Q5WL63 · Q5WL63_SHOC1

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
Site33Involved in heme-bound ligand stabilization and O-O bond activation
Site88Influences the redox potential of the prosthetic heme and FAD groups
Binding site89Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue
Active site99Charge relay system
Active site141Charge relay system
Binding site194FAD (UniProtKB | ChEBI)
Binding site210-213FAD (UniProtKB | ChEBI)
Binding site280-285NADP+ (UniProtKB | ChEBI)
Site400Influences the redox potential of the prosthetic heme and FAD groups
Binding site401-404FAD (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
    • Ordered locus names
      ABC0350

Organism names

Accessions

  • Primary accession
    Q5WL63

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain5-142Globin
Region153-411Reductase
Domain156-267FAD-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
    411
  • Mass (Da)
    46,481
  • Last updated
    2004-11-23 v1
  • Checksum
    F66A58E5D4C2967E
MSTVMLKEESKRLVKATVPILAAHGETITKHFYKRMFHHHPELLNVFNRTNQKIGRQPQALANSIYAAAQHIDNLEAILPVVKRIAHKHRSLNIKPEQYPIVGENLLAAMKEVLGEAASDDVIEAWREAYEIIAGVFIEVEKQMYDQAGKAPGGWSGFRSFVVEKKKQESKAITSFYLKPKDGNEIASYQPGQYMTVKVNIPGDTYTHMRQYSLSDAPGKGYYRISVKREEGNTECPPGVVSNYLHQHIREGDVLEMTAPAGDFTLKQGEERPIVLISGGVGITPLMSMFNTLMQQGTKQKVTFIHAAIDGTYHAMHDHVAQTASQKENVHYAVCYERPTSEDQMNPYMKKEGYIDEQFLRSMIEDHHADFYFCGPIPFMKTVYHILNNWGVPEEQIHYEFFGPAGTLASS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP006627
EMBL· GenBank· DDBJ
BAD62892.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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