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Database: UniProt
Entry: A0A2N3IJ69_9BACT
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ID   A0A2N3IJ69_9BACT        Unreviewed;       410 AA.
AC   A0A2N3IJ69;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Glutamate/Leucine/Phenylalanine/Valine dehydrogenase {ECO:0000313|EMBL:PKQ70364.1};
GN   ORFNames=Rain11_0592 {ECO:0000313|EMBL:PKQ70364.1};
OS   Raineya orbicola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX   NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ70364.1, ECO:0000313|Proteomes:UP000233387};
RN   [1] {ECO:0000313|EMBL:PKQ70364.1, ECO:0000313|Proteomes:UP000233387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ70364.1,
RC   ECO:0000313|Proteomes:UP000233387};
RA   Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA   Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT   "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT   the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PKQ70364.1}.
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DR   EMBL; NKXO01000007; PKQ70364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3IJ69; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000233387; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233387}.
FT   DOMAIN          182..410
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   410 AA;  45277 MW;  AF63075EF805A80A CRC64;
     MKELLTKFEN KPAEIVFEWH DSETEAKGWI VINSLRGGAA GGGTRMRKGL DRREVESLAK
     TMEIKFTVSG PPIGGAKSGI DFDPQDPRKH EVLKRWYKVA FALLKNYYGT GGDLNVDEIH
     EVIPITEEYG LWHPQEGIVN GHYNPSKPEK IRKIGQLRQG VSKIIEDARY IPDGAKRKYT
     VADMITGYGV AEAIRHFYTL WGGELKGKRA IIQGWGNVGA TAALYLAKEG AKIVGIIDRV
     GGLLNPNGFT LDEIKKLFAD RSSNFLVAEK LLPFEEVNQQ IWSVGAEVFV PAAASRLVTQ
     QQAELLIQNG LEVVSCGANV PFADPEIFYG KIAQFVDSKV ALIPDFVANC GMARTFAYLM
     SEKGSNITDQ AIFSDISETI FNALQKVHQS NTAKTLLSEK AFEIALKQLV
//
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