A2RIB7 · NAOX_LACLM
- ProteinNADH oxidase
- GenenoxE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids446 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the four-electron reduction of molecular oxygen to water. Active on beta-NADH, but not on alpha-NADH, beta-NADPH or alpha-NADPH. Under aerobic conditions, oxygen acts as the electron acceptor. Under anaerobic conditions, DCIP and MB can replace oxygen as the electron acceptor.
Catalytic activity
NADH oxidase
2 H+ + 2 NADH + O2 = 2 H2O + 2 NAD+
Cofactor
Note: Binds 1 FAD per subunit.
Activity regulation
Inhibited by hydrogen peroxide, sulfhydryl reagents and quinine, but not by EDTA.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.1 μM | beta-NADH | in the presence of oxygen |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
83 μmol/min/mg | toward beta-NADH (in the presence of oxygen) |
pH Dependence
Optimum pH is 6.0-9.0. Below pH 6.0 the enzyme is reversibly inactivated, above pH 10.0 the enzyme is irreversibly inactivated.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7-11 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GTNHA | ||||||
Active site | 10 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 32 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 42 | Redox-active | ||||
Sequence: C | ||||||
Binding site | 42 | FAD (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 79 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 109-112 | FAD (UniProtKB | ChEBI) | ||||
Sequence: ATGS | ||||||
Binding site | 131 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 158 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 159 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 178 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 187 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 244 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 282 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 298 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 299 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 300 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 301 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 329 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 427 | FAD (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NADH dehydrogenase (ubiquinone) activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADH oxidase
- EC number
- Short namesNOXase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus > Lactococcus cremoris subsp. cremoris
Accessions
- Primary accessionA2RIB7
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000292941 | 1-446 | NADH oxidase | |||
Sequence: MKIVVIGTNHAGIATANTLLEQYPGHEIVMIDRNSNMSYLGCGTAIWVGRQIEKPDELFYAKAEDFEAKGVKILTETEVSEIDFANKKVYAKTKSDDEIIEAYDKLVLATGSRPIIPNLPGKDLKGIHFLKLFQEGQAIDAEFAKEKVKRIAVIGAGYIGTEIAEAAKRRGKEVLLFDAENTSLASYYDEEFAKGMDENLAQHGIELHFGELAKEFKANEEGYVSQIVTNKATYDVDLVINCIGFTANSALASDKLATFKNGAIKVDKHQQSSDPDVYAVGDVATIYSNALQDFTYIALASNAVRSGIVAGHNIGGKELESVGVQGSNGISIFGYNMTSTGLSVKAAKKLGLEVSFSDFEDKQKAWFLHENNDSVKIRIVYETKSRRIIGAQLASKSEIIAGNINMFSLAIQEKKTIDELALLDLFFLPHFNSPYNYMTVAALNAK | ||||||
Modified residue | 42 | Cysteine sulfinic acid (-SO2H) | ||||
Sequence: C |
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Length446
- Mass (Da)48,872
- Last updated2007-03-06 v1
- Checksum1B1FA2FE313D6C03
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 11 | in Ref. 3; AA sequence | ||||
Sequence: A → AA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY046926 EMBL· GenBank· DDBJ | AAL02357.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM406671 EMBL· GenBank· DDBJ | CAL97012.1 EMBL· GenBank· DDBJ | Genomic DNA |