Detail Information for IndEnz0018000787
IED ID IndEnz0018000787
Enzyme Type ID peroxidase000787
Protein Name NADH oxidase
NOXase
EC 7.1.1.2
Gene Name nox EF_1586
Organism Enterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecalis (Streptococcus faecalis) Enterococcus faecalis (strain ATCC 700802 / V583)
Enzyme Sequence MKVVVVGCTHAGTSAVKSILANHPEAEVTVYERNDNISFLSCGIALYVGGVVKNAADLFYSNPEELASLGATVKMEHNVEEINVDDKTVTAKNLQTGATETVSYDKLVMTTGSWPIIPPIPGIDAENILLCKNYSQANVIIEKAKDAKRVVVVGGGYIGIELVEAFVESGKQVTLVDGLDRILNKYLDKPFTDVLEKELVDRGVNLALGENVQQFVADEQGKVAKVITPSQEFEADMVIMCVGFRPNTELLKDKVDMLPNGAIEVNEYMQTSNPDIFAAGDSAVVHYNPSQTKNYIPLATNAVRQGMLVGRNLTEQKLAYRGTQGTSGLYLFGWKIGSTGVTKESAKLNGLDVEATVFEDNYRPEFMPTTEKVLMELVYEKGTQRIVGGQLMSKYDITQSANTLSLAVQNKMTVEDLAISDFFFQPHFDRPWNYLNLLAQAALENM
Enzyme Length 446
Uniprot Accession Number P37061
Absorption
Active Site ACT_SITE 10; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 42; /note=Redox-active; /evidence=ECO:0000269|PubMed:8262333
Activity Regulation
Binding Site BINDING 32; /note=FAD; /evidence=ECO:0000250; BINDING 42; /note=FAD; /evidence=ECO:0000250; BINDING 177; /note=NAD; /evidence=ECO:0000250; BINDING 186; /note=NAD; /evidence=ECO:0000250; BINDING 243; /note=NAD; via amide nitrogen; /evidence=ECO:0000250; BINDING 299; /note=FAD; via amide nitrogen; /evidence=ECO:0000250; BINDING 328; /note=NAD; via carbonyl oxygen; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
DNA Binding
EC Number 7.1.1.2
Enzyme Function FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to water.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 7..11; /note=FAD; /evidence=ECO:0000250; NP_BIND 110..113; /note=FAD; /evidence=ECO:0000250; NP_BIND 150..165; /note=NAD; /evidence=ECO:0000250; NP_BIND 271..281; /note=FAD; /evidence=ECO:0000250
Features Active site (2); Binding site (7); Chain (1); Modified residue (1); Nucleotide binding (4)
Keywords Direct protein sequencing;FAD;Flavoprotein;NAD;Oxidation;Oxidoreductase;Redox-active center;Reference proteome;Translocase
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 42; /note=Cysteine sulfenic acid (-SOH); /evidence=ECO:0000269|PubMed:8262333
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 48,915
Kinetics
Metal Binding
Rhea ID RHEA:29091
Cross Reference Brenda