ID A0A1N7N1Y4_9RHOB Unreviewed; 346 AA.
AC A0A1N7N1Y4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:SIS92386.1};
GN ORFNames=SAMN05421774_10362 {ECO:0000313|EMBL:SIS92386.1};
OS Gemmobacter megaterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIS92386.1, ECO:0000313|Proteomes:UP000186141};
RN [1] {ECO:0000313|EMBL:SIS92386.1, ECO:0000313|Proteomes:UP000186141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26375 {ECO:0000313|EMBL:SIS92386.1,
RC ECO:0000313|Proteomes:UP000186141};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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 ---------------------------------------------------------------------------
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; FTOT01000003; SIS92386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7N1Y4; -.
DR STRING; 1086013.SAMN05421774_10362; -.
DR Proteomes; UP000186141; 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 CDD; cd01075; NAD_bind_Leu_Phe_Val_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; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186141}.
FT DOMAIN 137..343
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 72
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 172..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 346 AA; 35664 MW; 49FB6C04B495D3C9 CRC64;
MTQPEDIVDF HDPDTGLVGC IVLHSTALGP AAGGCRLWQY ADPQAMRADA MRLAEGMSYK
NALAGLPMGG GKAVIRRPPG HFNREALFRA FGRVVDGLGG RYITAEDVGT SVEDMLAVAS
STRHVAGLPA DGPGPGGDPS PWTAQGVFVS MRASVQRRLG TDLAGCVVAI QGLGHVGSAL
ADLLHAAGAR LVVADLSDAH VRQVAARTGA RIVPPDRIHA TEAHVFAPCA LGAVIHAGTI
PELRAKVICG AANNQLATPQ DGARLAARDI LYAPDYVVNA GGIINVAGEH LGWSADQTRS
RVLETAGRLD QVFRFADTAG VAPDVAADEL ARAAIGAAAQ IVQAPA
//
