A0A0A1Z321 · A0A0A1Z321_PSEFL
- ProteinFlavohemoprotein
- Genehmp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids393 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
Catalytic activity
- 2 nitric oxide + NADH + 2 O2 = 2 nitrate + NAD+ + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 29 | Involved in heme-bound ligand stabilization and O-O bond activation | |||
Site | 84 | Influences the redox potential of the prosthetic heme and FAD groups | |||
Binding site | 85 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue | |||
Active site | 95 | Charge relay system | |||
Active site | 138 | Charge relay system | |||
Binding site | 191 | FAD (UniProtKB | ChEBI) | |||
Binding site | 205-208 | FAD (UniProtKB | ChEBI) | |||
Binding site | 268-273 | NADP+ (UniProtKB | ChEBI) | |||
Site | 383 | Influences the redox potential of the prosthetic heme and FAD groups | |||
Binding site | 384-387 | FAD (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | nitric oxide dioxygenase NAD(P)H activity | |
Molecular Function | oxygen binding | |
Molecular Function | oxygen carrier activity | |
Biological Process | cellular response to nitrosative stress | |
Biological Process | nitric oxide catabolic process | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameFlavohemoprotein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A0A1Z321
Proteomes
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-136 | Globin | |||
Region | 150-393 | Reductase | |||
Domain | 153-256 | FAD-binding FR-type | |||
Domain
Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Sequence similarities
Belongs to the globin family. Two-domain flavohemoproteins subfamily.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)43,356
- Last updated2015-02-04 v1
- ChecksumDA1802CE3739D279
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ASGY01000085 EMBL· GenBank· DDBJ | KGE67619.1 EMBL· GenBank· DDBJ | Genomic DNA |