ID L8JN96_9BACT Unreviewed; 408 AA.
AC L8JN96;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase family protein {ECO:0000313|EMBL:ELR69683.1};
GN ORFNames=C900_04908 {ECO:0000313|EMBL:ELR69683.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR69683.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR69683.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR69683.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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:ELR69683.1}.
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DR EMBL; AMZN01000070; ELR69683.1; -; Genomic_DNA.
DR RefSeq; WP_009582061.1; NZ_AMZN01000070.1.
DR AlphaFoldDB; L8JN96; -.
DR STRING; 1237149.C900_04908; -.
DR PATRIC; fig|1237149.3.peg.4376; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000011135; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011135}.
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; 45129 MW; EBF7BA44BA6677DA CRC64;
MRELLHKFEN KKPEIVFEWN DEETGAEGWV VINSLRGGAA GGGTRMRKGL DKREVESLAK
TMEVKFTVSG PAIGGAKSGI NFDPNDPRKG EVLERWFAAV KPLMKYYYGT GGDLNVDEIH
EVIPITEDCG VWHPQEGVFK GHFQPTEAQM INRIGQLRHG VSKVLEDENF SPDLKRKYTV
ADMITGYGVA EAIRHYYDIW GGNVADKKAV IQGWGNVGAA AGFYLAQMGV KVIGIIDRDG
GVINKDGFSF EEITGYFLER KGNQLKAENI MSFDEVNSQV WDLGYEIFVP AAASRLVTKD
QVERMLAAGL EVLSCGANVP FADKEIFFGP IGVYTDERCS VIPDFIANCG MARVFAYLMS
DEVGLNDEDI FNDTSETIRK ALNKTHAVNA KKTNIASTSF EIALKQLV
//
