ID W1TM44_9ACTO Unreviewed; 418 AA.
AC W1TM44;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=Q618_VCMC00001G0288 {ECO:0000313|EMBL:ETI82707.1};
OS Varibaculum cambriense DORA_20.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Varibaculum.
OX NCBI_TaxID=1403948 {ECO:0000313|EMBL:ETI82707.1, ECO:0000313|Proteomes:UP000018843};
RN [1] {ECO:0000313|EMBL:ETI82707.1, ECO:0000313|Proteomes:UP000018843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_20 {ECO:0000313|Proteomes:UP000018843};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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:ETI82707.1}.
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DR EMBL; AZMI01000001; ETI82707.1; -; Genomic_DNA.
DR AlphaFoldDB; W1TM44; -.
DR STRING; 184870.HMPREF1862_00239; -.
DR PATRIC; fig|1403948.3.peg.718; -.
DR eggNOG; COG0334; Bacteria.
DR Proteomes; UP000018843; Unassembled WGS sequence.
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:UP000018843}.
FT DOMAIN 185..415
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 192
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 148
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 418 AA; 45550 MW; BF60371CA0052B7D CRC64;
MSEDYKPNPY EDAKNQLREA QKILGFSEGD YEMLASPRRE MSVSIPIRRD DGTHEVLHGY
RVQHNLTRGP AKGGIRYNEH VDIDEVRALS MWMTWKCALV NLPYGGAKGG VTIDPSKYSQ
AELERVTRRY ISEILPIIGP EKDVPAPDVG TNEQTMAWIM DTYSQFQGYT VPGICTGKPV
SLGGSLGRAE ATSLGVVIMV EAALKKKGIK FADASLAIQG FGKVGRGAAE IAQRRGGKVV
AISDIFGAIY NADGIDTKAL GEYVDEKGKV VGFPGAEPMD ASQLLLLDVD VVVPAAIEGV
LTKDNAPDVK AKIIVEGANG PTDSAADKIL NEKGVMVVPD ILANSGGVIV SYYEWVQGRD
NFFWPLERVQ KEEEQRITAA WKDVEAYAEE KGVTLRVAAT VLAVERVLQA HKRRGLYP
//
