ID A0A2N0FSF8_9FLAO Unreviewed; 410 AA.
AC A0A2N0FSF8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase {ECO:0000313|EMBL:PKA97375.1};
GN ORFNames=B0O79_1031 {ECO:0000313|EMBL:PKA97375.1};
OS Flavobacteriaceae bacterium MAR_2009_75.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250285 {ECO:0000313|EMBL:PKA97375.1, ECO:0000313|Proteomes:UP000232536};
RN [1] {ECO:0000313|EMBL:PKA97375.1, ECO:0000313|Proteomes:UP000232536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_75 {ECO:0000313|EMBL:PKA97375.1,
RC ECO:0000313|Proteomes:UP000232536};
RA Teeling H.;
RT "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT Genomic & Taxonomic Observatory).";
RL Submitted (NOV-2017) 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:PKA97375.1}.
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DR EMBL; PHTZ01000001; PKA97375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0FSF8; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000232536; 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..409
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 410 AA; 45311 MW; 7CE1EE0769304196 CRC64;
MKELLHTYEN KAPEIVFNWK DSETDAEGWT VINSLRGGAA GGGTRMREGL DMNEVLSLAK
TMEVKFTVSG PPIGGAKSGI NFDPNDPRKK GVLERWYHAV SPLLKSYYGT GGDLNVDEIH
EVIPITEDAG VWHPQEGVFN GHFKPTEADK INRIGQLRLG VIKPLEHSEY SPDTSRKFTV
ADMITGFGVA EAVRHYYDVY GGDVEGKRAV VQGFGNVGAA AAYYLAQMGA KVVGIIDRAG
GIIKEEGFSF EEIKTLFLNK KGNTLVADAD QLISFEEINE RIWKLPTEIF APCAASRLIQ
KEQISRMIES GLEIISCGAN VPFADKEIFF GPIMEYADGK VSLIPDFISN CGMARVFAYF
MEKRVAMDDE MIFNDTSLTI KKAILNIFSQ NSSPKNISRK AFEIALKQLI
//
