ID A0A286IMC1_9BACT Unreviewed; 424 AA.
AC A0A286IMC1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN06298216_2204 {ECO:0000313|EMBL:SOE21748.1};
OS Spirosomataceae bacterium TFI 002.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE21748.1, ECO:0000313|Proteomes:UP000217493};
RN [1] {ECO:0000313|EMBL:SOE21748.1, ECO:0000313|Proteomes:UP000217493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFI 002 {ECO:0000313|EMBL:SOE21748.1,
RC ECO:0000313|Proteomes:UP000217493};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; LT907983; SOE21748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286IMC1; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000217493; Chromosome i.
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; 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:UP000217493}.
FT DOMAIN 191..422
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 154
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 424 AA; 46130 MW; 8338F0AD990AE444 CRC64;
MKYIEPAPIK DKENPLESMM SRFDEAVKLL GISDEMYHIL KTPARQVIVG LPVTMDDGSV
KVFEGYRVLH SNILGPGKGG IRFDPDVTLD EVRALAAWMT WKCAVVDIPY GGAKGGIACN
PREMSAGEME RLTRAYTRQM LDIFGPDKDI PAPDMGTGPR EMAWLMDEYS KAKGMTTHAV
VTGKPLVLGG SLGRTEATGR GVMVSTLSAM DKMKINPYKA TAAIQGFGNV GSFAGKLLAE
KGVKILAVSD ISGTYYNENG LDIAAAMAYR DANKGILEGF KEAELLKGED ILFLDVDALI
PAAKEDVITK ENAHLIKAKL IVEGANGPTS AKADVILNNN GVLAVPDILA NAGGVTVSYF
EWVQNRIGYK WGEDRINRRC ERSMKNAFNT VYKLSKKHDV SMRIAAYMVA IDKVAATYKF
RGGF
//
