ID A0A0U2UHG2_9BACL Unreviewed; 424 AA.
AC A0A0U2UHG2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=IJ21_02290 {ECO:0000313|EMBL:ALS25673.1};
OS Paenibacillus sp. 32O-W.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS25673.1, ECO:0000313|Proteomes:UP000059673};
RN [1] {ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS25673.1, ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|EMBL:ALS25673.1,
RC ECO:0000313|Proteomes:UP000059673};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013653; ALS25673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2UHG2; -.
DR STRING; 1695218.IJ21_02290; -.
DR KEGG; pow:IJ21_02290; -.
DR PATRIC; fig|1695218.3.peg.232; -.
DR Proteomes; UP000059673; Chromosome.
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:UP000059673}.
FT DOMAIN 192..422
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 155
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 424 AA; 45873 MW; 07EB65C484911877 CRC64;
MALSVANQAT TENLNPYEIA QRQIEEAASH LQLPAHVVEF LKKPKRVLSV NFPVKMDDGT
VRVFEGFRSQ HNDALGPNKG GIRFHPDVTM DEVKALSMWM SFKCGVVGLP YGGGKGGVIC
DPRKLSKGEL ERVSRGFMEA IAEIVGPEKD IPAPDVYTTP EIMGWMMDTY SRLRGAFTPG
VITGKPLIVG GSKGRNEATA RGCVFTIEEA MRQLGKPMQG ATVAIQGYGN AGRIAAKLLS
EQGCTIVAVS DSGGAIYLPE GLPVDEIGRL KDEKGSVRYY EAANAITNEE LLELEVDILI
PAALENVITA ANASRIKAKI VAEAANGPTT PEADKVLFEK GIVVIPDILA NAGGVTVSYF
EWVQNLANFY WSEEEVNSKL KVKMTESYGV VSELASKHNV PLRTAAYMVS IQRIAEAMKA
RGWV
//
