ID A0A0C2RQT0_9BACL Unreviewed; 414 AA.
AC A0A0C2RQT0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=KR50_31470 {ECO:0000313|EMBL:KIL44089.1};
OS Jeotgalibacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL44089.1, ECO:0000313|Proteomes:UP000031972};
RN [1] {ECO:0000313|EMBL:KIL44089.1, ECO:0000313|Proteomes:UP000031972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-57 {ECO:0000313|EMBL:KIL44089.1,
RC ECO:0000313|Proteomes:UP000031972};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Jeotgalibacillus campisalis genome sequencing.";
RL Submitted (JAN-2015) 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:KIL44089.1}.
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DR EMBL; JXRR01000020; KIL44089.1; -; Genomic_DNA.
DR RefSeq; WP_041060617.1; NZ_JXRR01000020.1.
DR AlphaFoldDB; A0A0C2RQT0; -.
DR PATRIC; fig|220754.4.peg.3161; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000031972; 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; 1.10.8.1210; -; 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; 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:UP000031972}.
FT DOMAIN 183..412
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 146
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 414 AA; 45638 MW; 656188E882939555 CRC64;
MAENLNLFTS TQGIIREALT KMGYDEPVYE LMKEPMRLLT VRMPVRMDDG STRVFTGYRA
QHNDSVGPTK GGVRFHPDVD EEEVKALSMW MTLKCGIVDL PYGGGKGGII CDPRTMSMRE
LENLSRAYVR AISQIVGPTK DIPAPDVYTN SQIMAWMMDE YSRIDEFNSP GFITGKPIVL
GGSQGREKAT AQGVTICIDQ AAKKRGLSIK GARVVVQGFG NAGSFLAKFM HDAGAKVIAI
SDAHGAIHDP EGLDIDYLLD RRDSFGTVTT LFENTLTNSE LLEIECDILV PAAVSNQITA
ENVDRINASI IVEAANGPTT IEATKRLNDR GVLLVPDVLA SAGGVTVSYF EWVQNNQGYY
WTEEEVNEKL EKKLITAFNQ VYDLSQSRKV NMRLAAYMVG VRKSAEASRF RGWV
//
