ID A0A1L3ME69_9MICO Unreviewed; 357 AA.
AC A0A1L3ME69;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:APH00632.1};
GN ORFNames=ASJ30_03035 {ECO:0000313|EMBL:APH00632.1};
OS Janibacter indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=857417 {ECO:0000313|EMBL:APH00632.1, ECO:0000313|Proteomes:UP000182938};
RN [1] {ECO:0000313|EMBL:APH00632.1, ECO:0000313|Proteomes:UP000182938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFY001 {ECO:0000313|EMBL:APH00632.1,
RC ECO:0000313|Proteomes:UP000182938};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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; CP013290; APH00632.1; -; Genomic_DNA.
DR RefSeq; WP_072623800.1; NZ_CP013290.1.
DR AlphaFoldDB; A0A1L3ME69; -.
DR KEGG; jte:ASJ30_03035; -.
DR Proteomes; UP000182938; 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; 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:UP000182938}.
FT DOMAIN 152..352
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 357 AA; 36694 MW; 8354D2A9211F7A5B CRC64;
MTTVTHPVPT SDAIATPWAS EQTITCRDDR VGLRAIIAID DTTLGPGFGG VRYRAYPSTE
AAAREAQRLA AAMTLKHALA ELPYGGAKSV VVLDGDAPAP GSPERRALFA RFGEMIARTA
GSYVPGVDMG TLLEDMQTIR DDGGARAFCD EVSPSPFTAR GVYAAMRAAA VHHHGEGGLS
GLRVVVQGIG SVGEEVARLA HGDGARVTLA DIDTARAQAL ATELGGDTVP TEAAPFTEAD
VFAPCAVARV VTRDSIDRLP ARIIAGAAND TLDSPDCAGA LQAAGITFVP DFVANAGGVI
QVHGGVAGWS PEETLAAIDR IGERVTGLLA AAEAEGITPV EAALRRADAA LGRTVVR
//
