DNA.
DR RefSeq; WP_007788874.1; NZ_ADGQ01000032.1.
DR AlphaFoldDB; E0E269; -.
DR STRING; 596315.HMPREF0634_1400; -.
DR GeneID; 84800316; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000003244; 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; cd01076; NAD_bind_1_Glu_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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003244}.
FT DOMAIN 180..415
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 143
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 417 AA; 45617 MW; C7768D3FA05BA052 CRC64;
MANVFEMAQA QVKNACDKLG MEPQVYELLK EPRRVIEVNI PVKMDDGSIK VFKGYRSQHC
DAVGPTKGGI RFHPNVSLEE VKALSIWMTF KCSVTGIPYG GGKGGIIVDP SELSEGELER
LSRGYIDGIY KLIGEKVDVP APDVNTNGKI MSWMVDEYNK LVGVSSIGVL TGKPVEFGGS
LGRNEATGYG VAVTVRESAK KMGIDMTHAK IAVQGFGNVG AFTVKNIQKL GGTVVAVAEW
AKEVGPYAIY KEDGLDFQAM WDYRAEKGNL VDFPGSKMIS MDEFWSAQVD VVVPAALENS
IDAAVAEKIQ AKLVCEAANG PTTPEGDEVL NRKGIILTPD ILTNAGGVTV SYFEWVQNLY
GYYWSEAEVE AKEDEAMVKA FEALWAIKEE YGVTMRESAY MHSVKRVATA MKLRGWY
//
