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Reviewed, UniProtKB/Swiss-Prot P37061 (NAOX_ENTFA)

Last modified February 9, 2010. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NADH oxidase
      Short name=NOXase
    EC=1.6.99.3
Gene names
Name: nox
Ordered Locus Names: EF_1586
OrganismEnterococcus faecalis (Streptococcus faecalis) [Complete proteome] [HAMAP]
Taxonomic identifier1351 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

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Protein attributes

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

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General annotation (Comments)

Function

Catalyzes the four-electron reduction of molecular oxygen to water.

Catalytic activity

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

The active site is the redox-active Cys-42 oxidized to Cys-SOH. The oxidized form is stabilized by an hydrogen bond formation with His-10.

Sequence similarities

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

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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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

NADH dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446NADH oxidase
PRO_0000184701

Regions

Nucleotide binding7 – 115FAD By similarity
Nucleotide binding110 – 1134FAD By similarity
Nucleotide binding150 – 16516NAD By similarity
Nucleotide binding271 – 28111FAD By similarity

Sites

Active site101Proton acceptor By similarity
Active site421Redox-active Ref.4
Binding site321FAD By similarity
Binding site421FAD By similarity
Binding site1771NAD By similarity
Binding site1861NAD By similarity
Binding site2431NAD; via amide nitrogen By similarity
Binding site2991FAD; via amide nitrogen By similarity
Binding site3281NAD; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue421Cysteine sulfenic acid (-SOH)

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Sequences

Sequence LengthMass (Da)Tools
P37061-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: D0762A47FC3DC071

FASTA44648,915
        10         20         30         40         50         60 
MKVVVVGCTH AGTSAVKSIL ANHPEAEVTV YERNDNISFL SCGIALYVGG VVKNAADLFY 

        70         80         90        100        110        120 
SNPEELASLG ATVKMEHNVE EINVDDKTVT AKNLQTGATE TVSYDKLVMT TGSWPIIPPI 

       130        140        150        160        170        180 
PGIDAENILL CKNYSQANVI IEKAKDAKRV VVVGGGYIGI ELVEAFVESG KQVTLVDGLD 

       190        200        210        220        230        240 
RILNKYLDKP FTDVLEKELV DRGVNLALGE NVQQFVADEQ GKVAKVITPS QEFEADMVIM 

       250        260        270        280        290        300 
CVGFRPNTEL LKDKVDMLPN GAIEVNEYMQ TSNPDIFAAG DSAVVHYNPS QTKNYIPLAT 

       310        320        330        340        350        360 
NAVRQGMLVG RNLTEQKLAY RGTQGTSGLY LFGWKIGSTG VTKESAKLNG LDVEATVFED 

       370        380        390        400        410        420 
NYRPEFMPTT EKVLMELVYE KGTQRIVGGQ LMSKYDITQS ANTLSLAVQN KMTVEDLAIS 

       430        440 
DFFFQPHFDR PWNYLNLLAQ AALENM

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases."
Ross R.P., Claiborne A.
J. Mol. Biol. 227:658-671(1992) [PubMed: 1404382] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661.
[2]"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis."
Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. expand/collapse author list , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.
Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: V583 / ATCC 700802.
[3]"The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers."
Ahmed S.A., Claiborne A.
J. Biol. Chem. 264:19856-19863(1989) [PubMed: 2511195] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-17; 34-52 AND 226-250.
Strain: ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661.
[4]"Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation."
Claiborne A., Miller H., Parsonage D., Ross R.P.
FASEB J. 7:1483-1490(1993) [PubMed: 8262333] [Abstract]
Cited for: ACTIVE SITE.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X68847 Genomic DNA. Translation: CAA48728.1.
AE016830 Genomic DNA. Translation: AAO81372.1.
PIRS26965.
RefSeqNP_815302.1.

3D structure databases

SMRP37061. Positions 1-443.
ModBaseSearch...

Protein family/group databases

PeroxiBase5456. EfNadOxd01.

Genome annotation databases

GeneID1200486.
GenomeReviewsGene locus EF_1586 in contig AE016830_GR.
KEGGefa:EF1586.
NMPDRfig|226185.1.peg.1487.
TIGREF_1586.

Phylogenomic databases

HOGENOMHBG535576.
OMAFFFQPHF.

Enzyme and pathway databases

BRENDA1.6.99.3. 704.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProtoNetSearch...

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Entry information

Entry nameNAOX_ENTFA
AccessionPrimary (citable) accession number: P37061
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 9, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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