ID   LGB_PSOTE               Reviewed;         145 AA.
AC   P27199;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Leghemoglobin;
OS   Psophocarpus tetragonolobus (Winged bean) (Dolichos tetragonolobus).
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; indigoferoid/millettioid clade; Phaseoleae; Psophocarpus.
OX   NCBI_TaxID=3891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. UP599;
RX   PubMed=7764023; DOI=10.1007/bf00199763;
RA   Manen J.F., Simon P.;
RT   "A possible explanation for the multiple polyadenylation sites in
RT   transcripts coding for a winged-bean leghemoglobin.";
RL   Planta 191:289-292(1993).
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   EMBL; X65874; CAA46704.1; -; mRNA.
DR   EMBL; S65139; AAC60563.1; -; mRNA.
DR   PIR; S21456; S21456.
DR   AlphaFoldDB; P27199; -.
DR   SMR; P27199; -.
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   CHAIN           1..145
FT                   /note="Leghemoglobin"
FT                   /id="PRO_0000192999"
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         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"
SQ   SEQUENCE   145 AA;  15551 MW;  A5A2B15657728759 CRC64;
     MGGFTEKQEA LVNSSYEAFK ANVPQYSVVF YTSILEKAPA AKDLFPFLAN GVDPTNPKLI
     GHAEKLFGLV HDSAAQLRAK GAVVADAALG SLHAQKGVTD PQFVVVKEAL LKTVKEAVGD
     KWSDELSNAW EVAYNELAAA LKKAF