Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P37062

- NAPE_ENTFA

UniProt

P37062 - NAPE_ENTFA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NADH peroxidase

Gene

npr

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

NADH + H2O2 = NAD+ + 2 H2O.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Proton acceptor1 Publication
Binding sitei32 – 321FAD2 Publications
Active sitei42 – 421Redox-active1 Publication
Binding sitei42 – 421FAD2 Publications
Binding sitei132 – 1321FAD2 Publications
Binding sitei160 – 1601NAD; via amide nitrogen1 Publication
Binding sitei179 – 1791NAD1 Publication
Binding sitei188 – 1881NAD1 Publication
Binding sitei243 – 2431NAD; via amide nitrogen1 Publication
Binding sitei281 – 2811FAD2 Publications
Binding sitei297 – 2971NAD; via carbonyl oxygen1 Publication
Binding sitei299 – 2991FAD; via amide nitrogen2 Publications
Binding sitei328 – 3281NAD; via carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 115FAD2 Publications
Nucleotide bindingi110 – 1134FAD2 Publications

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. NADH peroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-1199-MONOMER.
SABIO-RKP37062.

Protein family/group databases

PeroxiBasei4010. EfNadPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH peroxidase (EC:1.11.1.1)
Short name:
NPXase
Short name:
Npx
Gene namesi
Name:npr
Ordered Locus Names:EF_1211
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
ProteomesiUP000001415: Chromosome

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447NADH peroxidasePRO_0000184705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Cysteine sulfenic acid (-SOH)1 Publication

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi226185.EF1211.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 2213Combined sources
Beta strandi26 – 3914Combined sources
Helixi41 – 433Combined sources
Helixi44 – 485Combined sources
Helixi55 – 573Combined sources
Beta strandi58 – 603Combined sources
Helixi63 – 686Combined sources
Beta strandi72 – 754Combined sources
Beta strandi77 – 837Combined sources
Turni84 – 874Combined sources
Beta strandi88 – 936Combined sources
Turni94 – 963Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi113 – 1153Combined sources
Turni121 – 1244Combined sources
Beta strandi125 – 1295Combined sources
Helixi133 – 14412Combined sources
Beta strandi151 – 1555Combined sources
Helixi159 – 17012Combined sources
Beta strandi174 – 18310Combined sources
Turni184 – 1885Combined sources
Helixi191 – 20212Combined sources
Turni203 – 2053Combined sources
Beta strandi206 – 2116Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi244 – 2474Combined sources
Helixi249 – 2513Combined sources
Turni252 – 2543Combined sources
Beta strandi276 – 2783Combined sources
Helixi280 – 2823Combined sources
Beta strandi285 – 2873Combined sources
Turni288 – 2914Combined sources
Beta strandi292 – 2943Combined sources
Helixi299 – 31113Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi327 – 3315Combined sources
Beta strandi334 – 3407Combined sources
Helixi343 – 3497Combined sources
Beta strandi354 – 36310Combined sources
Beta strandi372 – 3798Combined sources
Turni381 – 3833Combined sources
Beta strandi385 – 39511Combined sources
Helixi400 – 40910Combined sources
Helixi414 – 4185Combined sources
Turni426 – 4283Combined sources
Helixi434 – 44512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP37062.
SMRiP37062. Positions 1-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37062.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0446.
KOiK05910.
OMAiMSCGMEL.
OrthoDBiEOG6QVRCJ.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. 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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

P37062-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKVIVLGSSH GGYEAVEELL NLHPDAEIQW YEKGDFISFL SCGMQLYLEG
60 70 80 90 100
KVKDVNSVRY MTGEKMESRG VNVFSNTEIT AIQPKEHQVT VKDLVSGEER
110 120 130 140 150
VENYDKLIIS PGAVPFELDI PGKDLDNIYL MRGRQWAIKL KQKTVDPEVN
160 170 180 190 200
NVVVIGSGYI GIEAAEAFAK AGKKVTVIDI LDRPLGVYLD KEFTDVLTEE
210 220 230 240 250
MEANNITIAT GETVERYEGD GRVQKIVTDK NAYDADLVVV AVGVRPNTAW
260 270 280 290 300
LKGTLELHPN GLIKTDEYMR TSEPDVFAVG DATLIKYNPA DTEVNIALAT
310 320 330 340 350
NARKQGRFAV KNLEEPVKPF PGVQGSSGLA VFDYKFASTG INEVMAQKLG
360 370 380 390 400
KETKAVTVVE DYLMDFNPDK QKAWFKLVYD PETTQILGAQ LMSKADLTAN
410 420 430 440
INAISLAIQA KMTIEDLAYA DFFFQPAFDK PWNIINTAAL EAVKQER
Length:447
Mass (Da):49,566
Last modified:April 23, 2003 - v2
Checksum:i3FAF85AF5BB2A70B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261I → V in CAA44611. (PubMed:1719212)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62755 Genomic DNA. Translation: CAA44611.1.
AE016830 Genomic DNA. Translation: AAO81008.1.
PIRiS18332.
RefSeqiNP_814938.1. NC_004668.1.

Genome annotation databases

EnsemblBacteriaiAAO81008; AAO81008; EF_1211.
GeneIDi1200111.
KEGGiefa:EF1211.
PATRICi21852806. VBIEntFae7065_1134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62755 Genomic DNA. Translation: CAA44611.1 .
AE016830 Genomic DNA. Translation: AAO81008.1 .
PIRi S18332.
RefSeqi NP_814938.1. NC_004668.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F8W X-ray 2.45 A 1-447 [» ]
1JOA X-ray 2.80 A 1-447 [» ]
1NHP X-ray 2.00 A 1-447 [» ]
1NHQ X-ray 2.00 A 1-447 [» ]
1NHR X-ray 2.10 A 1-447 [» ]
1NHS X-ray 2.00 A 1-447 [» ]
1NPX X-ray 2.16 A 1-447 [» ]
2NPX X-ray 2.40 A 1-447 [» ]
ProteinModelPortali P37062.
SMRi P37062. Positions 1-447.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 226185.EF1211.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

Protein family/group databases

PeroxiBasei 4010. EfNadPrx01.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO81008 ; AAO81008 ; EF_1211 .
GeneIDi 1200111.
KEGGi efa:EF1211.
PATRICi 21852806. VBIEntFae7065_1134.

Phylogenomic databases

eggNOGi COG0446.
KOi K05910.
OMAi MSCGMEL.
OrthoDBi EOG6QVRCJ.

Enzyme and pathway databases

BioCyci EFAE226185:GHI1-1199-MONOMER.
SABIO-RK P37062.

Miscellaneous databases

EvolutionaryTracei P37062.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, OXIDATION AT CYS-42.
    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.

Entry informationi

Entry nameiNAPE_ENTFA
AccessioniPrimary (citable) accession number: P37062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 23, 2003
Last modified: November 26, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3