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Database: UniProt
Entry: A0A1G3WJ56_9BACT
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Original site: A0A1G3WJ56_9BACT 
ID   A0A1G3WJ56_9BACT        Unreviewed;       359 AA.
AC   A0A1G3WJ56;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:OHE40194.1};
GN   ORFNames=A2102_05020 {ECO:0000313|EMBL:OHE40194.1};
OS   Tenericutes bacterium GWF2_38_8.
OC   Bacteria; Mycoplasmatota.
OX   NCBI_TaxID=1802353 {ECO:0000313|EMBL:OHE40194.1, ECO:0000313|Proteomes:UP000177256};
RN   [1] {ECO:0000313|EMBL:OHE40194.1, ECO:0000313|Proteomes:UP000177256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHE40194.1}.
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DR   EMBL; MICY01000124; OHE40194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3WJ56; -.
DR   Proteomes; UP000177256; 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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 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}.
FT   DOMAIN          144..354
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        83
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   359 AA;  39984 MW;  9DDC1D2B28E2EF0A CRC64;
     MSDFKHFDYM EKHGYEQVVY FYDKTSGLKG ITCIHNTTLG PALGGTRLWN YASEEEAVVD
     CLRLARGMSY KNAAAGLNLG GGKTVLIGDP ETVKSEGYFR ALGRFVQSLN GRYITAEDVN
     TSTKDMDFVN METDHVVGLE GKSGNPSPMT ALGAFHGIRA ALQYKFKDED ISKYSFAVQG
     AGQTGYYLIK KLVEMKAKKI YFSEINKKHI ERMKKENPEV LFVEPKDFYA LDVDVIVPCA
     MGGSLNDTTI PQIKAKVIAG TANNVLLDED VHGNMLKEMG ILYAPDFVIN AGGVINVAHE
     LKGYNIGRAT RDIEKIYDRL TEIFTIAEKE NIHTQLAAKV YAKNRIETIK NVRGNYINR
//
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