ID A0A0Q9KI14_9BACL Unreviewed; 459 AA.
AC A0A0Q9KI14;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=ASG81_16685 {ECO:0000313|EMBL:KRE41185.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE41185.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE41185.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE41185.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE41185.1}.
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DR EMBL; LMRV01000050; KRE41185.1; -; Genomic_DNA.
DR RefSeq; WP_056636471.1; NZ_LMRV01000050.1.
DR AlphaFoldDB; A0A0Q9KI14; -.
DR STRING; 1736388.ASG81_16685; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000051180; 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}.
FT DOMAIN 226..456
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 252
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 156
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 459 AA; 50219 MW; 41A58980B336ACEA CRC64;
MASQTGAIVQ QSLNALMGDP AFLPNLQNQS REQAFLSLAA ILSTPNKVHK AFLRITVDNG
NVVRIPAYRI QHNDTLGPYK GGIRFHESVS EDEVTNLAAL MTLKNALHEV PFGGGKGGVV
INPRSYSTKE LYLICKKYVQ YFSDVLGPDK DIPAPDMGTG EREMDWMMAE YKSIHPGQPY
LGSFTGKSVI NGGSLGRREA TGKGVYFTFR YMLHDFLKAQ SSRLAGSTNP FVQTALAHAG
KPLSIAVQGF GNVGSVAAME AYKCTYLQNK VVAVSDRNVT LYNPDGLSVP SLLEYAAQHQ
GDLPSDEAAL SALGLKAQIL GREDVLYLDV DVLILAALEE QIRQDNAGRV IARIIVEGAN
APVTGGADEA LTAKGTIIIP DILANAGGVI VSYFEWLQGR ETQFFSEEQV YKMLYDKMQK
TLISILPAFF ENPFPLRHNC YNHAVMKLST VLYRQGKLY
//
