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Database: UniProt
Entry: A0A0A5GRM8_9BACI
LinkDB: A0A0A5GRM8_9BACI
Original site: A0A0A5GRM8_9BACI 
ID   A0A0A5GRM8_9BACI        Unreviewed;       416 AA.
AC   A0A0A5GRM8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=N781_01065 {ECO:0000313|EMBL:KGX93820.1};
OS   Pontibacillus halophilus JSM 076056 = DSM 19796.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX93820.1, ECO:0000313|Proteomes:UP000030528};
RN   [1] {ECO:0000313|EMBL:KGX93820.1, ECO:0000313|Proteomes:UP000030528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX93820.1,
RC   ECO:0000313|Proteomes:UP000030528};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX93820.1}.
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DR   EMBL; AVPE01000001; KGX93820.1; -; Genomic_DNA.
DR   RefSeq; WP_026799082.1; NZ_AVPE01000001.1.
DR   AlphaFoldDB; A0A0A5GRM8; -.
DR   STRING; 1385510.GCA_000425205_00265; -.
DR   eggNOG; COG0334; Bacteria.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000030528; 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; 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:UP000030528}.
FT   DOMAIN          182..412
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         189
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         220
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            145
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   416 AA;  46189 MW;  11771511F8E60904 CRC64;
     MSQNSPYQQL QNQLEQVVEE LEITPSVFQI LKEPKHVVRI SIPLQRDDGT VETYTGYRSL
     HSDLLGPGKG GIRFHPNVNE DEVMALSVWM TMKTAILKLP FGGAKGGIQV DPNDLSKREL
     QELSRQYIRM LEHVIGPQKD IPAPDVNTNG RIMGWMLDEF TRLRGRNVPG FITGKPPVIG
     GSEGRVEATG RGVVVTILRA LEKMDMEKKG AKVAIQGFGN VGSVTAKRLN EEGLKVVAVA
     DVNGMLYDEE GIDVLELCEY VEENGSIEGF QNQELKPSDG IFETDCDIFI PAALENVITS
     ETAPKLKASI VAEAANGPTT GDGDHILKER DIFVIPDILC NSGGVMVSAF EWMQNDSHDH
     WEKDFVVQRL DKDLSEAFRE VYKISQEKNI AMRKAAYQVA VNRLSDAMYE RGWVEG
//
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