ID   A0A267TC31_9BACT        Unreviewed;       419 AA.
AC   A0A267TC31;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:PAC30362.1};
GN   ORFNames=BWI92_12720 {ECO:0000313|EMBL:PAC30362.1};
OS   Flectobacillus sp. BAB-3569.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Flectobacillus.
OX   NCBI_TaxID=1509483 {ECO:0000313|EMBL:PAC30362.1, ECO:0000313|Proteomes:UP000215844};
RN   [1] {ECO:0000313|EMBL:PAC30362.1, ECO:0000313|Proteomes:UP000215844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-3569 {ECO:0000313|EMBL:PAC30362.1,
RC   ECO:0000313|Proteomes:UP000215844};
RA   Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT   "Flectobacillus sp. BAB-3569 genome sequencing.";
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:PAC30362.1}.
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DR   EMBL; NJFZ01000012; PAC30362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267TC31; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000215844; 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:UP000215844}.
FT   DOMAIN          184..418
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   419 AA;  46326 MW;  8A4A188435F56659 CRC64;
     MKEALKRFEN KRPEIVFEWK DSETEAEGWV VINSLRGGAA GGGTRMRKGL DKREVESLAK
     TMEIKFTVSG PQIGGAKSGI NFDPSDPRKK GVLERWYKAV APLLKNYYGT GGDLNVDEVH
     EVIPVTEKYG LWHPQEGIVN GHFHASEAQK IRLIGQLRQG VSKIIEDWNY TPTSTQNIHR
     YTVSDLITGY GVAEAVKHYY SLWGGNLSEK RAIIQGWGNV AAAAGLNLAR MGVKIVGIID
     RNGGLVVPEG LGLEEIKDLF FNKKQNTLYA ENMLSFEETN AKIWEVGAEI FIPAAASRIV
     SAEQVEKLVN NGLEVISCGA NVPFNDPEIF YGPTMELADN KVALIPDFVA NCGMARVFAY
     LMSDSAMVTD EGIFEDVSET IYKALDELHA QHQGRTLLAN ELYSIALEKL ENKVEVESV
//