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P37061

- NAOX_ENTFA

UniProt

P37061 - NAOX_ENTFA

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Protein

NADH oxidase

Gene

nox

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Proton acceptorBy similarity
Binding sitei32 – 321FADBy similarity
Active sitei42 – 421Redox-active1 Publication
Binding sitei42 – 421FADBy similarity
Binding sitei177 – 1771NADBy similarity
Binding sitei186 – 1861NADBy similarity
Binding sitei243 – 2431NAD; via amide nitrogenBy similarity
Binding sitei299 – 2991FAD; via amide nitrogenBy similarity
Binding sitei328 – 3281NAD; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 115FADBy similarity
Nucleotide bindingi110 – 1134FADBy similarity
Nucleotide bindingi150 – 16516NADBy similarityAdd
BLAST
Nucleotide bindingi271 – 28111FADBy similarityAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-1572-MONOMER.
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
ProteomesiUP000001415: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446NADH oxidasePRO_0000184701Add
BLAST

Amino acid modifications

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

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. Positions 1-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0446.
OMAiHAYIPLA.
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. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. 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 .
PIRi S26965.
RefSeqi NP_815302.1. NC_004668.1.
WP_002361833.1. NZ_KE136528.1.

3D structure databases

ProteinModelPortali P37061.
SMRi P37061. Positions 1-443.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 226185.EF1586.

Protein family/group databases

PeroxiBasei 5456. EfNadOxd01.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO81372 ; AAO81372 ; EF_1586 .
GeneIDi 1200486.
KEGGi efa:EF1586.
PATRICi 21853530. VBIEntFae7065_1491.

Phylogenomic databases

eggNOGi COG0446.
OMAi HAYIPLA.
OrthoDBi EOG6QVRCJ.

Enzyme and pathway databases

BioCyci EFAE226185:GHI1-1572-MONOMER.
SABIO-RK P37061.

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. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases."
    Ross R.P., Claiborne A.
    J. Mol. Biol. 227:658-671(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700802 / V583.
  3. "The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers."
    Ahmed S.A., Claiborne A.
    J. Biol. Chem. 264:19856-19863(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-17; 34-52 AND 226-250.
    Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
  4. "Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation."
    Claiborne A., Miller H., Parsonage D., Ross R.P.
    FASEB J. 7:1483-1490(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, OXIDATION AT CYS-42.

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 26, 2014
This is version 110 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

External Data

Dasty 3