ID K2JU58_9GAMM Unreviewed; 348 AA.
AC K2JU58;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:EKE86981.1};
GN ORFNames=A10D4_02027 {ECO:0000313|EMBL:EKE86981.1};
OS Idiomarina xiamenensis 10-D-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE86981.1, ECO:0000313|Proteomes:UP000014115};
RN [1] {ECO:0000313|EMBL:EKE86981.1, ECO:0000313|Proteomes:UP000014115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-D-4 {ECO:0000313|EMBL:EKE86981.1,
RC ECO:0000313|Proteomes:UP000014115};
RX PubMed=23209204; DOI=10.1128/JB.01855-12;
RA Lai Q., Wang L., Wang W., Shao Z.;
RT "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL J. Bacteriol. 194:6938-6938(2012).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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:EKE86981.1}.
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DR EMBL; AMRG01000002; EKE86981.1; -; Genomic_DNA.
DR RefSeq; WP_008487407.1; NZ_AMRG01000002.1.
DR AlphaFoldDB; K2JU58; -.
DR SMR; K2JU58; -.
DR STRING; 740709.A10D4_02027; -.
DR PATRIC; fig|740709.3.peg.408; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000014115; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000014115}.
FT DOMAIN 141..348
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 177..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 348 AA; 37147 MW; C3ABBE5695BC691B CRC64;
MSLFEHKEFD QHEQVVFCHD KATGLKAIIA IHDTTMGPAL GGTRLWNYAS SSEALTDVLR
LSRGMTYKSA ISGLPLGGGK AVIIGDAKQI KSAELFRAYG RFVNSLSGRY ITAEDVNIRT
SDIAIVAEET NFVAGTEGKA GDPSPHTALG TYLGLKIAAK HRLGSEDLSG VKIAVQGLGA
VGYAFAEYLA KDGAELFVTD INEEAVNKAV NELGATAVGL DDIYGLDVDI YAPCALGATI
NDDTLQQLKA KVIAGSANNQ LATPKHDQLV KDQGILYAPD YVINAGGVIH ICSEAANFTV
EETEKRVRGI YDTLDNVFTR AAEQNRPTGE IADAMAREII ANEKKKKA
//
