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A2RIB7 (NAOX_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NADH oxidase
Short name=NOXase
EC=1.6.99.3
Gene names
Name:noxE
Ordered Locus Names:llmg_0408
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus ›

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.3

Catalytic activity

NADH + acceptor = NAD+ + reduced acceptor. Ref.2 Ref.3

Cofactor

Binds 1 FAD per subunit. Ref.2 Ref.3

Enzyme regulation

Inhibited by hydrogen peroxide, sulfhydryl reagents and quinine, but not by EDTA. Ref.2 Ref.3

Subunit structure

Homodimer. Ref.2 Ref.3

Sequence similarities

Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.

Biophysicochemical properties

Kinetic parameters:

KM=4.1 µM for beta-NADH (in the presence of oxygen) Ref.2 Ref.3

Vmax=83 µmol/min/mg enzyme toward beta-NADH (in the presence of oxygen) Ref.2

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. Ref.2

Ontologies

Keywords
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMOxidation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_functionNADH dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446NADH oxidase
PRO_0000292941

Regions

Nucleotide binding7 – 115FAD By similarity UniProtKB P37062
Nucleotide binding109 – 1124FAD By similarity UniProtKB P37062

Sites

Active site101Proton acceptor By similarity UniProtKB P37062
Active site421Redox-active By similarity UniProtKB P37062
Binding site421FAD By similarity UniProtKB P37062
Binding site1591NAD; via amide nitrogen By similarity UniProtKB P37062
Binding site1781NAD By similarity UniProtKB P37062
Binding site1871NAD By similarity UniProtKB P37062
Binding site2441NAD; via amide nitrogen By similarity UniProtKB P37062
Binding site2821FAD By similarity UniProtKB P37062
Binding site2981NAD; via carbonyl oxygen By similarity UniProtKB P37062
Binding site3001FAD; via amide nitrogen By similarity UniProtKB P37062
Binding site3291NAD; via carbonyl oxygen By similarity UniProtKB P37062

Amino acid modifications

Modified residue421Cysteine sulfenic acid (-SOH) By similarity UniProtKB P37062

Experimental info

Sequence conflict111A → AA AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
A2RIB7 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 1B1FA2FE313D6C03

FASTA44648,872
        10         20         30         40         50         60 
MKIVVIGTNH AGIATANTLL EQYPGHEIVM IDRNSNMSYL GCGTAIWVGR QIEKPDELFY 

        70         80         90        100        110        120 
AKAEDFEAKG VKILTETEVS EIDFANKKVY AKTKSDDEII EAYDKLVLAT GSRPIIPNLP 

       130        140        150        160        170        180 
GKDLKGIHFL KLFQEGQAID AEFAKEKVKR IAVIGAGYIG TEIAEAAKRR GKEVLLFDAE 

       190        200        210        220        230        240 
NTSLASYYDE EFAKGMDENL AQHGIELHFG ELAKEFKANE EGYVSQIVTN KATYDVDLVI 

       250        260        270        280        290        300 
NCIGFTANSA LASDKLATFK NGAIKVDKHQ QSSDPDVYAV GDVATIYSNA LQDFTYIALA 

       310        320        330        340        350        360 
SNAVRSGIVA GHNIGGKELE SVGVQGSNGI SIFGYNMTST GLSVKAAKKL GLEVSFSDFE 

       370        380        390        400        410        420 
DKQKAWFLHE NNDSVKIRIV YETKSRRIIG AQLASKSEII AGNINMFSLA IQEKKTIDEL 

       430        440 
ALLDLFFLPH FNSPYNYMTV AALNAK

« Hide

References

« Hide 'large scale' references
[1]"Metabolic engineering of lactic acid bacteria, the combined approach: kinetic modelling, metabolic control and experimental analysis."
Hoefnagel M.H.N., Starrenburg M.J.C., Martens D.E., Hugenholtz J., Kleerebezem M., Van Swam I.I., Bongers R., Westerhoff H.V., Snoep J.L.
Microbiology 148:1003-1013(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.
[3]"Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis."
Lopez de Felipe F., Hugenholtz J.
Int. Dairy J. 11:37-44(2001) [AGRICOLA] [Europe PMC]
Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY046926 Genomic DNA. Translation: AAL02357.1.
AM406671 Genomic DNA. Translation: CAL97012.1.
RefSeqYP_001031758.1. NC_009004.1.

3D structure databases

ProteinModelPortalA2RIB7.
ModBaseSearch...

Protein-protein interaction databases

STRING416870.llmg_0408.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL97012; CAL97012; llmg_0408.
GeneID4796799.
KEGGllm:llmg_0408.
PATRIC22281862. VBILacLac4574_0419.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0446.
HOGENOMHOG000276710.
KOK00359.
OMAAINFLTE.
ProtClustDBCLSK697203.

Enzyme and pathway databases

BioCycLLAC416870:GCDT-419-MONOMER.
SABIO-RKA2RIB7.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNAOX_LACLM
AccessionPrimary (citable) accession number: A2RIB7
Secondary accession number(s): P81759, Q8KR34
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 6, 2007
Last modified: May 29, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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