ID A0A1Q8QXW4_9FIRM Unreviewed; 355 AA.
AC A0A1Q8QXW4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:OLN32171.1};
GN ORFNames=DSOL_1777 {ECO:0000313|EMBL:OLN32171.1};
OS Desulfosporosinus metallidurans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN32171.1, ECO:0000313|Proteomes:UP000186102};
RN [1] {ECO:0000313|EMBL:OLN32171.1, ECO:0000313|Proteomes:UP000186102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL {ECO:0000313|EMBL:OLN32171.1,
RC ECO:0000313|Proteomes:UP000186102};
RA Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT "Complete genome of Desulfosporosinus sp. OL.";
RL Submitted (SEP-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|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:OLN32171.1}.
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DR EMBL; MLBF01000010; OLN32171.1; -; Genomic_DNA.
DR RefSeq; WP_075364461.1; NZ_MLBF01000010.1.
DR AlphaFoldDB; A0A1Q8QXW4; -.
DR STRING; 1888891.DSOL_1777; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000186102; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186102}.
FT DOMAIN 144..351
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 355 AA; 38910 MW; 943D30402924A878 CRC64;
MEIFDYLEKY DYEQLVICQD QTSGLKAIIC IHDTTLGPAL GGTRMWNYAN EEEAILDALR
LARGMTYKNA AAGLNLGGGK TVIIGDSRTQ KSEELFRAFG RYVQSLNGRY ITAEDVGTTV
RDMDWVHLET DFVTGVSSSY GASGDPSPMT ARGVWRGMKA TAKEVYGNDS LNGKVIAIQG
LGHVGHDLAK HLHGEGASLI VTDIHQEAVK RVVEETGAKA VGLEEIYGVQ ADIFAPCALG
AVINDETIPQ LKVQIIAGAA NNVLKEERHG DKLHELGILY APDYVINSGG VINVADELEG
YNYERALKKV EMVYDNVAKV LKIAKQDNIP TYQAADRMAE ERIMKIGRVR SNYLR
//
