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Protein

NADH oxidase

Gene

noxE

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

NADH + acceptor = NAD+ + reduced acceptor.1 Publication

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Enzyme regulationi

Inhibited by hydrogen peroxide, sulfhydryl reagents and quinine, but not by EDTA.1 Publication

Kineticsi

  1. KM=4.1 µM for beta-NADH (in the presence of oxygen)1 Publication
  1. Vmax=83 µmol/min/mg enzyme toward beta-NADH (in the presence of oxygen)1 Publication

pH dependencei

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Proton acceptorBy similarity
Active sitei42 – 421Redox-activeBy similarity
Binding sitei42 – 421FADBy similarity
Binding sitei159 – 1591NAD; via amide nitrogenBy similarity
Binding sitei178 – 1781NADBy similarity
Binding sitei187 – 1871NADBy similarity
Binding sitei244 – 2441NAD; via amide nitrogenBy similarity
Binding sitei282 – 2821FADBy similarity
Binding sitei298 – 2981NAD; via carbonyl oxygenBy similarity
Binding sitei300 – 3001FAD; via amide nitrogenBy similarity
Binding sitei329 – 3291NAD; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 115FADBy similarity
Nucleotide bindingi109 – 1124FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciLLAC416870:GCDT-419-MONOMER.
BRENDAi1.6.3.4. 2903.
SABIO-RKA2RIB7.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH oxidase (EC:1.6.99.3)
Short name:
NOXase
Gene namesi
Name:noxEImported
Ordered Locus Names:llmg_0408
OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic identifieri416870 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
ProteomesiUP000000364 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446NADH oxidasePRO_0000292941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Cysteine sulfenic acid (-SOH)By similarity

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi416870.llmg_0408.

Structurei

3D structure databases

ProteinModelPortaliA2RIB7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0446.
HOGENOMiHOG000276710.
OMAiRYEITIV.
OrthoDBiEOG6QVRCJ.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

A2RIB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIVVIGTNH AGIATANTLL EQYPGHEIVM IDRNSNMSYL GCGTAIWVGR
60 70 80 90 100
QIEKPDELFY AKAEDFEAKG VKILTETEVS EIDFANKKVY AKTKSDDEII
110 120 130 140 150
EAYDKLVLAT GSRPIIPNLP GKDLKGIHFL KLFQEGQAID AEFAKEKVKR
160 170 180 190 200
IAVIGAGYIG TEIAEAAKRR GKEVLLFDAE NTSLASYYDE EFAKGMDENL
210 220 230 240 250
AQHGIELHFG ELAKEFKANE EGYVSQIVTN KATYDVDLVI NCIGFTANSA
260 270 280 290 300
LASDKLATFK NGAIKVDKHQ QSSDPDVYAV GDVATIYSNA LQDFTYIALA
310 320 330 340 350
SNAVRSGIVA GHNIGGKELE SVGVQGSNGI SIFGYNMTST GLSVKAAKKL
360 370 380 390 400
GLEVSFSDFE DKQKAWFLHE NNDSVKIRIV YETKSRRIIG AQLASKSEII
410 420 430 440
AGNINMFSLA IQEKKTIDEL ALLDLFFLPH FNSPYNYMTV AALNAK
Length:446
Mass (Da):48,872
Last modified:March 6, 2007 - v1
Checksum:i1B1FA2FE313D6C03
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → AA AA sequence (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046926 Genomic DNA. Translation: AAL02357.1.
AM406671 Genomic DNA. Translation: CAL97012.1.
RefSeqiWP_011834457.1. NC_009004.1.

Genome annotation databases

EnsemblBacteriaiCAL97012; CAL97012; llmg_0408.
KEGGillm:llmg_0408.
PATRICi22281862. VBILacLac4574_0419.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046926 Genomic DNA. Translation: AAL02357.1.
AM406671 Genomic DNA. Translation: CAL97012.1.
RefSeqiWP_011834457.1. NC_009004.1.

3D structure databases

ProteinModelPortaliA2RIB7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_0408.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL97012; CAL97012; llmg_0408.
KEGGillm:llmg_0408.
PATRICi22281862. VBILacLac4574_0419.

Phylogenomic databases

eggNOGiCOG0446.
HOGENOMiHOG000276710.
OMAiRYEITIV.
OrthoDBiEOG6QVRCJ.

Enzyme and pathway databases

BioCyciLLAC416870:GCDT-419-MONOMER.
BRENDAi1.6.3.4. 2903.
SABIO-RKA2RIB7.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiNAOX_LACLM
AccessioniPrimary (citable) accession number: A2RIB7
Secondary accession number(s): P81759, Q8KR34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 6, 2007
Last modified: July 22, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.