ID A0A495ADV0_9BACI Unreviewed; 426 AA.
AC A0A495ADV0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=D8M06_02450 {ECO:0000313|EMBL:RKQ37684.1};
OS Oceanobacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ37684.1, ECO:0000313|Proteomes:UP000269301};
RN [1] {ECO:0000313|EMBL:RKQ37684.1, ECO:0000313|Proteomes:UP000269301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ37684.1,
RC ECO:0000313|Proteomes:UP000269301};
RX PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT bacterium from a hypersaline lake.";
RL Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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:RKQ37684.1}.
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DR EMBL; RBZP01000001; RKQ37684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495ADV0; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000269301; 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:UP000269301}.
FT DOMAIN 195..424
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 158
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 426 AA; 47065 MW; 80B2F381BCD6E1C7 CRC64;
MVAEQAADST NTNEENMDVL ISTRAVIKTA LEKLGYPEEV YALLKDPMRM MTVRIPVRMD
DGAIKVFTGY RAQHNDAVGP TKGGIRFHPK VTEKEIKALS IWMSLKAGIV DLPYGGAKGG
IICDPREMSF RELEGLSRGY VRAISQIVGP TKDIPAPDVF TNSQIMAWMM DEYSRIDEFN
NPGFITGKPI VLGGSHGRET ATAKGVTIVL NEAAKKKGID VKGARVIVQG FGNAGSYLSK
FLHDAGAKVV GISDAYGALY DEEGLDIDYL LDRRDSFGTV TKLFNKTITN KELLERECDI
LVPAAVENQI TKENAHKIKA RIVVEAANGP TTMEGTKILS ERGILLVPDV LASAGGVTVS
YFEWVQNNQG YYWSEKEIEE KLNEIMVKSF NTIYNTSKTR RVDMRLAAYM VGVRKMAEAS
RFRGWV
//
