LGB1_MEDSA
ID LGB1_MEDSA Reviewed; 147 AA.
AC P09187;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Leghemoglobin-1;
DE AltName: Full=Leghemoglobin I;
OS Medicago sativa (Alfalfa).
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; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Iroquois;
RX PubMed=2726471; DOI=10.1093/nar/17.8.3307;
RA Davidowitz E.J., Lang-Unnasch N.;
RT "Nucleotide sequence of a cDNA clone encoding a leghemoglobin from Medicago
RT sativa.";
RL Nucleic Acids Res. 17:3307-3307(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Hybrid 11 X 8; TISSUE=Root nodule;
RX AGRICOLA=IND91035192; DOI=10.1007/BF00019516;
RA Barker D.G., Gallusci P., Lullien V., Khan H., Gherardi M., Huguet T.;
RT "Identification of two groups of leghemoglobin genes in alfalfa (Medicago
RT sativa) and a study of their expression during root nodule development.";
RL Plant Mol. Biol. 11:761-772(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1888894; DOI=10.1007/bf00017926;
RA Davidowitz E.J., Creissen G., Vincze E., Kiss G.B., Lang-Unnasch N.;
RT "Sequence analysis of alfalfa (Medicago sativa) leghemoglobin cDNA and
RT genomic clones.";
RL Plant Mol. Biol. 16:161-165(1991).
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; X13375; CAA31750.1; -; mRNA.
DR EMBL; X14311; CAA32492.1; -; mRNA.
DR EMBL; M36100; AAA32657.1; -; mRNA.
DR PIR; S08508; S08508.
DR PIR; S15768; S15768.
DR AlphaFoldDB; P09187; -.
DR SMR; P09187; -.
DR PRIDE; P09187; -.
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..147
FT /note="Leghemoglobin-1"
FT /id="PRO_0000192986"
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 94
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 CONFLICT 33
FT /note="V -> I (in Ref. 2; CAA32492/AAA32657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16055 MW; DBD0A94E743CB28A CRC64;
MSFTDKQEAL VNSSWEAFKQ NLPRYSVFFY TVVLEKAPAA KGLFSFLKNS AEVQDSPQLQ
AHAEKVFGLV RDSAVQLRAT GGVVLGDATL GAIHVRKGVV DPHFVVVKEA LLKTIKEAAG
DKWSEELNTA WEVAYDALAT AIKKAMS
