A0A0C4WWL5 · A0A0C4WWL5_9GAMM

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

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site29Involved in heme-bound ligand stabilization and O-O bond activation
Site84Influences the redox potential of the prosthetic heme and FAD groups
Binding site85Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue
Active site95Charge relay system
Active site138Charge relay system
Binding site191FAD (UniProtKB | ChEBI)
Binding site205-208FAD (UniProtKB | ChEBI)
Binding site268-273NADP+ (UniProtKB | ChEBI)
Site383Influences the redox potential of the prosthetic heme and FAD groups
Binding site384-387FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionFAD binding
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionnitric oxide dioxygenase NAD(P)H activity
Molecular Functionoxygen binding
Molecular Functionoxygen carrier activity
Biological Processresponse to nitrosative stress
Biological Processresponse to toxic substance

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Flavohemoprotein
  • Alternative names
    • Flavohemoglobin
    • Hemoglobin-like protein
    • Nitric oxide dioxygenase
      (NO oxygenase
      ; NOD
      ) (EC:1.14.12.17
      ) . EC:1.14.12.17 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      hmp
    • ORF names
      Achr_39510

Organism names

Accessions

  • Primary accession
    A0A0C4WWL5

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-135Globin
Region150-393Reductase
Domain153-256FAD-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 status
    Complete
  • Length
    393
  • Mass (Da)
    43,214
  • Last updated
    2015-04-29 v1
  • Checksum
    A0BEE1F80559AB17
MLTEQQRAIVKATVPLLETGGEALTRHFYGIMLTEYPEVRPLFNQAHQASGEQPRALANAVLMYARHIDRLEALGPLVGQIVNKHVSLQVLPEHYPIVGTCLLRAIREVLGAEIATDAVLDAWGAAYGMLAGLLIGAEEAAYAANAAAPGGWRGARTFRVARRVVESEEIVSFHLRPEDGGVLPAFQPGQYIGLRLLLDGEEVRRNYSLSAAPNGEEYRISVKRHAEGRVSRHLHEQVREGDRLELYPPAGEFVLDASDKPLVLIGAGVGITPLLAMLEAALPAGRPVRFIHCARHGGVQAFRQQVEALAARHPQLKPFFCYSEPRAGDRADASGRLDAERLAAWLPAERNLEAYFLGPKPFMAQVKRQLRELGVPQEQCHYEFFGPAQALEN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010415
EMBL· GenBank· DDBJ
AJE23337.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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