A2RIB7 · NAOX_LACLM

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

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

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 μMbeta-NADHin the presence of oxygen
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
83 μmol/min/mgtoward 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.

TypeIDPosition(s)Description
Binding site7-11FAD (UniProtKB | ChEBI)
Active site10Proton acceptor
Binding site32FAD (UniProtKB | ChEBI)
Active site42Redox-active
Binding site42FAD (UniProtKB | ChEBI)
Binding site79FAD (UniProtKB | ChEBI)
Binding site109-112FAD (UniProtKB | ChEBI)
Binding site131FAD (UniProtKB | ChEBI)
Binding site158FAD (UniProtKB | ChEBI)
Binding site159NAD+ (UniProtKB | ChEBI)
Binding site178NAD+ (UniProtKB | ChEBI)
Binding site187NAD+ (UniProtKB | ChEBI)
Binding site244NAD+ (UniProtKB | ChEBI)
Binding site282FAD (UniProtKB | ChEBI)
Binding site298NAD+ (UniProtKB | ChEBI)
Binding site299FAD (UniProtKB | ChEBI)
Binding site300FAD (UniProtKB | ChEBI)
Binding site301FAD (UniProtKB | ChEBI)
Binding site329NAD+ (UniProtKB | ChEBI)
Binding site427FAD (UniProtKB | ChEBI)

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADH oxidase
  • EC number
  • Short names
    NOXase

Gene names

    • Name
      noxE
    • Ordered locus names
      llmg_0408

Organism names

Accessions

  • Primary accession
    A2RIB7
  • Secondary accessions
    • P81759
    • Q8KR34

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002929411-446NADH oxidase
Modified residue42Cysteine sulfinic acid (-SO2H)

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    446
  • Mass (Da)
    48,872
  • Last updated
    2007-03-06 v1
  • Checksum
    1B1FA2FE313D6C03
MKIVVIGTNHAGIATANTLLEQYPGHEIVMIDRNSNMSYLGCGTAIWVGRQIEKPDELFYAKAEDFEAKGVKILTETEVSEIDFANKKVYAKTKSDDEIIEAYDKLVLATGSRPIIPNLPGKDLKGIHFLKLFQEGQAIDAEFAKEKVKRIAVIGAGYIGTEIAEAAKRRGKEVLLFDAENTSLASYYDEEFAKGMDENLAQHGIELHFGELAKEFKANEEGYVSQIVTNKATYDVDLVINCIGFTANSALASDKLATFKNGAIKVDKHQQSSDPDVYAVGDVATIYSNALQDFTYIALASNAVRSGIVAGHNIGGKELESVGVQGSNGISIFGYNMTSTGLSVKAAKKLGLEVSFSDFEDKQKAWFLHENNDSVKIRIVYETKSRRIIGAQLASKSEIIAGNINMFSLAIQEKKTIDELALLDLFFLPHFNSPYNYMTVAALNAK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict11in Ref. 3; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY046926
EMBL· GenBank· DDBJ
AAL02357.1
EMBL· GenBank· DDBJ
Genomic DNA
AM406671
EMBL· GenBank· DDBJ
CAL97012.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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