Q9I609 · NIRN_PSEAE

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).

Catalytic activity

Cofactor

heme c (UniProtKB | Rhea| CHEBI:61717 )

Pathway

Porphyrin-containing compound metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site31heme c (UniProtKB | ChEBI); covalent
Binding site34heme c (UniProtKB | ChEBI); covalent
Binding site35Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue
Binding site68heme c (UniProtKB | ChEBI)
Binding site73Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue
Binding site165Fe (UniProtKB | ChEBI) of heme d1 (UniProtKB | ChEBI); proximal binding residue
Binding site167heme d1 (UniProtKB | ChEBI)
Binding site169heme d1 (UniProtKB | ChEBI)
Binding site182heme c (UniProtKB | ChEBI)
Binding site182heme d1 (UniProtKB | ChEBI)
Binding site207heme d1 (UniProtKB | ChEBI)
Binding site208heme d1 (UniProtKB | ChEBI)
Binding site341Fe (UniProtKB | ChEBI) of heme d1 (UniProtKB | ChEBI); distal binding residue
Binding site390heme d1 (UniProtKB | ChEBI)
Binding site435heme d1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentperiplasmic space
Molecular Functionelectron transfer activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity
Biological Processheme biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydro-heme d1 dehydrogenase
  • EC number

Gene names

    • Name
      nirN
    • Ordered locus names
      PA0509

Organism names

Accessions

  • Primary accession
    Q9I609
  • Secondary accessions
    • P95418

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis165Abolishes heme d1 binding. Loss of activity.
Mutagenesis341Still able to bind heme d1 but lacks catalytic activity.
Mutagenesis435Decreases both heme d1 binding and turnover.
Mutagenesis435Does not affect heme d1 binding but decreases catalytic activity.
Mutagenesis479Still able to bind heme d1 but lacks catalytic activity.

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_500432713219-493Dihydro-heme d1 dehydrogenase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain19-96Cytochrome c
Region114-468D1-heme domain

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    493
  • Mass (Da)
    53,978
  • Last updated
    2001-03-01 v1
  • Checksum
    8E11E64DF8B637A4
MRLIGLALGLLLGALAQAGEAPGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQLDDAAADALVAYLYQAPPREPQWSAEDIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVFATPNISRGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGKYNVGNKIGYAEGTSH

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict214in Ref. 1; BAA12683

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D84475
EMBL· GenBank· DDBJ
BAA12683.1
EMBL· GenBank· DDBJ
Genomic DNA
AE004091
EMBL· GenBank· DDBJ
AAG03898.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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