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Database: UniProt
Entry: A0A167WSE6_9FLAO
LinkDB: A0A167WSE6_9FLAO
Original site: A0A167WSE6_9FLAO 
ID   A0A167WSE6_9FLAO        Unreviewed;       408 AA.
AC   A0A167WSE6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:OAB27702.1};
GN   ORFNames=FBFR_11045 {ECO:0000313|EMBL:OAB27702.1};
OS   Flavobacterium fryxellicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB27702.1, ECO:0000313|Proteomes:UP000077164};
RN   [1] {ECO:0000313|EMBL:OAB27702.1, ECO:0000313|Proteomes:UP000077164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB27702.1,
RC   ECO:0000313|Proteomes:UP000077164};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Flavobacterium fryxellicola DSM 16209.";
RL   Submitted (MAR-2016) 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}.
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:OAB27702.1}.
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DR   EMBL; LVJE01000016; OAB27702.1; -; Genomic_DNA.
DR   RefSeq; WP_066081182.1; NZ_LVJE01000016.1.
DR   AlphaFoldDB; A0A167WSE6; -.
DR   STRING; 249352.SAMN05444395_105185; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000077164; 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; 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; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          181..408
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   408 AA;  44607 MW;  69C0D708BE0EAA59 CRC64;
     MKDLLKKFEN KEPEIVFHWK DAETGAEGWT VINSLRGGAA GGGTRMRKGL DMNEVLSLAK
     TMEVKFSVSG PAIGGAKSGI NFDPNDPRKK GVLQRWYKAV SPLLKSYYGT GGDLNVDEIH
     EVIPMTEECG VWHPQEGVFN GHFKPTEADK INRIGQLRQG VVKVIENPRF SPDVSKKYTV
     ADMITGFGVA EAVRNYYAIY GGEVKGKKAI VQGFGNVGSA AAFYLAEMGV KVIGIIDRDG
     GLINEEGFSF EEIRALFIAK DGNKLVAKNM IPFDEINEKI WTIGAEIFTP CAASRLVTQS
     QIDSLIGNGL EVISCGANVP FADAAIFFGP IMEDVDHKVS LIPDFISNCG MARVFAYFME
     KKVQMTDEAI FQDTSETIRK AIEKAHALNS SKTNISATAF EIALKQLV
//
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