A0A101MCA0 · A0A101MCA0_PENFR
- ProteinCopper-containing nitrite reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids367 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H+ + nitrite
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 124 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 129 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 164 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 165 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 173 | Cu cation 2 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 178 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M | ||||||
Binding site | 327 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | copper ion binding | |
Molecular Function | nitrite reductase (NO-forming) activity |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCopper-containing nitrite reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A101MCA0
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Disordered | ||||
Sequence: MDSAKTEKARGSDPTLTPQANEVSQLHS | ||||||
Compositional bias | 10-28 | Polar residues | ||||
Sequence: RGSDPTLTPQANEVSQLHS | ||||||
Domain | 85-187 | Plastocyanin-like | ||||
Sequence: QYKYEQWDFNGTVPGPFIRARVGDVVELSLTNRDETGNPHNIDCHAFLGPGGGSALTTAEEGQTKTARFRLHCPGLYVYHCAAAPVPVHIANGMYGLMYVQPA |
Sequence similarities
Belongs to the multicopper oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length367
- Mass (Da)39,944
- Last updated2016-04-13 v1
- Checksum7FA5464FF2F30FFC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 10-28 | Polar residues | ||||
Sequence: RGSDPTLTPQANEVSQLHS |
Keywords
- Technical term