ID A0A1H2XUI1_9BACL Unreviewed; 427 AA.
AC A0A1H2XUI1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN04489725_12430 {ECO:0000313|EMBL:SDW96491.1};
OS Alicyclobacillus hesperidum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=89784 {ECO:0000313|EMBL:SDW96491.1, ECO:0000313|Proteomes:UP000182589};
RN [1] {ECO:0000313|Proteomes:UP000182589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12489 {ECO:0000313|Proteomes:UP000182589};
RA Varghese 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; FNOJ01000024; SDW96491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2XUI1; -.
DR STRING; 89784.SAMN04489725_12430; -.
DR Proteomes; UP000182589; Unassembled WGS sequence.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000182589}.
FT DOMAIN 195..424
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 158
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 427 AA; 47311 MW; 32FCEF0030508CEE CRC64;
MTQSESASFE DKRTDGTYIL EDTQSIIEQA LQVLGYGREV YDLLKLPLRV LTVRFPVKMD
DGTVKVFTGY RAQHNDSVGP TKGGIRLHPD LSQAEIEASA IWMSIRCGIA DLPFGGGKGG
IVCDPRDMSF AEIERVSRAY VRAISQIVGP AKDIPAPDVF SNSQNIAWMF DEYSHLRESD
SPGFITGKPV ILGGTRGRDG AAARGVAITI EESAKHRDIR LEGARVIVQG FGGIGSYIAK
YLHDRGAKVV GVADAYGALY REDGLDVDEL LERRDSFGTV TRLYRNVLSN KELLEMPCDV
LIPAATGSQI TEENASRIQA SIIVEATNAP TTHDALDILT EREILVVPDV VSFSGDVIVS
YFEWVQNNQG YYWEEPEVHS RLDSRVRTSF HRVYQTAVKY QVNMRVAAYI VGVQRLAEAS
RWRGWIS
//
