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Database: UniProt
Entry: A0A0U4BVT0_9BACT
LinkDB: A0A0U4BVT0_9BACT
Original site: A0A0U4BVT0_9BACT 
ID   A0A0U4BVT0_9BACT        Unreviewed;       363 AA.
AC   A0A0U4BVT0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:ALW84353.1};
GN   ORFNames=AUC43_04165 {ECO:0000313|EMBL:ALW84353.1};
OS   Hymenobacter sedentarius.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW84353.1, ECO:0000313|Proteomes:UP000059542};
RN   [1] {ECO:0000313|EMBL:ALW84353.1, ECO:0000313|Proteomes:UP000059542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5B {ECO:0000313|EMBL:ALW84353.1,
RC   ECO:0000313|Proteomes:UP000059542};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; CP013909; ALW84353.1; -; Genomic_DNA.
DR   RefSeq; WP_068190256.1; NZ_CP013909.1.
DR   AlphaFoldDB; A0A0U4BVT0; -.
DR   STRING; 1411621.AUC43_04165; -.
DR   KEGG; hyg:AUC43_04165; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000059542; Chromosome.
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|ARBA:ARBA00023027, 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:UP000059542}.
FT   DOMAIN          153..361
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT   BINDING         189..194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ   SEQUENCE   363 AA;  39316 MW;  11DF53208C4351BB CRC64;
     MIEAQTLAPE AIFGQIAEHQ HEQVVFCHDH ETGLKAIIGI HNTVLGPALG GTRMWHYASD
     MEALNDVLRL SRGMTYKAAI SGLNLGGGKA VIIGDAKTLK TEALLRKFGR FVKNLNGKYI
     TAEDVNMTTK DMEYIRMETK HVAGLPESMG GSGDPSPVTA FGTYMGMKAA AKKAFGSDSL
     KDKRIGVQGV GHVGTYLLEY LQKEGAKLIV TDYYEDRALE AAARFGATAV GLEEIYDQQM
     DIYSPCALGA TLNDETIPRL KCQVVAGCAN NQLKVENQHG PELVRRGIVY APDFLINAGG
     LINVYSEVVG TSRQGALTQT EKIYDYTLQV LAKAEEEGTH PQAAAIKQAK ERIASVGKVK
     STY
//
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