O48665 · LGB5_PEA
- ProteinLeghemoglobin Lb120-29
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids146 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44 | heme b (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 61 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 64 | heme b (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 93 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue | ||||
Sequence: H | ||||||
Binding site | 96 | heme b (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxygen binding | |
Molecular Function | oxygen carrier activity | |
Biological Process | nitrogen fixation | |
Biological Process | nodulation | |
Biological Process | response to abscisic acid |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameLeghemoglobin Lb120-29
- Short namesPsLb120-29
Organism names
- Strain
- Taxonomic lineageEukaryota > 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 accessionO48665
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000192995 | 2-146 | Leghemoglobin Lb120-29 | |||
Sequence: GFTDKQEALVNSSWELFKQNPGYSVLFYNIILKKAPATKGMFSFLKDSAGVVDSPKLQAHAEKVFGMVHDSAVQLRVSGEVVLGDATLGAIHIQKGVVDSHFVVVKEALLETIKEASGEKWSEELSTAWEVAYEGLASAIKKAMS | ||||||
Modified residue | 24 | Nitrated tyrosine | ||||
Sequence: Y | ||||||
Modified residue | 29 | Nitrated tyrosine | ||||
Sequence: Y | ||||||
Modified residue | 44 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 134 | Nitrated tyrosine | ||||
Sequence: Y |
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
- PTM
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-146 | Globin | ||||
Sequence: GFTDKQEALVNSSWELFKQNPGYSVLFYNIILKKAPATKGMFSFLKDSAGVVDSPKLQAHAEKVFGMVHDSAVQLRVSGEVVLGDATLGAIHIQKGVVDSHFVVVKEALLETIKEASGEKWSEELSTAWEVAYEGLASAIKKAMS |
Sequence similarities
Belongs to the plant globin family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length146
- Mass (Da)15,860
- Last updated2007-01-23 v3
- Checksum32C105A6995087C4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB009844 EMBL· GenBank· DDBJ | BAA24088.1 EMBL· GenBank· DDBJ | mRNA |