ID A0A098EPL2_9BACL Unreviewed; 460 AA.
AC A0A098EPL2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-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 Name=gdhA_1 {ECO:0000313|EMBL:CEG23722.1};
GN ORFNames=BN1080_02726 {ECO:0000313|EMBL:CEG23722.1};
OS Planococcus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG23722.1, ECO:0000313|Proteomes:UP000043699};
RN [1] {ECO:0000313|EMBL:CEG23722.1, ECO:0000313|Proteomes:UP000043699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES2 {ECO:0000313|EMBL:CEG23722.1,
RC ECO:0000313|Proteomes:UP000043699};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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; CCXS01000001; CEG23722.1; -; Genomic_DNA.
DR RefSeq; WP_052652639.1; NZ_LR698965.1.
DR AlphaFoldDB; A0A098EPL2; -.
DR STRING; 1499687.BN1080_02726; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000043699; 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; 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; 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.
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:UP000043699}.
FT DOMAIN 217..458
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 104
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 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 180
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 460 AA; 50768 MW; EFED483903387370 CRC64;
MKAVNESIQT KEPSAHEYIK AVHKKVRDRN PGEPEFLQAA WEVFSSLQPV FEQHPEYVEE
GILERISEPE RFIAFRVTWE DDAGNVHVNR GYRVQFNSTL GPFKGGLRFH PTLTGSVVKF
LGFEQIFKNA LTGLPIGGGK GGADFDPKGR SDREIMRFCQ SFMTELSRHI GPDIDVPAGD
IGVGKREIGY LFGQYKRIRN AFEAGVFTGK NPDNGGSLIR KEATGYGTVY FVEEMLKGEG
LSFEGSRVIV SGSGNVSIYA MEKAIEFGAT VVACSDSEGY IYDPEGIDVN TVKRLKEVER
KRIYHYLEHH PKARFGKDKS DIWKIPCDIA LPCATQNEIG REGAEALVDN GVKAIGEGAN
MPCDEEAVRI LTNNHVLFAP AKAANAGGVA VSAMEMSQNS MRYSWTSEEV DEKLHQVMKN
IYRNCIETAE KYGAPGNLIA GANIAGFKKV ADAMLEHGLN
//
