ID A0A1Y2PBL4_9FLAO Unreviewed; 408 AA.
AC A0A1Y2PBL4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:OSY87863.1};
GN ORFNames=WH52_09120 {ECO:0000313|EMBL:OSY87863.1};
OS Tenacibaculum holothuriorum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1635173 {ECO:0000313|EMBL:OSY87863.1, ECO:0000313|Proteomes:UP000194221};
RN [1] {ECO:0000313|EMBL:OSY87863.1, ECO:0000313|Proteomes:UP000194221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-2 {ECO:0000313|EMBL:OSY87863.1,
RC ECO:0000313|Proteomes:UP000194221};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Tenacibaculum sp. S2-2, isolated from intestinal
RT microbiota of sea cucumber, Apostichopus japonicas.";
RL Submitted (MAR-2015) 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:OSY87863.1}.
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DR EMBL; LAPZ01000006; OSY87863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2PBL4; -.
DR STRING; 1635173.WH52_09120; -.
DR InParanoid; A0A1Y2PBL4; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000194221; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000194221}.
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; 45329 MW; 9E4CC05636408B05 CRC64;
MKDLLKKYEE KQPEIVFNWK DPETEAEGWT VINSLRGGAA GGGTRMRKGL DKYEVMSLAK
TMEVKFTVSG PAIGGAKSGI NFDPHDPRKK GVLERWYKAV APLLKNYYGT GGDLNVDEIH
EVIPITEDSG VWHPQEGVFN GHFKPTEADK INRIGQLRHG VIKVLEDENL SPSVTRKYTV
ADMITGYGVA EAVKHYYDIY GGSVVGKRAI VQGFGNVGSA AAYYLAQMGA KVVGIIDREG
GVINEEGFSF EEIKEMFLDK DGNTLVAKNM IPFEEMNTRI WNLPCEIFAP CAASRLVQQD
QINKMINTGL EVISCGANVP FADKEIFFGP IMEDTDKKVS LIPDFISNCG MARVFAYFME
RRVEMSDEAI FEDTSNTIKK ALQRTFAKSA SKTRISETAF EIALKELI
//
