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Protein

NADH peroxidase

Gene

npr

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei10Proton acceptor1 Publication1
Binding sitei32FAD2 Publications1
Active sitei42Redox-active1 Publication1
Binding sitei42FAD2 Publications1
Binding sitei132FAD2 Publications1
Binding sitei160NAD; via amide nitrogen1 Publication1
Binding sitei179NAD1 Publication1
Binding sitei188NAD1 Publication1
Binding sitei243NAD; via amide nitrogen1 Publication1
Binding sitei281FAD2 Publications1
Binding sitei297NAD; via carbonyl oxygen1 Publication1
Binding sitei299FAD; via amide nitrogen2 Publications1
Binding sitei328NAD; via carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 11FAD2 Publications5
Nucleotide bindingi110 – 113FAD2 Publications4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BRENDAi1.11.1.1. 2095.
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
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001847051 – 447NADH peroxidaseAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42Cysteine sulfenic acid (-SOH)1 Publication1

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi226185.EF1211.

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 22Combined sources13
Beta strandi26 – 39Combined sources14
Helixi41 – 43Combined sources3
Helixi44 – 48Combined sources5
Helixi55 – 57Combined sources3
Beta strandi58 – 60Combined sources3
Helixi63 – 68Combined sources6
Beta strandi72 – 75Combined sources4
Beta strandi77 – 83Combined sources7
Turni84 – 87Combined sources4
Beta strandi88 – 93Combined sources6
Turni94 – 96Combined sources3
Beta strandi99 – 103Combined sources5
Beta strandi105 – 109Combined sources5
Beta strandi113 – 115Combined sources3
Turni121 – 124Combined sources4
Beta strandi125 – 129Combined sources5
Helixi133 – 144Combined sources12
Beta strandi151 – 155Combined sources5
Helixi159 – 170Combined sources12
Beta strandi174 – 183Combined sources10
Turni184 – 188Combined sources5
Helixi191 – 202Combined sources12
Turni203 – 205Combined sources3
Beta strandi206 – 211Combined sources6
Beta strandi214 – 218Combined sources5
Beta strandi220 – 222Combined sources3
Beta strandi225 – 230Combined sources6
Beta strandi232 – 234Combined sources3
Beta strandi236 – 240Combined sources5
Beta strandi244 – 247Combined sources4
Helixi249 – 251Combined sources3
Turni252 – 254Combined sources3
Beta strandi276 – 278Combined sources3
Helixi280 – 282Combined sources3
Beta strandi285 – 287Combined sources3
Turni288 – 291Combined sources4
Beta strandi292 – 294Combined sources3
Helixi299 – 311Combined sources13
Beta strandi313 – 315Combined sources3
Beta strandi327 – 331Combined sources5
Beta strandi334 – 340Combined sources7
Helixi343 – 349Combined sources7
Beta strandi354 – 363Combined sources10
Beta strandi372 – 379Combined sources8
Turni381 – 383Combined sources3
Beta strandi385 – 395Combined sources11
Helixi400 – 409Combined sources10
Helixi414 – 418Combined sources5
Turni426 – 428Combined sources3
Helixi434 – 445Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37062.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QMW. Bacteria.
COG0446. LUCA.
KOiK05910.
OMAiQWSLLNL.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. 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)DescriptionActionsGraphical viewLength
Sequence conflicti226I → V in CAA44611 (PubMed:1719212).Curated1

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.
WP_002379347.1. NZ_KE136528.1.

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.
PIRiS18332.
RefSeqiNP_814938.1. NC_004668.1.
WP_002379347.1. NZ_KE136528.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF1211.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protein family/group databases

PeroxiBasei4010. EfNadPrx01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107QMW. Bacteria.
COG0446. LUCA.
KOiK05910.
OMAiQWSLLNL.

Enzyme and pathway databases

BRENDAi1.11.1.1. 2095.
SABIO-RKP37062.

Miscellaneous databases

EvolutionaryTraceiP37062.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 133 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.