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S3IRS5 · S3IRS5_9ENTR

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

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.

Type
IDPosition(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 site139Charge relay system
Binding site192FAD (UniProtKB | ChEBI)
Binding site208-211FAD (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
      HMPREF0201_03517

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 4568
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Cedecea

Accessions

  • Primary accession
    S3IRS5

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain4-138Globin
Region151-400Reductase
Domain154-259FAD-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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    400
  • Mass (Da)
    44,294
  • Last updated
    2013-09-18 v1
  • MD5 Checksum
    6CA615963E459C7A2C5F206ED7F6D46D
MENAMLDAQTIAVVKSTIPLLAATGPKLTAHFYDRMFSHNPELKEIFNMSNQRNGDQREALFNAICAYAANIENLATLLPAVEKIAQKHTTFQIKPEQYDIVGGHLLATLDELFSPGQEVLDAWGKAYGVLAGVFITRESEIYQDNAAKKGGWEGTRPFTIVAKEPQSSLITSFELAPADGGPVADYQPGQYLGIWLKPEGFPHQEIRQYSLTRQPNGKSYRIAVKREDKGMVSNWLHNHAQPGDKVHLAAPAGDFFMSVESGTPVTLISAGVGQTPMLAMLDTLAGSGHQAQVNWLHAAEHGDVHAFSDEVAALGAKLPRFESHVWYREPSDKDREQARFTREGLMDLLAEEGKLSDPAMQFYLCGPINFMRFAAEQLVKIGVDKDRIHYECFGPHKVM

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ATDT01000031
EMBL· GenBank· DDBJ
EPF15281.1
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.
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