LGB1_PEA
ID LGB1_PEA Reviewed; 148 AA.
AC P02233;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Leghemoglobin-1;
DE AltName: Full=Leghemoglobin I;
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 PROTEIN SEQUENCE OF 2-148.
RC STRAIN=cv. Torstai; TISSUE=Root nodule;
RX PubMed=7378476; DOI=10.1016/0005-2795(80)90012-4;
RA Lehtovaara P., Lappalainen A., Ellfolk N.;
RT "The amino acid sequence of pea (Pisum sativum) leghemoglobin.";
RL Biochim. Biophys. Acta 623:98-106(1980).
CC -!- FUNCTION: Provides oxygen to the bacteroids. This role is essential for
CC symbiotic nitrogen fixation.
CC -!- SUBUNIT: Monomer.
CC -!- TISSUE SPECIFICITY: Root nodules.
CC -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR PIR; A02555; GPPMI.
DR AlphaFoldDB; P02233; -.
DR SMR; P02233; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Metal-binding; Nitrogen fixation;
KW Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7378476"
FT CHAIN 2..148
FT /note="Leghemoglobin-1"
FT /id="PRO_0000192991"
FT BINDING 61
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 93
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"
FT VARIANT 22
FT /note="P -> Q"
FT VARIANT 24..25
FT /note="YS -> NA"
FT VARIANT 26
FT /note="I -> T"
FT VARIANT 26
FT /note="I -> V"
FT VARIANT 32
FT /note="V -> I"
FT VARIANT 94..95
FT /note="VQ -> AG"
SQ SEQUENCE 148 AA; 15966 MW; 6A6A6F3EE99D4589 CRC64;
MGFTDKQEAL VNSSSEFKQN LPGYSILFYT IVLEKAPAAK GLFSFLKDTA GVEDSPKLQA
HAEQVFGLVR DSAAQLRTKG EVVLGNATLG AIHVQKGVTN PHFVVVKEAL LQTIKKASGN
NWSEELNTAW EVAYDGLATA IKKAMKTA