LGB2_LUPLU
ID LGB2_LUPLU Reviewed; 154 AA.
AC P02240;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Leghemoglobin-2;
DE AltName: Full=Leghemoglobin II;
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 PROTEIN SEQUENCE OF 2-154.
RC TISSUE=Root nodule;
RA Egorov T.A., Kazakov V.K., Shakhparonov M.I., Feigina M.Y., Kostetsky P.V.;
RT "Primary structure of leghemoglobin II from the nodules of the yellow lupin
RT (Lupinus luteus L.).";
RL Bioorg. Khim. 4:476-480(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-154.
RX PubMed=2442601; DOI=10.1007/bf00580652;
RA Konieczny A., Jensen E.O., Marcker K.A., Legocki A.B.;
RT "Molecular cloning of lupin leghemoglobin cDNA.";
RL Mol. Biol. Rep. 12:61-66(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RA Arutiunian E.G., Kuranova I.P., Vainshtein B.K., Steigemann W.;
RT "X-ray structural investigation of leghemoglobin. VI. Structure of acetate-
RT ferrileghemoglobin at a resolution of 2.0 A.";
RL Sov. Phys. Crystallogr. 25:43-52(1980).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS).
RC TISSUE=Root nodule;
RX PubMed=1118009; DOI=10.1038/254163a0;
RA Vainshtein B.K., Harutyunyan E.H., Kuranova I.P., Borisov V.V.,
RA Sosfenov N.I., Pavlovsky A.G., Grebenko A.I., Konareva N.V.;
RT "Structure of leghaemoglobin from lupin root nodules at 5-A resolution.";
RL Nature 254:163-164(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 -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR EMBL; M17893; AAA33410.1; -; mRNA.
DR PIR; S41328; GPYL2.
DR PDB; 1GDI; X-ray; 1.80 A; A=2-154.
DR PDB; 1GDJ; X-ray; 1.70 A; A=2-154.
DR PDB; 1GDK; X-ray; 1.80 A; A=2-154.
DR PDB; 1GDL; X-ray; 1.80 A; A=2-154.
DR PDB; 1LH1; X-ray; 2.00 A; A=2-154.
DR PDB; 1LH2; X-ray; 2.00 A; A=2-154.
DR PDB; 1LH3; X-ray; 2.00 A; A=2-154.
DR PDB; 1LH5; X-ray; 2.00 A; A=2-154.
DR PDB; 1LH6; X-ray; 2.00 A; A=2-154.
DR PDB; 1LH7; X-ray; 2.00 A; A=2-154.
DR PDB; 2GDM; X-ray; 1.70 A; A=2-154.
DR PDB; 2LH1; X-ray; 2.00 A; A=2-154.
DR PDB; 2LH2; X-ray; 2.00 A; A=2-154.
DR PDB; 2LH3; X-ray; 2.00 A; A=2-154.
DR PDB; 2LH5; X-ray; 2.00 A; A=2-154.
DR PDB; 2LH6; X-ray; 2.00 A; A=2-154.
DR PDB; 2LH7; X-ray; 2.00 A; A=2-154.
DR PDBsum; 1GDI; -.
DR PDBsum; 1GDJ; -.
DR PDBsum; 1GDK; -.
DR PDBsum; 1GDL; -.
DR PDBsum; 1LH1; -.
DR PDBsum; 1LH2; -.
DR PDBsum; 1LH3; -.
DR PDBsum; 1LH5; -.
DR PDBsum; 1LH6; -.
DR PDBsum; 1LH7; -.
DR PDBsum; 2GDM; -.
DR PDBsum; 2LH1; -.
DR PDBsum; 2LH2; -.
DR PDBsum; 2LH3; -.
DR PDBsum; 2LH5; -.
DR PDBsum; 2LH6; -.
DR PDBsum; 2LH7; -.
DR AlphaFoldDB; P02240; -.
DR SMR; P02240; -.
DR EvolutionaryTrace; P02240; -.
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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Nitrogen fixation; Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..154
FT /note="Leghemoglobin-2"
FT /id="PRO_0000192985"
FT BINDING 64
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 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 CONFLICT 62
FT /note="Q -> AS (in Ref. 2; AAA33410)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="Q -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="T -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:1GDJ"
FT TURN 46..50
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 59..82
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1GDJ"
FT HELIX 129..153
FT /evidence="ECO:0007829|PDB:1GDJ"
SQ SEQUENCE 154 AA; 16783 MW; 57091640CBAEAF81 CRC64;
MGALTESQAA LVKSSWEEFN ANIPKHTHRF FILVLEIAPA AKDLFSFLKG TSEVPQNNPE
LQAHAGKVFK LVYEAAIQLQ VTGVVVTDAT LKNLGSVHVS KGVADAHFPV VKEAILKTIK
EVVGAKWSEE LNSAWTIAYD ELAIVIKKEM NDAA
