ID K6DS76_9BACI Unreviewed; 431 AA.
AC K6DS76;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=BABA_02897 {ECO:0000313|EMBL:EKN71088.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN71088.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN71088.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN71088.1}.
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DR EMBL; AJLS01000034; EKN71088.1; -; Genomic_DNA.
DR RefSeq; WP_007083619.1; NZ_AJLS01000034.1.
DR AlphaFoldDB; K6DS76; -.
DR STRING; 1117379.BABA_02897; -.
DR PATRIC; fig|1117379.3.peg.591; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000006316; 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:UP000006316}.
FT DOMAIN 200..429
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 163
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 431 AA; 47509 MW; 73CE13108CC1D95C CRC64;
MTVNTAELNN LEKDQQKEEE SLNLFYSTQT VIQKALKKLG YTNEMYELLK DPIRLLTVRI
PVRMDDGSVK VFTGYRSQHN DAVGPTKGGV RFHPEVNEEE VKALSIWMTL KCGITDLPYG
GGKGGIICDP RKMSFRELER LSRGYVRAIS QIVGPSKDIP APDVYTNSQI MAWMMDEYSR
LREFDSPGFI TGKPIVLGGS QGRETATAAG VTICIEEAVK KKGMELKGAR VVIQGFGNAG
SFLAKFLHDA GAKVVAVSDV YGGVYDPNGL DIDYLLDRRD SFGTFSQLFK DTITNQELLE
LECDILVPAA ISNQITAKNA ANIKASIVVE AANGPTTLEA TSILTERGVL LVPDILASAG
GVTVSYFEWV QNNQGYYWSE EEVHQKLAKV MIDSFENIYK TAAAHEVDMR LAAYMTGIKK
AAEASRFRGW V
//
