A0A510I8S9 · A0A510I8S9_9VIBR

  • 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.

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
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 site135Charge relay system
Binding site188FAD (UniProtKB | ChEBI)
Binding site204-207FAD (UniProtKB | ChEBI)
Binding site268-273NADP+ (UniProtKB | ChEBI)
Site386Influences the redox potential of the prosthetic heme and FAD groups
Binding site387-390FAD (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
      VroAM7_27970

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AM7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio

Accessions

  • Primary accession
    A0A510I8S9

Proteomes

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain1-136Globin
Region147-394Reductase
Domain150-255FAD-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
    394
  • Mass (Da)
    44,083
  • Last updated
    2019-10-16 v1
  • Checksum
    909BAF9E21AB2ABD
MLSNQTIDIVKATAPLLAETGPKLTAHFYDRMFTHNPELKDIFNMSNQRNGDQREALFNAICAYATNIDNLPALLGAVEKIAHKHTSFMITKDQYQIVGTHLLATIDELFSPGQEVIDAWAEAYGVLANVFIQREEQIYQENAALQGGWRGLREFELVGKQLESENICSFVFKPTDGEVVSEYKPGQYLGIYINSDKFENQEIRQYSLSSAVQENTYRISVKREQGGKVSNFLHDELDIGDKVQLAAPAGDFFMDVDAATPVVLVSAGVGLTPTLSMLESLSEHQAPVTWVHAAENGQQHAFKQHVSQIVNAKENMNSLVWYNQPTAEDKIGEDFQFTGFVNLNEIEAALKQDNVQVYFCGPVGFMQHVAKQLLELGVAQEQFHYECFGPHKVV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP019798
EMBL· GenBank· DDBJ
BBL90144.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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