ID A0A410G391_9FLAO Unreviewed; 408 AA.
AC A0A410G391;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:QAA81758.1};
GN ORFNames=EI546_08510 {ECO:0000313|EMBL:QAA81758.1};
OS Aequorivita sp. H23M31.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=2494375 {ECO:0000313|EMBL:QAA81758.1, ECO:0000313|Proteomes:UP000285517};
RN [1] {ECO:0000313|EMBL:QAA81758.1, ECO:0000313|Proteomes:UP000285517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H23M31 {ECO:0000313|EMBL:QAA81758.1,
RC ECO:0000313|Proteomes:UP000285517};
RA Bae J.-W.;
RT "Complete genome sequencing of Aequorivita sp. H23M31.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP034951; QAA81758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410G391; -.
DR KEGG; aev:EI546_08510; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000285517; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000285517}.
FT DOMAIN 181..407
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 408 AA; 44808 MW; 9BED704362F56143 CRC64;
MKDLLKKYEE KEPEIIFHWN DPETEAEGWT VINSLRGGAA GGGTRMRKGL DMNEVLSLAK
TMEVKFTVAG PPIGGAKSGI NFDPFDPRKK GVLERWFKAV SPLLKAYYGT GGDMNVDQRL
EVIPFLEQNG IGHPQEGVFN GHFNPSEEDK INRISQLRNG VGKTVENPKY SPDVSGGYKV
ADMITGFGVA EAVKHYYNIY GGSVKGKRAI IQGFGNVGSA AAYYLSQMGA KIVGIIDRDG
GIINQDGFSF GEIKQLFVNK DGNTLVADNM IPFDEINEQI WKLNAEIFAP CAASRIVTKD
QVSQMIEKGL EVISCGANVP FADKEIFFGP IMEYTDEHLS LIPDFISNCG MARVFAYLME
GKVELSDEAV FNDASMTIKR AIQNVFIANN SKANVSKTAF EIALKQLI
//
