NADH oxidase - Lactococcus lactis subsp. cremoris (strain MG1363)

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Reviewed, UniProtKB/Swiss-Prot A2RIB7 (NAOX_LACLM)

Last modified November 25, 2008. Version 18. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    NADH oxidase
      Short name=NOXase
    EC=1.6.99.3

Gene names

Name:	noxE
Ordered Locus Names:	llmg_0408

Organism

Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	NADH + acceptor = NAD(+) + reduced acceptor.
Cofactor	Binds 1 FAD per subunit.
Enzyme regulation	Inhibited by hydrogen peroxide, sulfhydryl reagents and quinine, but not by EDTA.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: K_M=4.1 µM for beta-NADH (in the presence of oxygen) V_max=83 µmol/min/mg enzyme 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.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Oxidation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

446

NADH oxidase

PRO_0000292941

Regions

Nucleotide binding

5

FAD By similarity

Nucleotide binding

4

FAD By similarity

Sites

Active site

1

Proton acceptor By similarity

Active site

1

Redox-active By similarity

Binding site

1

FAD By similarity

Binding site

1

NAD; via amide nitrogen By similarity

Binding site

1

NAD By similarity

Binding site

1

NAD By similarity

Binding site

1

NAD; via amide nitrogen By similarity

Binding site

1

FAD By similarity

Binding site

1

NAD; via carbonyl oxygen By similarity

Binding site

1

FAD; via amide nitrogen By similarity

Binding site

1

NAD; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

1

Cysteine sulfenic acid (-SOH) By similarity

Experimental info

Sequence conflict

1

A → AA AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

A2RIB7-1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 1B1FA2FE313D6C03
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446

48,872

        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

References

	« Hide 'large scale' referencesShow '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: 11932446] [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: 17307855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: IND23261759] Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases
	AY046926 Genomic DNA. Translation: AAL02357.1. AM406671 Genomic DNA. Translation: CAL97012.1.
RefSeq	YP_001031758.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4796799.
GenomeReviews	Gene locus llmg_0408 in contig AM406671_GR.
KEGG	llm:llmg_0408.
Organism-specific databases
CMR	Search...
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 2 hits. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00411. PNDRDTASEI.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

NAOX_LACLM

Accession

Primary (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:	November 25, 2008
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents