ID A0A3N2AP12_9MICO Unreviewed; 354 AA.
AC A0A3N2AP12;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase {ECO:0000313|EMBL:ROR64726.1};
GN ORFNames=EDD26_0073 {ECO:0000313|EMBL:ROR64726.1};
OS Agrococcus jenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=46353 {ECO:0000313|EMBL:ROR64726.1, ECO:0000313|Proteomes:UP000275456};
RN [1] {ECO:0000313|EMBL:ROR64726.1, ECO:0000313|Proteomes:UP000275456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9580 {ECO:0000313|EMBL:ROR64726.1,
RC ECO:0000313|Proteomes:UP000275456};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, 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:ROR64726.1}.
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; RKHJ01000001; ROR64726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2AP12; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000275456; Unassembled WGS sequence.
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; 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; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 143..348
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 77
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 181..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 354 AA; 36507 MW; 50885577CB6D13FE CRC64;
MSAIPEFNHE RVLTSMGARS DVVITVALHS SVLGPALGGC RMWTYPTWAD GQADALRLSS
AMTLKNAAAG LDAGGGKAVI ALPMGTRIDA DRRRAALLDL GDLVEALDGR YRTAEDVGTT
EHDMLVVRER TEHVVGLPAE NGGAGEPAGA TALGVYSSIA PTLEEAFGSD DIAARSFVIS
GLGQVGGRLA RMLAGHGATL FLTDIDGRKQ QLADDLGATW IAPGEALTTP ADVLVPAGLG
GILTDEAIEA LPVRAVVGPA NNPLAEHSGA ARLAERGIVY APDFVVNAGG VIHLQGMADG
MQWPAIAERL TGISDTLRGV FASARQRGIT PLEAAEALAA ERIDAARGRM TVSA
//
