ID   LGB1_VICFA              Reviewed;         144 AA.
AC   P02232;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Leghemoglobin-1;
DE   AltName: Full=Leghemoglobin I;
OS   Vicia faba (Broad bean) (Faba vulgaris).
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; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-144.
RC   TISSUE=Root nodule;
RX   PubMed=1123063; DOI=10.1016/0014-5793(75)80849-0;
RA   Richardson M., Dilworth M.J., Scawen M.D.;
RT   "The amino acid sequence of leghaemoglobin I from root nodules of broad
RT   bean (Vicia faba L.).";
RL   FEBS Lett. 51:33-37(1975).
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   -!- MISCELLANEOUS: Asp-5, Gln-6, Gly-23, Gly-24, Lys-35, Gly-42, Gln-57,
CC       Gln-65, Glu-72, Ile-75, Gln-78, Glu-127, Ile-129, and Glu-135 were also
CC       found in this pooled preparation.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   PIR; A02554; GPVF.
DR   AlphaFoldDB; P02232; -.
DR   SMR; P02232; -.
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:1123063"
FT   CHAIN           2..144
FT                   /note="Leghemoglobin-1"
FT                   /id="PRO_0000193006"
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   144 AA;  15531 MW;  6D26E91BD3AD6F22 CRC64;
     MGFTEKQEAL VNSSSQLFKQ NPSNYSVLFY TIILQKAPTA KAMFSFLKDS AGVVDSPKLG
     AHAEKVFGMV RDSAVQLRAT GEVVLDGKDG SIHIQKGVLD PHFVVVKEAL LKTIKEASGD
     KWSEELSAAW EVAYDGLATA IKAA