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Database: UniProt
Entry: A0A1I0VCR1_9BACI
LinkDB: A0A1I0VCR1_9BACI
Original site: A0A1I0VCR1_9BACI 
ID   A0A1I0VCR1_9BACI        Unreviewed;       426 AA.
AC   A0A1I0VCR1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=SAMN04488072_101294 {ECO:0000313|EMBL:SFA73376.1};
OS   Lentibacillus halodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=237679 {ECO:0000313|EMBL:SFA73376.1, ECO:0000313|Proteomes:UP000198642};
RN   [1] {ECO:0000313|EMBL:SFA73376.1, ECO:0000313|Proteomes:UP000198642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFA73376.1,
RC   ECO:0000313|Proteomes:UP000198642};
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; FOJW01000001; SFA73376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0VCR1; -.
DR   STRING; 237679.SAMN04488072_101294; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000198642; 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:UP000198642}.
FT   DOMAIN          195..424
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  46640 MW;  01FE1A2CEE5B6736 CRC64;
     MVADNAADST KEKSESTDVL TSTRTVVKTA LEKLGYPDEV FELLKDPMRM MTVRIPVRMD
     DGSIKIFTGY RAQHNDAVGP TKGGVRFHPN VTEKEVKALS IWMSLKAGIV DLPYGGGKGG
     IICDPREMSF RELEGLSRGY VRAISQIVGP NKDIPAPDVF TNSQIMAWMM DEYSRIDEFN
     NPGFITGKPI VLGGSHGRES ATAKGVTICI NEAAKKKGID VKGARVVVQG FGNAGSFLAK
     FLHDAGAKIV GISDAYGALH EPDGLDIDYL LDRRDSFGTV TKLFNNTIAN QDLLELDCDI
     LVPAAVENQI TKQNAHDIKA SIVVEAANGP TTLEATKILS ERGILLVPDV LASSGGVTVS
     YFEWVQNNQG FYWTAEEIDE KLHEIIIKSF NNIYNTAETR RIDMRLAAYM AGVRKMAEAA
     RFRGWV
//
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