T0QUF1 · T0QUF1_AERSA

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 site137Charge relay system
Binding site190FAD (UniProtKB | ChEBI)
Binding site206-209FAD (UniProtKB | ChEBI)
Binding site270-275NADP+ (UniProtKB | ChEBI)
Site389Influences the redox potential of the prosthetic heme and FAD groups
Binding site390-393FAD (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
      Asalp_07720

Organism names

Accessions

  • Primary accession
    T0QUF1

Proteomes

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-134Globin
Region149-397Reductase
Domain152-257FAD-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
    397
  • Mass (Da)
    44,173
  • Last updated
    2013-10-16 v1
  • Checksum
    24D8A6D76D642FB7
MLDQATIAVIKSTIPLLESAGPALTQHFYQRMFSHNPELKDIFNLAHQRSGGQPLALFNAVAAYAKNIDNLGALAGAVERIAHKHTGFMIQPEQYHIVGSHLLATLKELGGSAVTDEVLDAWGKAYGVLASIFIGRESEIYQEKASEIGGWQGPRPFIIKEKRVESELITSFMLAPIDGKPVLHFKPGQYLSIQLNHPELEYQEIRQYSLSDAPNGRDYRISVKREPQGQVSNLLHDHLQVGDKVDLMPPTGDFFLQASASTPVVLLSAGVGLTPMLSMLNQLLSTGHDADVCWLHACERGSLHAFKEDIQRKRQQHHKLQSRVWYREPSDRDEQGKDYDFSGTMDLSQVSGLLVPQAHYYFCGPLGFMQGIKTQLSAAGIPTEQLHYEVFGPHQDL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP022426
EMBL· GenBank· DDBJ
ATP08013.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp