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UniProtKB/Swiss-Prot entry P37062

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NAPE_ENTFA
Primary accession number P37062
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on April 23, 2003 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 77)
Name and origin of the protein
Protein name NADH peroxidase
Synonyms NPXase
Npx
EC 1.11.1.1
Gene name
Name: npr
OrderedLocusNames: EF_1211
From
Enterococcus faecalis (Streptococcus faecalis) [TaxID: 1351] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661;
DOI=10.1016/0022-2836(91)80180-3; PubMed=1719212 [NCBI, ExPASy, EBI, Israel, Japan]
Ross R.P., Claiborne A.;
"Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases.";
J. Mol. Biol. 221:857-871(1991).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=V583 / ATCC 700802;
DOI=10.1126/science.1080613; PubMed=12663927 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis.";
Science 299:2071-2074(2003).
[3]
 PROTEIN SEQUENCE OF 1-51.
STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661;
PubMed=2501302 [NCBI, ExPASy, EBI, Israel, Japan]
Poole L.B., Claiborne A.;
"The non-flavin redox center of the streptococcal NADH peroxidase. I. Thiol reactivity and redox behavior in the presence of urea.";
J. Biol. Chem. 264:12322-12329(1989).
[4]
 X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).
STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661;
PubMed=1942054 [NCBI, ExPASy, EBI, Israel, Japan]
Stehle T., Ahmed S.A., Claiborne A., Schulz G.E.;
"Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16-A resolution.";
J. Mol. Biol. 221:1325-1344(1991).
[5]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND FAD.
STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661;
PubMed=8425532 [NCBI, ExPASy, EBI, Israel, Japan]
Stehle T., Claiborne A., Schulz G.E.;
"NADH binding site and catalysis of NADH peroxidase.";
Eur. J. Biochem. 211:221-226(1993).
[6]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, AND ACTIVE SITE.
STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661;
DOI=10.1021/bi961037s; PubMed=8756456 [NCBI, ExPASy, EBI, Israel, Japan]
Yeh J.I., Claiborne A., Hol W.G.J.;
"Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8-A resolution.";
Biochemistry 35:9951-9957(1996).
[7]
 STRUCTURE BY NMR.
STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661;
DOI=10.1021/bi9707990; PubMed=9214307 [NCBI, ExPASy, EBI, Israel, Japan]
Crane E.J. III, Vervoort J., Clairborne A.;
"13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase.";
Biochemistry 36:8611-8618(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X62755; CAA44611.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE016830; AAO81008.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S18332; S18332.
RefSeq NP_814938.1; -.
3D structure databases
PDB
1F8W; X-ray; 2.45 A; A=1-447.[ExPASy / RCSB / EBI]
1JOA; X-ray; 2.80 A; A=1-447.[ExPASy / RCSB / EBI]
1NHP; X-ray; 2.00 A; A=1-447.[ExPASy / RCSB / EBI]
1NHQ; X-ray; 2.00 A; A=1-447.[ExPASy / RCSB / EBI]
1NHR; X-ray; 2.10 A; A=1-447.[ExPASy / RCSB / EBI]
1NHS; X-ray; 2.00 A; A=1-447.[ExPASy / RCSB / EBI]
1NPX; X-ray; 2.16 A; A=1-447.[ExPASy / RCSB / EBI]
2NPX; X-ray; 2.40 A; A=1-447.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F8W; -.
1JOA; -.
1NHP; -.
1NHQ; -.
1NHR; -.
1NHS; -.
1NPX; -.
2NPX; -.
ModBase P37062.
Protein family/group databases
PeroxiBase 4010; EfNadPrx01.
Enzyme and pathway databases
BioCyc EFAE226185:EF_1211-MON; -.
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 of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 2.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS P37062.
Genome annotation databases
GeneID 1200111; -.
GenomeReviews AE016830_GR; EF_1211.
KEGG efa:EF1211; -.
NMPDR fig|226185.1.peg.1123; -.
TIGR EF_1211; -.
Phylogenomic databases
HOGENOM P37062; -.
Other
LinkHub P37062; -.
ProtoNet P37062.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   447  447     NADH peroxidase. PRO_0000184705
NP_BIND   7    11  5     FAD. 
NP_BIND   110   113  4     FAD. 
ACT_SITE   10    10        Proton acceptor. 
ACT_SITE   42    42        Redox-active. 
BINDING   32    32        FAD. 
BINDING   42    42        FAD. 
BINDING   132   132        FAD. 
BINDING   160   160        NAD; via amide nitrogen. 
BINDING   179   179        NAD. 
BINDING   188   188        NAD. 
BINDING   243   243        NAD; via amide nitrogen. 
BINDING   281   281        FAD. 
BINDING   297   297        NAD; via carbonyl oxygen. 
BINDING   299   299        FAD; via amide nitrogen. 
BINDING   328   328        NAD; via carbonyl oxygen. 
MOD_RES   42    42        Cysteine sulfenic acid (-SOH). 
CONFLICT   226   226        I -> V (in Ref. 1; CAA44611). 
STRAND   2     6  5      
HELIX   10    22  13      
STRAND   26    31  6      
STRAND   33    39  7      
HELIX   41    43  3      
HELIX   44    48  5      
HELIX   55    57  3      
STRAND   58    60  3      
HELIX   63    67  5      
TURN   68    70  3      
STRAND   71    74  4      
STRAND   77    83  7      
TURN   84    87  4      
STRAND   88    93  6      
TURN   94    96  3      
STRAND   99   103  5      
STRAND   105   109  5      
STRAND   113   115  3      
TURN   121   124  4      
STRAND   125   129  5      
HELIX   133   144  12      
STRAND   151   155  5      
HELIX   159   170  12      
STRAND   174   178  5      
STRAND   180   183  4      
TURN   184   188  5      
HELIX   191   202  12      
TURN   203   205  3      
STRAND   206   209  4      
STRAND   214   218  5      
STRAND   220   222  3      
STRAND   225   230  6      
STRAND   232   234  3      
STRAND   236   240  5      
STRAND   244   247  4      
HELIX   249   251  3      
STRAND   276   278  3      
STRAND   285   287  3      
HELIX   288   290  3      
STRAND   292   294  3      
HELIX   299   311  13      
STRAND   313   315  3      
STRAND   327   331  5      
STRAND   334   340  7      
HELIX   343   349  7      
STRAND   354   363  10      
STRAND   372   379  8      
TURN   381   383  3      
STRAND   385   395  11      
HELIX   400   409  10      
HELIX   414   418  5      
TURN   426   428  3      
HELIX   434   445  12      
Sequence information
Length: 447 AA [This is the length of the unprocessed precursor] Molecular weight: 49566 Da [This is the MW of the unprocessed precursor] CRC64: 3FAF85AF5BB2A70B [This is a checksum on the sequence] 
        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
P37062 in FASTA format

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