Reviewed,
UniProtKB/Swiss-Prot Q5XC60 (NAOX_STRP6)
Last modified
November 25, 2008.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable NADH oxidase Short name=NOXase EC=1.6.99.3 | ||
| Gene names |
| ||
| Organism | Streptococcus pyogenes serotype M6 [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 301450 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 456 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the four-electron reduction of molecular oxygen to water By similarity. |
| Catalytic activity | NADH + acceptor = NAD(+) + reduced acceptor. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Miscellaneous | The active site is the redox-active Cys-44 oxidized to Cys-SOH. The oxidized form is stabilized by an hydrogen bond formation with His-11 By similarity. |
| Sequence similarities | Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family. |
| Mass spectrometry | Molecular weight is 49603.57 Da from positions 1 - 456. Determined by ESI. Ref.2 |
Ontologies
Keywords | |
|---|---|
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| PTM | Oxidation |
| Technical term | Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 456 | 456 | Probable NADH oxidase | PRO_0000259672 | |||||
Regions | |||||||||
| Nucleotide binding | 8 – 12 | 5 | FAD By similarity | ||||||
| Nucleotide binding | 110 – 113 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 163 – 178 | 16 | NAD By similarity | ||||||
| Nucleotide binding | 282 – 292 | 11 | FAD By similarity | ||||||
Sites | |||||||||
| Active site | 11 | 1 | Proton acceptor By similarity | ||||||
| Active site | 44 | 1 | Redox-active By similarity | ||||||
| Binding site | 44 | 1 | FAD By similarity | ||||||
| Binding site | 171 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 190 | 1 | NAD By similarity | ||||||
| Binding site | 199 | 1 | NAD By similarity | ||||||
| Binding site | 254 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 292 | 1 | FAD By similarity | ||||||
| Binding site | 308 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 310 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 339 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 44 | 1 | Cysteine sulfenic acid (-SOH) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 177 | 1 | E → V AA sequence Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain." Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M. J. Infect. Dis. 190:727-738(2004) [PubMed: 15272401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-946 / MGAS10394 / Serotype M6. |
| [2] | "Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins." Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A. Submitted (MAY-2000) to UniProtKB Cited for: PROTEIN SEQUENCE OF 75-89; 107-121; 127-143; 163-181 AND 303-315, MASS SPECTROMETRY. Strain: JRS4 / Serotype M6. |
Cross-references
Sequence databases | |
|---|---|
| CP000003 Genomic DNA. Translation: AAT87003.1. | |
| RefSeq | YP_060186.1. |
3D structure databases | |
| SMR | Q5XC60. Positions 2-456. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2941962. |
| GenomeReviews | Gene locus M6_Spy0868 in contig CP000003_GR. |
| KEGG | spa:M6_Spy0868. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q5XC60. |
Enzyme and pathway databases | |
| BioCyc | SPYO286636:M6_SPY0868-MON. |
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] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00411. PNDRDTASEI. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | NAOX_STRP6 | ||||||||
| Accession | Primary (citable) accession number: Q5XC60 Secondary accession number(s): P82571 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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