ID A0A1C7IDL1_9FIRM Unreviewed; 390 AA.
AC A0A1C7IDL1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=A4V09_12840 {ECO:0000313|EMBL:ANU76579.1};
OS Blautia pseudococcoides.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1796616 {ECO:0000313|EMBL:ANU76579.1, ECO:0000313|Proteomes:UP000092574};
RN [1] {ECO:0000313|Proteomes:UP000092574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL58 {ECO:0000313|Proteomes:UP000092574};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-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}.
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DR EMBL; CP015405; ANU76579.1; -; Genomic_DNA.
DR RefSeq; WP_065542740.1; NZ_CP065312.1.
DR AlphaFoldDB; A0A1C7IDL1; -.
DR STRING; 1796616.A4V09_12840; -.
DR KEGG; byl:A4V09_12840; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000092574; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
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 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.
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:UP000092574}.
FT DOMAIN 156..387
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 70
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 106
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 390 AA; 42819 MW; FC23181261EF7033 CRC64;
MANKPYLVVE WNDTETDAKG WMCAYNFVNH YCGGGTRMHP TVTKEEVIRL ATTMGYKYKA
CESLTTGGCK AGIAYDYKAP DALDVLRRFL TATAPVINAG VSIGGDLGVD YSDVLRILDD
LGIGIPQTKA MKEDPDIHQG IVNHDRAEKE LTYDGFKMYD MITGYGVAAA ADEAWKMKGG
KEGASVIIQG FGCVGASCVN SLNNMGYKVI GIADVNGLVY CKDGLDIPKL VATRLPKGEL
NKESFEDNYE IYPNSQWLEK ECDILIPAAL EDVINKDNAD KIKASLLVEA ANIPTTSEAD
EILRKNGVDV AVDFISNLGG IRIYEAVIFR LVKIENMSDE DAAAAIVNDT TDLIRKQTRR
VFEESKKTGE FTRDVARRLF TPDKSDTPDM
//
