A0A069PWB7 · A0A069PWB7_9BURK

  • Protein
    Flavohemoprotein
  • Gene
    hmp
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
Site31Involved in heme-bound ligand stabilization and O-O bond activation
Site86Influences the redox potential of the prosthetic heme and FAD groups
Binding site87Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue
Active site97Charge relay system
Active site139Charge relay system
Binding site187FAD (UniProtKB | ChEBI)
Binding site272-277NADP+ (UniProtKB | ChEBI)
Site392Influences the redox potential of the prosthetic heme and FAD groups
Binding site393-396FAD (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 Processcellular response to nitrosative stress
Biological Processnitric oxide catabolic process
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
      BG61_00595

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 50014
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia

Accessions

  • Primary accession
    A0A069PWB7

Proteomes

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain6-136Globin
Region148-400Reductase
Domain149-259FAD-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    400
  • Mass (Da)
    42,869
  • Last updated
    2014-10-01 v1
  • Checksum
    05530302920C86DE
MTALTADQIARVKATAPVLAEHGANITKHFYKRMFAHHPELKNLFNQAHQQSGGQPEALARAVYAYAANIDNLGVLGGAVTHIANKHASLNIRAEHYPIVGENLLASISEVLGDAVDPATLDAWAAAYGQLAGILIGAEQNLYDGAAWSGFRPFVVMRKEMESDEITSFYLKPSDGGKVCDFTPGQYVSVKRFVKAIGVDQPRQYTLSDAPNGQWLRISVKRERPANVPAGHISNGLHDGVEAGSIVEVSAPMGEFTLDRAKTTPVVLISGGVGITPMVSMLASLAGEGSARPVAFVHACRHGRVHAFRQWVNEIVAARPNVSRTVFYEAAGGEDRQGVDFDLVGRMDLSKVAGKVLLPDADYYVCGPVEFMRAQQQALIASGVDAARIHTEVFGSGGLE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JFHC01000001
EMBL· GenBank· DDBJ
KDR44702.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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