[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

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

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; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0016692;	Molecular function: NADH peroxidase activity (inferred from electronic annotation from EC).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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]

ProtoNet

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; -.

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

Feature table viewer

`Key`	`From 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

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools