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Database: UniProt
Entry: A0A0B0IHR4_9BACI
LinkDB: A0A0B0IHR4_9BACI
Original site: A0A0B0IHR4_9BACI 
ID   A0A0B0IHR4_9BACI        Unreviewed;       420 AA.
AC   A0A0B0IHR4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-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=LQ50_10265 {ECO:0000313|EMBL:KHF40367.1};
OS   Halalkalibacter okhensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF40367.1, ECO:0000313|Proteomes:UP000030832};
RN   [1] {ECO:0000313|EMBL:KHF40367.1, ECO:0000313|Proteomes:UP000030832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA   Prakash J.S.;
RT   "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL   Submitted (SEP-2014) 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:KHF40367.1}.
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DR   EMBL; JRJU01000010; KHF40367.1; -; Genomic_DNA.
DR   RefSeq; WP_034628571.1; NZ_JRJU01000010.1.
DR   AlphaFoldDB; A0A0B0IHR4; -.
DR   STRING; 333138.LQ50_10265; -.
DR   eggNOG; COG0334; Bacteria.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000030832; 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:UP000030832}.
FT   DOMAIN          189..418
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            152
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   420 AA;  46269 MW;  88A4D88D376C9174 CRC64;
     MTENKKQAEQ LDVLASTQSV IKKALDKLGY PEEMYELMKE PIRMLTVRIP VRMDDGSTKI
     FTGFRAQHND SVGPTKGGVR FHPSVTEKEV KALSIWMSLK AGIVDLPYGG GKGGIICDPR
     EMSFRELERI SRGYVRAISQ IVGPTKDIPA PDVFTNSQIM AWMLDEYSRI REFDSPGFIT
     GKPLVLGGSH GRESATAKGV TICIREAAKK KGIELEGARV VIQGFGNAGS FLAKFMHDAG
     ALVVGISDAY GGLYDADGLD IDYLLDRRDS FGTVTKLFKD TISNQELLEL DCDILVPAAI
     ENQITEANAD RIKAAIVVEA ANGPTTMEAT RILSERDVLL VPDVLASAGG VTVSYFEWVQ
     NNQGYYWTEE EVEGKLEAVM VGSFNNIYNL ARTRKVDMRL AAYMIGVRKM AEASRFRGWV
//
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