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   02-SEP-2026, entry version 103.
DE   RecName: Full=Leghemoglobin-1 {ECO:0000303|PubMed:1123063};
DE   AltName: Full=Leghemoglobin I {ECO:0000303|PubMed:1123063};
GN   Name=LBI {ECO:0000303|PubMed:1123063};
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, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Early white; 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: Leghemoglobin that reversibly binds oxygen O(2) through a
CC       pentacoordinated heme iron (By similarity). In root nodules,
CC       facilitates the diffusion of oxygen to the bacteroids while preventing
CC       the bacterial nitrogenase from being inactivated by buffering dioxygen,
CC       nitric oxide and carbon monoxide, and promoting the formation of
CC       reactive oxygen species (ROS, e.g. H(2)O(2)) (By similarity). This role
CC       is essential for symbiotic nitrogen fixation (SNF) (By similarity).
CC       {ECO:0000250|UniProtKB:P02237, ECO:0000250|UniProtKB:Q43296}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P02240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P02240}. Nucleus {ECO:0000250|UniProtKB:P02240}.
CC   -!- TISSUE SPECIFICITY: Root nodules. {ECO:0000269|PubMed:1123063}.
CC   -!- PTM: Nitrated in effective nodules and particularly in hypoxic
CC       conditions; this mechanism may play a protective role in the symbiosis
CC       by buffering toxic peroxynitrite NO(2)(-). Nitration level decrease
CC       during nodule senescence. {ECO:0000250|UniProtKB:P02234}.
CC   -!- PTM: Phosphorylation at Ser-45 disrupts the molecular environment of
CC       its porphyrin ring oxygen binding pocket, thus leading to a reduced
CC       oxygen consumption and to the delivery of oxygen O(2) to symbiosomes.
CC       {ECO:0000250|UniProtKB:Q3C1F7}.
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. {ECO:0000305|PubMed:1123063}.
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:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:UniProtKB-ARBA.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001032; Leghaemoglobin-like.
DR   InterPro; IPR019824; Leghaemoglobin_Fe_BS.
DR   PANTHER; PTHR22924; LEGHEMOGLOBIN-RELATED; 1.
DR   PANTHER; PTHR22924:SF92; NON-SYMBIOTIC HEMOGLOBIN 2; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00188; PLANTGLOBIN.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   PROSITE; PS00208; PLANT_GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding; Nitration;
KW   Nitrogen fixation; Nodulation; Nucleus; Oxygen transport; Phosphoprotein;
KW   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   DOMAIN          2..144
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         45
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         62
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         65
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
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   BINDING         96
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   MOD_RES         25
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02234"
FT   MOD_RES         30
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02234"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3C1F7"
FT   MOD_RES         134
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02234"
SQ   SEQUENCE   144 AA;  15531 MW;  6D26E91BD3AD6F22 CRC64;
     MGFTEKQEAL VNSSSQLFKQ NPSNYSVLFY TIILQKAPTA KAMFSFLKDS AGVVDSPKLG
     AHAEKVFGMV RDSAVQLRAT GEVVLDGKDG SIHIQKGVLD PHFVVVKEAL LKTIKEASGD
     KWSEELSAAW EVAYDGLATA IKAA
//