Q8GAZ4 · HMP_BURST

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:
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD 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)
Site384Influences the redox potential of the prosthetic heme and FAD groups
Binding site385-388FAD (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

Organism names

Accessions

  • Primary accession
    Q8GAZ4

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000524281-393Flavohemoprotein

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-139Globin
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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    43,707
  • Last updated
    2003-03-01 v1
  • Checksum
    D17DB36399BB717B
MLSAEHRAIVKATVPLLESGGEALTTHFYKTMLAEYPSVRPLFNQAHQQSGDQPRALANAVLMYARHIDQLEQLGGLVSQIVNKHVALNILPEHYPIVGACLLRAIREVLGAEIATDAVIEAWGAAYQQLADLLIGLEENVYVEKETATGGWRGTRAFVVARKVKESDEITSFYLRPADGGELLEFHPGQYIGLKLIVDGEEIRRNYSLSAAANGREYRISVKREPNGKASNYLHDSVNEGATLDLLTPSGDFTLEHNDKPLVLISGGVGITPTLAMLNAALQTSRPIHFIHATRHGGVHAFRDHIDELAARHPQLKRFYVYEKPRHDDEAHHAEGYIDEARLIEWLPATRDVDVYFLGPKSFMQAVKRHLKTIGVPEKQSRYEFFGPASALD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB035325
EMBL· GenBank· DDBJ
BAC16771.1
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.
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