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Protein

NADH oxidase

Gene

nox

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the four-electron reduction of molecular oxygen to water.

Catalytic activityi

NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10Proton acceptorBy similarity1
Binding sitei32FADBy similarity1
Active sitei42Redox-active1 Publication1
Binding sitei42FADBy similarity1
Binding sitei177NADBy similarity1
Binding sitei186NADBy similarity1
Binding sitei243NAD; via amide nitrogenBy similarity1
Binding sitei299FAD; via amide nitrogenBy similarity1
Binding sitei328NAD; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 11FADBy similarity5
Nucleotide bindingi110 – 113FADBy similarity4
Nucleotide bindingi150 – 165NADBy similarityAdd BLAST16
Nucleotide bindingi271 – 281FADBy similarityAdd BLAST11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

SABIO-RKP37061.

Protein family/group databases

PeroxiBasei5456. EfNadOxd01.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH oxidase (EC:1.6.99.3)
Short name:
NOXase
Gene namesi
Name:nox
Ordered Locus Names:EF_1586
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001847011 – 446NADH oxidaseAdd BLAST446

Amino acid modifications

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

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi226185.EF1586.

Structurei

3D structure databases

ProteinModelPortaliP37061.
SMRiP37061.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QMW. Bacteria.
COG0446. LUCA.
OMAiHAYIPLA.

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.

P37061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVVVGCTH AGTSAVKSIL ANHPEAEVTV YERNDNISFL SCGIALYVGG
60 70 80 90 100
VVKNAADLFY SNPEELASLG ATVKMEHNVE EINVDDKTVT AKNLQTGATE
110 120 130 140 150
TVSYDKLVMT TGSWPIIPPI PGIDAENILL CKNYSQANVI IEKAKDAKRV
160 170 180 190 200
VVVGGGYIGI ELVEAFVESG KQVTLVDGLD RILNKYLDKP FTDVLEKELV
210 220 230 240 250
DRGVNLALGE NVQQFVADEQ GKVAKVITPS QEFEADMVIM CVGFRPNTEL
260 270 280 290 300
LKDKVDMLPN GAIEVNEYMQ TSNPDIFAAG DSAVVHYNPS QTKNYIPLAT
310 320 330 340 350
NAVRQGMLVG RNLTEQKLAY RGTQGTSGLY LFGWKIGSTG VTKESAKLNG
360 370 380 390 400
LDVEATVFED NYRPEFMPTT EKVLMELVYE KGTQRIVGGQ LMSKYDITQS
410 420 430 440
ANTLSLAVQN KMTVEDLAIS DFFFQPHFDR PWNYLNLLAQ AALENM
Length:446
Mass (Da):48,915
Last modified:June 1, 1994 - v1
Checksum:iD0762A47FC3DC071
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68847 Genomic DNA. Translation: CAA48728.1.
AE016830 Genomic DNA. Translation: AAO81372.1.
PIRiS26965.
RefSeqiNP_815302.1. NC_004668.1.
WP_002361833.1. NZ_KE136528.1.

Genome annotation databases

EnsemblBacteriaiAAO81372; AAO81372; EF_1586.
GeneIDi1200486.
KEGGiefa:EF1586.
PATRICi21853530. VBIEntFae7065_1491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68847 Genomic DNA. Translation: CAA48728.1.
AE016830 Genomic DNA. Translation: AAO81372.1.
PIRiS26965.
RefSeqiNP_815302.1. NC_004668.1.
WP_002361833.1. NZ_KE136528.1.

3D structure databases

ProteinModelPortaliP37061.
SMRiP37061.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF1586.

Protein family/group databases

PeroxiBasei5456. EfNadOxd01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO81372; AAO81372; EF_1586.
GeneIDi1200486.
KEGGiefa:EF1586.
PATRICi21853530. VBIEntFae7065_1491.

Phylogenomic databases

eggNOGiENOG4107QMW. Bacteria.
COG0446. LUCA.
OMAiHAYIPLA.

Enzyme and pathway databases

SABIO-RKP37061.

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 nameiNAOX_ENTFA
AccessioniPrimary (citable) accession number: P37061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 120 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.