Q9KMY3 · HMP_VIBCH

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 (By similarity).

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 site137Charge relay system
Binding site190FAD (UniProtKB | ChEBI)
Binding site206-209FAD (UniProtKB | ChEBI)
Binding site274-279NADP+ (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 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
    • Ordered locus names
      VC_A0183

Organism names

Accessions

  • Primary accession
    Q9KMY3

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000524491-394Flavohemoprotein

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-138Globin
Region149-394Reductase
Domain152-262FAD-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

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
    394
  • Mass (Da)
    44,191
  • Last updated
    2000-10-01 v1
  • Checksum
    DDA3490FAE28823A
MLTQEHINIIKSTIPLLESAGPALTQHFYQRMFSHNPELKHIFNMTHQKTGRQSVALFEAIAAYAKHIDNLAALTSAVERIAHKHTSFNIQPEHYQIVGHHLLETLRELAPDAFTQPVEEAWTAAYFFLAQVFIDREGALYLERKQALGGWRDGRTFVVREKQVESAYVTSFVLVPADGGAVLDYQPGQYIGIEVTPEGSDYREIRQYSLSHASNGREYRISVKREGVGSDNPGLVSHYLHNNVKVGDSVKLYAPAGDFFYVERERPVVLISAGVGATPMQAILHTLAKQNKSGVTYLYACNSAKEHTFAQETAQLIAQQGWMQQVWYRDESADDVLQGEMQLAELILPIEDGDFYLCGPIGFMQYVVKQLLALGVDKARIHYEVFGPHAQLAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE003853
EMBL· GenBank· DDBJ
AAF96096.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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