ID A0A2T3HHM3_9SPHI Unreviewed; 359 AA.
AC A0A2T3HHM3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:PST81939.1};
GN ORFNames=C7T94_17270 {ECO:0000313|EMBL:PST81939.1};
OS Pedobacter yulinensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2126353 {ECO:0000313|EMBL:PST81939.1, ECO:0000313|Proteomes:UP000240912};
RN [1] {ECO:0000313|EMBL:PST81939.1, ECO:0000313|Proteomes:UP000240912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL28-9 {ECO:0000313|EMBL:PST81939.1,
RC ECO:0000313|Proteomes:UP000240912};
RA Keele B.F.;
RL Submitted (MAR-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:PST81939.1}.
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DR EMBL; PYLS01000007; PST81939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3HHM3; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000240912; 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:UP000240912}.
FT DOMAIN 149..357
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 85
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 185..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 359 AA; 38782 MW; 4E9EF01432BCCF13 CRC64;
MSEQSPSVLD QLSASGHKKV VFCNDSDSGL KAIIAIHDTT LGPALGGTRM YNYASEAEAL
EDVLRLSKRM TYKSAITGLN LGGGKGVIIG DSRKDKSEAL MRSYGRFIKN LNGEYITAEE
LGTTARDMEY IRMETQYVTG VPESLGGAGD PAPFSAQGVY YGIKASLKEV YGSDMLAGKT
VVVQGIGKVG EHLVSLLRKE NAVVLISDIN KDLTMHVASK YKAKPIDADK IFGIEADVYA
PCALGATIND KTIDKMKFAV IAGSANNQLA DDEKHGRALL EKGVVFAPDY LINAGGLISC
YSELTGLGKK RTIQLTEHIY DATREVLRMS KKENIPTLEA ANRIAEQRIA SIKKIKSSY
//
