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P37062 (NAPE_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH peroxidase
Short name=NPXase
Short name=Npx
EC=1.11.1.1
Gene names
Name:npr
Ordered Locus Names:EF_1211
OrganismEnterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]
Taxonomic identifier226185 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Enterococcaceae › Enterococcus ›

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Peroxidase whose active site is a redox-active cysteine-sulfenic acid.

Catalytic activity

NADH + H2O2 = NAD+ + 2 H2O.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homotetramer.

Miscellaneous

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447NADH peroxidase
PRO_0000184705

Regions

Nucleotide binding7 – 115FAD
Nucleotide binding110 – 1134FAD

Sites

Active site101Proton acceptor Ref.6
Active site421Redox-active Ref.6
Binding site321FAD
Binding site421FAD
Binding site1321FAD
Binding site1601NAD; via amide nitrogen
Binding site1791NAD
Binding site1881NAD
Binding site2431NAD; via amide nitrogen
Binding site2811FAD
Binding site2971NAD; via carbonyl oxygen
Binding site2991FAD; via amide nitrogen
Binding site3281NAD; via carbonyl oxygen

Amino acid modifications

Modified residue421Cysteine sulfenic acid (-SOH)

Experimental info

Sequence conflict2261I → V in CAA44611. Ref.1

Secondary structure

1 ............................................................................................. 447
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37062 [UniParc].

Last modified April 23, 2003. Version 2.
Checksum: 3FAF85AF5BB2A70B

FASTA44749,566
        10         20         30         40         50         60 
MKVIVLGSSH GGYEAVEELL NLHPDAEIQW YEKGDFISFL SCGMQLYLEG KVKDVNSVRY 

        70         80         90        100        110        120 
MTGEKMESRG VNVFSNTEIT AIQPKEHQVT VKDLVSGEER VENYDKLIIS PGAVPFELDI 

       130        140        150        160        170        180 
PGKDLDNIYL MRGRQWAIKL KQKTVDPEVN NVVVIGSGYI GIEAAEAFAK AGKKVTVIDI 

       190        200        210        220        230        240 
LDRPLGVYLD KEFTDVLTEE MEANNITIAT GETVERYEGD GRVQKIVTDK NAYDADLVVV 

       250        260        270        280        290        300 
AVGVRPNTAW LKGTLELHPN GLIKTDEYMR TSEPDVFAVG DATLIKYNPA DTEVNIALAT 

       310        320        330        340        350        360 
NARKQGRFAV KNLEEPVKPF PGVQGSSGLA VFDYKFASTG INEVMAQKLG KETKAVTVVE 

       370        380        390        400        410        420 
DYLMDFNPDK QKAWFKLVYD PETTQILGAQ LMSKADLTAN INAISLAIQA KMTIEDLAYA 

       430        440 
DFFFQPAFDK PWNIINTAAL EAVKQER

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases."
Ross R.P., Claiborne A.
J. Mol. Biol. 221:857-871(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700802 / V583.
[3]"The non-flavin redox center of the streptococcal NADH peroxidase. I. Thiol reactivity and redox behavior in the presence of urea."
Poole L.B., Claiborne A.
J. Biol. Chem. 264:12322-12329(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-51.
Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
[4]"Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16-A resolution."
Stehle T., Ahmed S.A., Claiborne A., Schulz G.E.
J. Mol. Biol. 221:1325-1344(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).
Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
[5]"NADH binding site and catalysis of NADH peroxidase."
Stehle T., Claiborne A., Schulz G.E.
Eur. J. Biochem. 211:221-226(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND FAD.
Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
[6]"Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8-A resolution."
Yeh J.I., Claiborne A., Hol W.G.J.
Biochemistry 35:9951-9957(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, ACTIVE SITE.
Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
[7]"13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase."
Crane E.J. III, Vervoort J., Clairborne A.
Biochemistry 36:8611-8618(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X62755 Genomic DNA. Translation: CAA44611.1.
AE016830 Genomic DNA. Translation: AAO81008.1.
PIRS18332.
RefSeqNP_814938.1. NC_004668.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8WX-ray2.45A1-447[»]
1JOAX-ray2.80A1-447[»]
1NHPX-ray2.00A1-447[»]
1NHQX-ray2.00A1-447[»]
1NHRX-ray2.10A1-447[»]
1NHSX-ray2.00A1-447[»]
1NPXX-ray2.16A1-447[»]
2NPXX-ray2.40A1-447[»]
ProteinModelPortalP37062.
SMRP37062. Positions 1-447.
ModBaseSearch...

Protein-protein interaction databases

STRING226185.EF1211.

Protein family/group databases

PeroxiBase4010. EfNadPrx01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO81008; AAO81008; EF_1211.
GeneID1200111.
KEGGefa:EF1211.
PATRIC21852806. VBIEntFae7065_1134.

Phylogenomic databases

eggNOGCOG0446.
KOK05910.
OMAFFFQPGF.
ProtClustDBCLSK457900.

Enzyme and pathway databases

BioCycEFAE226185:GHI1-1303-MONOMER.
SABIO-RKP37062.

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. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37062.

Entry information

Entry nameNAPE_ENTFA
AccessionPrimary (citable) accession number: P37062
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 23, 2003
Last modified: May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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