ID A0A0Q9N347_9MICC Unreviewed; 390 AA.
AC A0A0Q9N347;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=ASG92_02040 {ECO:0000313|EMBL:KRE68658.1};
OS Arthrobacter sp. Soil736.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE68658.1, ECO:0000313|Proteomes:UP000051775};
RN [1] {ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE68658.1, ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE68658.1,
RC ECO:0000313|Proteomes:UP000051775};
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:KRE68658.1}.
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DR EMBL; LMSB01000001; KRE68658.1; -; Genomic_DNA.
DR RefSeq; WP_056623645.1; NZ_LMSB01000001.1.
DR AlphaFoldDB; A0A0Q9N347; -.
DR STRING; 1736395.ASG92_02040; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000051775; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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 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 144..376
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 78
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 114
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 390 AA; 40817 MW; 0889FB3F050157CB CRC64;
MTDGVFGLID EWGPEKIVVV SDRKTGMRGV LVLDNTARGT GKGGTRMSPS LTVQEVARLA
RTMTWKWAAV DLFHGGAKAG ILGDPNDPNK EAILRAFARA LSNEVPSEYV FGLDMGLAEE
DAAIFLDELG DRGASTGLPR ALGGLPYDQL GVTGYGVAEA AEAAAENRNI ALKGSRVSIQ
GFGAVGQAAA VRLVELGATV VAVSTAAGAV HDPNGLDVAR LVNLRAEAGD ACVRHYGSVL
PADTALTADA DILIPAARED TVNDVIAAST NVKLVIEGAN LPTSPNSRRI LHERGIAVVP
DFIANAGGIV AAAHSMAARY SPFVVEPAEI FTMISTKLRA NTTAVLDESN RAGLTPHEAA
YALAQRRVLE AMQLRRQVPK KATDTIDVLV
//
