ID   LGB1_LUPLU              Reviewed;         154 AA.
AC   P02239;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Leghemoglobin-1 {ECO:0000303|PubMed:3628011};
DE            Short=LlLb1 {ECO:0000303|PubMed:3628011};
DE   AltName: Full=Leghemoglobin I {ECO:0000303|PubMed:3628011};
DE            Short=LulbI {ECO:0000303|PubMed:10778735};
GN   Name=Lb1 {ECO:0000303|PubMed:3628011};
OS   Lupinus luteus (European yellow lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3628011; DOI=10.1093/nar/15.16.6742;
RA   Konieczny A.;
RT   "Nucleotide sequence of lupin leghemoglobin I cDNA.";
RL   Nucleic Acids Res. 15:6742-6742(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Ventus; TISSUE=Root nodule;
RA   Strozycki P.M., Karlowski W.M., Legocki A.B.;
RT   "Yellow lupine gene coding for leghemoglobin I.";
RL   (er) Plant Gene Register PGR98-017(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-154.
RC   TISSUE=Root nodule;
RA   Egorov T.A., Feigina M.Y., Kazakov V.K., Shakhparonov M.I., Mimaleva S.I.,
RA   Ovchinnikov Y.A.;
RT   "The complete amino acid sequence of the leghemoglobin I from yellow lupin
RT   root nodules.";
RL   Bioorg. Khim. 2:125-128(1976).
RN   [4]
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Ventus;
RX   PubMed=10778735; DOI=10.1007/s004380051158;
RA   Strozycki P.M., Karlowski W.M., Dessaux Y., Petit A., Legocki A.B.;
RT   "Lupine leghemoglobin I: expression in transgenic Lotus and tobacco
RT   tissues.";
RL   Mol. Gen. Genet. 263:173-182(2000).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Taper;
RX   PubMed=25817415; DOI=10.1016/j.jplph.2015.01.019;
RA   Frankowski K., Wilmowicz E., Kucko A., Zienkiewicz A., Zienkiewicz K.,
RA   Kopcewicz J.;
RT   "Molecular cloning of the BLADE-ON-PETIOLE gene and expression analyses
RT   during nodule development in Lupinus luteus.";
RL   J. Plant Physiol. 179:35-39(2015).
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: Accumulates in developing root nodules and present
CC       in roots, especially in the upper part (PubMed:10778735,
CC       PubMed:25817415). Detected in leaves at low levels (PubMed:10778735).
CC       {ECO:0000269|PubMed:10778735, ECO:0000269|PubMed:25817415}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout root nodule development.
CC       {ECO:0000269|PubMed:25817415}.
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-46 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   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y00401; CAA68462.1; -; mRNA.
DR   EMBL; X77043; CAA54332.1; -; mRNA.
DR   EMBL; U50083; AAC04853.1; -; Genomic_DNA.
DR   PIR; A26808; GPYL.
DR   AlphaFoldDB; P02239; -.
DR   SMR; P02239; -.
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   CDD; cd08923; class1-2_nsHbs_Lbs; 1.
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|Ref.3"
FT   CHAIN           2..154
FT                   /note="Leghemoglobin-1"
FT                   /id="PRO_0000192984"
FT   DOMAIN          3..151
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         46
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         64
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         67
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         98
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         101
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3C1F7"
FT   MOD_RES         139
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02234"
FT   CONFLICT        80
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="E -> G (in Ref. 1; CAA68462)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  16753 MW;  58101C830CB21F14 CRC64;
     MGVLTDVQVA LVKSSFEEFN ANIPKNTHRF FTLVLEIAPG AKDLFSFLKG SSEVPQNNPD
     LQAHAGKVFK LTYEAAIQLQ VNGAVASDAT LKSLGSVHVS KGVVDAHFPV VKEAILKTIK
     EVVGDKWSEE LNTAWTIAYD ELAIIIKKEM KDAA
//