Detail Information for IndEnz0002002403
IED ID IndEnz0002002403
Enzyme Type ID protease002403
Protein Name Light-activated DNA-binding protein EL222
EL222
LOV-HTH DNA-binding protein
Gene Name ELI_04755
Organism Erythrobacter litoralis (strain HTCC2594)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Sphingomonadales Erythrobacteraceae Erythrobacter/Porphyrobacter group Erythrobacter Erythrobacter litoralis Erythrobacter litoralis (strain HTCC2594)
Enzyme Sequence MLDMGQDRPIDGSGAPGADDTRVEVQPPAQWVLDLIEASPIASVVSDPRLADNPLIAINQAFTDLTGYSEEECVGRNCRFLAGSGTEPWLTDKIRQGVREHKPVLVEILNYKKDGTPFRNAVLVAPIYDDDDELLYFLGSQVEVDDDQPNMGMARRERAAEMLKTLSPRQLEVTTLVASGLRNKEVAARLGLSEKTVKMHRGLVMEKLNLKTSADLVRIAVEAGI
Enzyme Length 225
Uniprot Accession Number Q2NB98
Absorption
Active Site
Activity Regulation
Binding Site BINDING 95; /note=FMN; /evidence=ECO:0007744|PDB:3P7N; BINDING 110; /note=FMN; /evidence=ECO:0007744|PDB:3P7N; BINDING 141; /note=FMN; /evidence=ECO:0007744|PDB:3P7N
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 183..202; /note=H-T-H motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00411
EC Number
Enzyme Function FUNCTION: Has reversible, light-dependent DNA-binding activity. Upon illumination an internal FMN-protein adduct is formed which changes the protein conformation so that the previously sequestered DNA-binding domain is free to bind DNA. Binds to sequences within in its own promoter when illuminated but not when it has been incubated in the dark. {ECO:0000269|PubMed:21606338}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 77..79; /note=FMN; /evidence=ECO:0007744|PDB:3P7N
Features Beta strand (5); Binding site (3); Chain (1); DNA binding (1); Domain (3); Helix (10); Modified residue (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Turn (1)
Keywords 3D-structure;Chromophore;DNA-binding;FMN;Flavoprotein;Nucleotide-binding;Reference proteome;Transcription;Transcription regulation
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 78; /note=S-4a-FMN cysteine; /evidence=ECO:0000305|PubMed:21606338
Post Translational Modification PTM: FMN binds covalently to cysteine after exposure to blue light, this bond is spontaneously broken in the dark; Cys-78 is 3.9 Angstroms from C4a of FMN in the dark, suggesting this is the adduct that is made. {ECO:0000305|PubMed:21606338}.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3P7N;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,741
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda