Q9I609 · NIRN_PSEAE
- ProteinDihydro-heme d1 dehydrogenase
- GenenirN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids493 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in heme d1 biosynthesis (PubMed:25204657, PubMed:8982003).
Catalyzes the introduction of a double bond into the propionate side chain of pyrrole ring D of dihydro-heme d1, therefore converting dihydro-heme d1 to heme d1 (PubMed:25204657).
Catalyzes the introduction of a double bond into the propionate side chain of pyrrole ring D of dihydro-heme d1, therefore converting dihydro-heme d1 to heme d1 (PubMed:25204657).
Catalytic activity
- A + dihydro-heme d1 = AH2 + heme d1This reaction proceeds in the forward direction.
Cofactor
Pathway
Porphyrin-containing compound metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 31 | heme c (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 34 | heme c (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 35 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 68 | heme c (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 73 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: M | ||||||
Binding site | 165 | Fe (UniProtKB | ChEBI) of heme d1 (UniProtKB | ChEBI); proximal binding residue | ||||
Sequence: H | ||||||
Binding site | 167 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 169 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 182 | heme c (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 182 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 207 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 208 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 341 | Fe (UniProtKB | ChEBI) of heme d1 (UniProtKB | ChEBI); distal binding residue | ||||
Sequence: H | ||||||
Binding site | 390 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 435 | heme d1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | electron transfer activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | heme biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydro-heme d1 dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9I609
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
The mutant exhibits decreased dissimilatory nitrite reductase (NIR) activity (PubMed:8982003).
In the absence of this gene, the formation of the acrylic double bond of heme d1 does not take place and dihydro-heme d1 is inserted into the nitrite reductase NirS (PubMed:25204657).
In the absence of this gene, the formation of the acrylic double bond of heme d1 does not take place and dihydro-heme d1 is inserted into the nitrite reductase NirS (PubMed:25204657).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 165 | Abolishes heme d1 binding. Loss of activity. | ||||
Sequence: H → A or Q | ||||||
Mutagenesis | 341 | Still able to bind heme d1 but lacks catalytic activity. | ||||
Sequence: H → A or Q | ||||||
Mutagenesis | 435 | Decreases both heme d1 binding and turnover. | ||||
Sequence: H → A | ||||||
Mutagenesis | 435 | Does not affect heme d1 binding but decreases catalytic activity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 479 | Still able to bind heme d1 but lacks catalytic activity. | ||||
Sequence: Y → F |
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MRLIGLALGLLLGALAQA | ||||||
Chain | PRO_5004327132 | 19-493 | Dihydro-heme d1 dehydrogenase | |||
Sequence: GEAPGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQLDDAAADALVAYLYQAPPREPQWSAEDIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVFATPNISRGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGKYNVGNKIGYAEGTSH |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-96 | Cytochrome c | ||||
Sequence: GEAPGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQLDDAAADALVAYLYQAP | ||||||
Region | 114-468 | D1-heme domain | ||||
Sequence: PHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVFATPNISRGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVK |
Domain
Consists of an N-terminal domain that binds the heme c cofactor, followed by a long linker segment, and a C-terminal region that exhibits an eight-bladed heme d1-binding beta-propeller domain.
Sequence similarities
Belongs to the cytochrome c family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length493
- Mass (Da)53,978
- Last updated2001-03-01 v1
- Checksum8E11E64DF8B637A4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 214 | in Ref. 1; BAA12683 | ||||
Sequence: D → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D84475 EMBL· GenBank· DDBJ | BAA12683.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG03898.1 EMBL· GenBank· DDBJ | Genomic DNA |