LGBA_SOYBN
ID LGBA_SOYBN Reviewed; 144 AA.
AC P02238;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Leghemoglobin A;
DE AltName: Full=Nodulin-2;
DE Short=N-2;
GN Name=LBA;
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6278428; DOI=10.1093/nar/10.2.689;
RA Hyldig-Nielsen J.J., Jensen E.O., Paludan K., Wiborg O., Garrett R.,
RA Joergensen P., Marcker K.A.;
RT "The primary structures of two leghemoglobin genes from soybean.";
RL Nucleic Acids Res. 10:689-701(1982).
RN [2]
RP PROTEIN SEQUENCE OF 2-144.
RX PubMed=4798828; DOI=10.3891/acta.chem.scand.27-3986;
RA Ellfolk N., Sievers G.;
RT "The primary structure of soybean leghemoglobin. IV. Fractionation and
RT sequence of thermolytic peptides of the apoprotein of the slow component
RT (Lba).";
RL Acta Chem. Scand. 27:3986-3992(1973).
RN [3]
RP SEQUENCE REVISION TO 51-55.
RX PubMed=4477921; DOI=10.3891/acta.chem.scand.28b-1245;
RA Ellfolk N., Sievers G.;
RT "Correction of the amino acid sequence of soybean leghemoglobin alpha.";
RL Acta Chem. Scand. B 28:1245-1246(1974).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=8307026; DOI=10.1111/j.1432-1033.1994.tb19977.x;
RA Morikis D., Lepre C.A., Wright P.E.;
RT "1H resonance assignments and secondary structure of the carbon monoxide
RT complex of soybean leghemoglobin determined by homonuclear two-dimensional
RT and three-dimensional NMR spectroscopy.";
RL Eur. J. Biochem. 219:611-626(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=15299933; DOI=10.1107/s0907444997000292;
RA Ellis P.J., Appleby C.A., Guss J.M., Hunter W.N., Ollis D.L., Freeman H.C.;
RT "Structure of ferric soybean leghemoglobin A nicotinate at 2.3-A
RT resolution.";
RL Acta Crystallogr. D 53:302-310(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9086279; DOI=10.1006/jmbi.1996.0833;
RA Hargrove M.S., Barry J.K., Brucker E.A., Berry M.B., Phillips G.N. Jr.,
RA Olson J.S., Arredondo-Peter R., Dean J.M., Klucas R.V., Sarath G.;
RT "Characterization of recombinant soybean leghemoglobin a and apolar distal
RT histidine mutants.";
RL J. Mol. Biol. 266:1032-1042(1997).
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; V00453; CAA23731.1; -; Genomic_DNA.
DR PIR; A93447; GPSYS.
DR RefSeq; NP_001235928.1; NM_001248999.2.
DR PDB; 1BIN; X-ray; 2.20 A; A/B=2-144.
DR PDB; 1FSL; X-ray; 2.30 A; A/B=2-144.
DR PDBsum; 1BIN; -.
DR PDBsum; 1FSL; -.
DR AlphaFoldDB; P02238; -.
DR SMR; P02238; -.
DR STRING; 3847.GLYMA10G34290.1; -.
DR PRIDE; P02238; -.
DR ProMEX; P02238; -.
DR EnsemblPlants; KRH34687; KRH34687; GLYMA_10G199100.
DR GeneID; 100527427; -.
DR Gramene; KRH34687; KRH34687; GLYMA_10G199100.
DR KEGG; gmx:100527427; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_11_2_1; -.
DR InParanoid; P02238; -.
DR OMA; LIMERAP; -.
DR OrthoDB; 696109at2759; -.
DR EvolutionaryTrace; P02238; -.
DR Proteomes; UP000008827; Chromosome 10.
DR Genevisible; P02238; GM.
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 GO; GO:0009877; P:nodulation; 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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Nitrogen fixation; Nodulation; Oxygen transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4798828"
FT CHAIN 2..144
FT /note="Leghemoglobin A"
FT /id="PRO_0000193002"
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"
FT CONFLICT 100
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="KA -> AK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 57..80
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:1BIN"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 100..118
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1BIN"
FT HELIX 124..143
FT /evidence="ECO:0007829|PDB:1BIN"
SQ SEQUENCE 144 AA; 15374 MW; E03D27BC73997DB5 CRC64;
MVAFTEKQDA LVSSSFEAFK ANIPQYSVVF YTSILEKAPA AKDLFSFLAN GVDPTNPKLT
GHAEKLFALV RDSAGQLKAS GTVVADAALG SVHAQKAVTD PQFVVVKEAL LKTIKAAVGD
KWSDELSRAW EVAYDELAAA IKKA
