P02238 · LGB3_SOYBN

Function

function

Leghemoglobin that reversibly binds oxygen O2 through a pentacoordinated heme iron (PubMed:29100196).
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:22308405, PubMed:29701804, PubMed:32297921).
This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:32297921).

Features

Showing features for binding site.

114420406080100120140
TypeIDPosition(s)Description
Binding site46heme b (UniProtKB | ChEBI)
Binding site62O2 (UniProtKB | ChEBI)
Binding site65heme b (UniProtKB | ChEBI)
Binding site93Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue
Binding site96heme 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 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 cobalt ion
Biological Processresponse to hydrogen sulfide
Biological Processresponse to nitrogen compound

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Leghemoglobin 3
  • Short names
    GmLb3
  • Alternative names
    • Hemoglobin 2-4
      (GmGLB2-4
      )
    • Leghemoglobin alpha
      (GmLba
      ; Leghemoglobin A
      )
    • Nodulin-2 (N-2)

Gene names

    • Name
      LB3
    • Synonyms
      GLB2-4
      , LBA
    • Ordered locus names
      Glyma_10G199100

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Williams 82
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja

Accessions

  • Primary accession
    P02238
  • Secondary accessions
    • C6T4A7

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylvaline
ChainPRO_00001930022-144Leghemoglobin 3
Modified residue26Nitrated tyrosine
Modified residue31Nitrated tyrosine
Modified residue46Phosphoserine
Modified residue134Nitrated tyrosine

Post-translational modification

Nitrated mainly at Tyr-31 and, to a lower extent, at Tyr-26 and Tyr-134, in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO2- (PubMed:17259612, PubMed:22308405, PubMed:25603991).
Nitration level decrease during nodule senescence (PubMed:17259612, PubMed:22308405, PubMed:25603991).
Phosphorylation at Ser-46 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

Specifically expressed in root nodules.

Induction

Negatively regulated by cobalt (Co) in a dose-dependent manner (PubMed:18838253).
Induced by hydrogen sulfide H2S (PubMed:31204904).
Suppressed by exposure to excess nitrogen (N); this repression is associated with nodule greening and reduced biological nitrogen fixation (BN) efficiency (PubMed:32297921).
Induced by iron-based nanomaterial (Fe-NMs) (PubMed:36479882).

Developmental stage

Gradual accumulation in developping and maturating root nodules (PubMed:32297921).
Levels decline during nodule senescence (PubMed:32297921).

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-144Globin

Sequence similarities

Belongs to the plant globin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    144
  • Mass (Da)
    15,374
  • Last updated
    2007-01-23 v2
  • Checksum
    E03D27BC73997DB5
MVAFTEKQDALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLANGVDPTNPKLTGHAEKLFALVRDSAGQLKASGTVVADAALGSVHAQKAVTDPQFVVVKEALLKTIKAAVGDKWSDELSRAWEVAYDELAAAIKKA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict100in Ref. 4; AA sequence
Sequence conflict102in Ref. 4; AA sequence
Sequence conflict106in Ref. 4; AA sequence
Sequence conflict143-144in Ref. 4; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
V00453
EMBL· GenBank· DDBJ
CAA23731.1
EMBL· GenBank· DDBJ
Genomic DNA
BT092268
EMBL· GenBank· DDBJ
ACU16517.1
EMBL· GenBank· DDBJ
mRNA
CM000843
EMBL· GenBank· DDBJ
KRH34687.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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