G7KGT0 · LGB8_MEDTR

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) (PubMed:17540516, PubMed:29868087, PubMed:32442331).
This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:29868087, PubMed:32442331).

Features

Showing features for binding site.

114720406080100120140
TypeIDPosition(s)Description
Binding site45heme b (UniProtKB | ChEBI)
Binding site62O2 (UniProtKB | ChEBI)
Binding site65heme b (UniProtKB | ChEBI)
Binding site94Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue
Binding site97heme b (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionoxygen binding
Molecular Functionoxygen carrier activity
Biological Processnitrogen fixation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Leghemoglobin 8
  • Short names
    MtLb8
  • Alternative names
    • Leghemoglobin 6
      (MtLb6
      )
    • Leghemoglobin Lb120-1
      (MtLb120-1
      )

Gene names

    • Name
      LB8
    • Synonyms
      LB120-1
      , LB6
    • ORF names
      MtrunA17_Chr5g0435621
    • Ordered locus names
      MTR_5g080440
      , Medtr5g080440

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Jemalong A17
  • 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 > Trifolieae > Medicago

Accessions

  • Primary accession
    G7KGT0

Proteomes

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Reduced nitrogenase activity in root nodules.

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00004602922-147Leghemoglobin 8
Modified residue25Nitrated tyrosine
Modified residue30Nitrated tyrosine
Modified residue45Phosphoserine
Modified residue135Nitrated 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-45 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

Proteomic databases

Expression

Tissue specificity

Root nodules.

Induction

Locally down-regulated by cadmium (Cd), thus leading to nodule inactivation and impaired biological nitrogen fixation (BNF).

Developmental stage

In root nodules, accumulates during maturation but gradually fades out during nodule senescence (PubMed:29868087).
Highest levels observed in the nitrogen fixation zone (III), but also observed in infection zone (II) (PubMed:29868087).

Interaction

Subunit

Monomer (By similarity).
Interacts with CAS31 in the cytoplasm; this interaction leads to its protection from denaturation under thermal and drought stresses (PubMed:29868087).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-147Globin

Sequence similarities

Belongs to the plant globin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    147
  • Mass (Da)
    15,940
  • Last updated
    2012-01-25 v1
  • Checksum
    1969AEDD62F07F70
MGFTEKQESLVNSSWESFKQNLSGYSVLFYTIILEKAPAAKGMFSFLKDTTGVQDSPQLQAHAAKVFEMVRDSAVQLRATGEVILGDATLGAIHIQKGVVDPHFVVVKEALLKTIKEAAGGNWSEELSTAWEVAYDGLAASIKKSMS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM001221
EMBL· GenBank· DDBJ
AES99407.1
EMBL· GenBank· DDBJ
Genomic DNA
PSQE01000005
EMBL· GenBank· DDBJ
RHN57001.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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