ID   LGB2_PEA                Reviewed;         147 AA.
AC   O48668;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Leghemoglobin Lb5-10;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sparkle; TISSUE=Root nodule;
RX   PubMed=11161022; DOI=10.1104/pp.125.2.641;
RA   Kawashima K., Suganuma N., Tamaoki M., Kouchi H.;
RT   "Two types of pea leghemoglobin genes showing different O2-binding
RT   affinities and distinct patterns of spatial expression in nodules.";
RL   Plant Physiol. 125:641-651(2001).
CC   -!- FUNCTION: Provides oxygen to the bacteroids. This role is essential for
CC       symbiotic nitrogen fixation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Root nodules.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; AB010831; BAA24685.1; -; mRNA.
DR   PIR; T06216; T06216.
DR   AlphaFoldDB; O48668; -.
DR   SMR; O48668; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001032; Leghaemoglobin.
DR   InterPro; IPR019824; Leghaemoglobin_Fe_BS.
DR   PANTHER; PTHR22924; PTHR22924; 1.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   PROSITE; PS00208; PLANT_GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Nitrogen fixation; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..147
FT                   /note="Leghemoglobin Lb5-10"
FT                   /id="PRO_0000192992"
FT   BINDING         62
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         94
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   147 AA;  15937 MW;  351F409DAC557306 CRC64;
     MGFTDKQEAL VNSSWESFKQ NLSGNSILFY TIILEKAPAA KGLFSFLKDT AGVEDSPKLQ
     AHAEQVFGLV RDSAAQLRTK GEVVLGNATL GAIHVQRGVT DPHFVVVKEA LLQTIKKASG
     NNWSEELNTA WEVAYDGLAT AIKKAMT