ID   A0A0U1KN37_9BACI        Unreviewed;       457 AA.
AC   A0A0U1KN37;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN   Name=gdhA {ECO:0000313|EMBL:CQR47398.1};
GN   ORFNames=BN1058_01710 {ECO:0000313|EMBL:CQR47398.1};
OS   Paraliobacillus sp. PM-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX   NCBI_TaxID=1462524 {ECO:0000313|EMBL:CQR47398.1, ECO:0000313|Proteomes:UP000199066};
RN   [1] {ECO:0000313|EMBL:CQR47398.1, ECO:0000313|Proteomes:UP000199066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM-2 {ECO:0000313|EMBL:CQR47398.1,
RC   ECO:0000313|Proteomes:UP000199066};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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; CTEI01000001; CQR47398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1KN37; -.
DR   STRING; 1462524.BN1058_01710; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000199066; 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; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 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; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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.
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:UP000199066}.
FT   DOMAIN          214..455
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         176
FT                   /ligand="substrate"
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         252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            177
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   457 AA;  49333 MW;  F34A338DA3CF0819 CRC64;
     MTQVDNQQLQ VAKDYVEKLF DKVVEKNPGE EEFHQAVKEV LDSLVPAIAQ NPAYMKEAVL
     DRMVEPERLL TFRVPWVDDE GNVQVNRGFR VQFNSAIGPY KGGLRFHPSV NASIIKFLGF
     EQMFKNSLTG QPIGAGKGGS DFDPKGKSDL EIMRFCQSFM TELSRYIGPD TDVPAGDIGV
     GAREIGYMFG QYKKLRGAYE AGVLTGKAIG YGGSLGRKEA TGYGTVYFVD EMLKDKGLSF
     NGSTVVVSGS GNVSIYAMEK AMELGAKVVA CSDSSGYIYD PNGIQLDTVK QLKEVESKRI
     YEYVDTHPEA TFVDDFSKIW TIPCDIALPC ATQNELNKEA ADTLISNGVK AIGEGANMPS
     TYDAVNAFIE NNVLFGPAKA ANAGGVAVSA LEMAQNSARL AWTAEEVDGK LQEIMKDIYQ
     ASVKASEQNG ATGNLVVGAN IAGFTKVADA MIAQGVI
//