ID   A0A0M2XPH8_9SPHI        Unreviewed;       412 AA.
AC   A0A0M2XPH8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:KKO89377.1};
GN   ORFNames=AAW12_21030 {ECO:0000313|EMBL:KKO89377.1};
OS   Sphingobacterium sp. Ag1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO89377.1, ECO:0000313|Proteomes:UP000034524};
RN   [1] {ECO:0000313|EMBL:KKO89377.1, ECO:0000313|Proteomes:UP000034524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKO89377.1,
RC   ECO:0000313|Proteomes:UP000034524};
RA   Pei D., Yu W., Kukutla P., Xu J.;
RT   "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) 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:KKO89377.1}.
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DR   EMBL; LBGU01000044; KKO89377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2XPH8; -.
DR   PATRIC; fig|1643451.3.peg.159; -.
DR   Proteomes; UP000034524; 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}.
FT   DOMAIN          181..411
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   412 AA;  45812 MW;  46AFC167195E8051 CRC64;
     MKELLGAFEH KSPEIVFEWK DSETDARGWI VINSLRGGAA GGGTRMRAGL DRHEVESLAK
     TMEVKFTVSG PAIGGAKSGI DFDPHDPRKN EVLERWFKVV TPLLKNYYGT GGDLNIDEIH
     DVIPLTEEYG LWHPQEGILN GHFKVNESNR IHQIGQLRYG VSKVLEDSSY SPDLKRKYKV
     ADMITGYGVS ESIRHYYQLF GENCFGKRAI IQGWGNVAAA AAFYLSKLGV KIVGIIDRVG
     GLINPEGFGE EDITRLLLER KGNELCSPDL ISFDQIQKEI WSLETDIFVP AAASRLVSKD
     QIQQLINHGL EVIASGANVP FADQEIFYGP VMEFADQHVA VIPDFIANCG MARVFAYLMQ
     RNIEISDDAI FSDVSSVIFE ALKKIRSVSS EKTHISSRAY EIALKQLVET GN
//