ID A0A1G8R675_9BACI Unreviewed; 461 AA.
AC A0A1G8R675;
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|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN04488123_11562 {ECO:0000313|EMBL:SDJ11890.1};
OS Natribacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Natribacillus.
OX NCBI_TaxID=549003 {ECO:0000313|EMBL:SDJ11890.1, ECO:0000313|Proteomes:UP000198853};
RN [1] {ECO:0000313|EMBL:SDJ11890.1, ECO:0000313|Proteomes:UP000198853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21771 {ECO:0000313|EMBL:SDJ11890.1,
RC ECO:0000313|Proteomes:UP000198853};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNEN01000015; SDJ11890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8R675; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000198853; 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 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 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:UP000198853}.
FT DOMAIN 235..458
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 156
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 461 AA; 51407 MW; F861A20774AFD061 CRC64;
MSRDDTRRFI QDVVNQLKKE SFSAEFQKNE NGGVFDSAAE ILKTTDKIIK SYIRVARDDG
SISRIPAYRV QHNNISGFYK GGIRFSDAVN EEEVENLAIL MTIKNALHEL PFGGAKGGVY
VDPKKFSQKE LNMVSKKYVQ RLKPDLGPTN DIPAPDLGTN ETIIDWMVGE YKTITPGESY
INSFTGKSDV NGGVTGRREA TGIGTFLTYY HLISRWFQEA EAEKVTRKKS WQNIEALRTG
EQPIKVAVQG FGNVGSIAAE EAIHCDYEHM VVAVSDKYVS LGNEEGLDIE KLITYHDVHG
QLPESQEGLA EAGVEAVIAE DPAAVLTSEC DVLILAAVED QITEDNMKDI SAKILVEGAN
APITMGADKY FEENGVMVIP DILANAGGVH VSYLEWIQTN MPKPFTKEEV ISEMSEKMKH
ISSRVYDHYF YAETHDTARV LCYKLALKRL ITLLYKHGKL Y
//