O48665 · LGB5_PEA

Function

function

Leghemoglobin that reversibly binds oxygen O2 through a pentacoordinated heme iron (By similarity).
In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H2O2) (By similarity).
This role is essential for symbiotic nitrogen fixation (SNF) (By similarity).

Features

Showing features for binding site.

114620406080100120140
TypeIDPosition(s)Description
Binding site44heme b (UniProtKB | ChEBI)
Binding site61O2 (UniProtKB | ChEBI)
Binding site64heme b (UniProtKB | ChEBI)
Binding site93Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue
Binding site96heme b (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionoxygen binding
Molecular Functionoxygen carrier activity
Biological Processnitrogen fixation
Biological Processnodulation
Biological Processresponse to abscisic acid

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Leghemoglobin Lb120-29
  • Short names
    PsLb120-29

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Sparkle
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum

Accessions

  • Primary accession
    O48665

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001929952-146Leghemoglobin Lb120-29
Modified residue24Nitrated tyrosine
Modified residue29Nitrated tyrosine
Modified residue44Phosphoserine
Modified residue134Nitrated tyrosine

Post-translational modification

Nitrated in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO2-. Nitration level decrease during nodule senescence.
Phosphorylation at Ser-44 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O2 to symbiosomes.

Keywords

Expression

Tissue specificity

Root nodules.

Induction

Strongly reduced levels in boron-deficient nodules (PubMed:20132519).
Inhibited by abscisic acid (ABA) in parallel with lower nitrogen fixation in nodules (PubMed:11283173).

Interaction

Subunit

Monomer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-146Globin

Sequence similarities

Belongs to the plant globin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    146
  • Mass (Da)
    15,860
  • Last updated
    2007-01-23 v3
  • Checksum
    32C105A6995087C4
MGFTDKQEALVNSSWELFKQNPGYSVLFYNIILKKAPATKGMFSFLKDSAGVVDSPKLQAHAEKVFGMVHDSAVQLRVSGEVVLGDATLGAIHIQKGVVDSHFVVVKEALLETIKEASGEKWSEELSTAWEVAYEGLASAIKKAMS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB009844
EMBL· GenBank· DDBJ
BAA24088.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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