LECB_SPAPA
ID LECB_SPAPA Reviewed; 239 AA.
AC P86353;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Seed lectin beta chain {ECO:0000303|Ref.1};
OS Spatholobus parviflorus (Butea parviflora).
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; Spatholobus.
OX NCBI_TaxID=132465;
RN [1] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Cotyledon {ECO:0000269|Ref.1};
RA Geethanandan K., Abhilash J., Bharath S.R., Sadasivan C., Haridas M.;
RT "Crystal structure of Spatholobus parviflorus seed lectin.";
RL Submitted (AUG-2009) to UniProtKB.
CC -!- FUNCTION: Galactose-binding lectin. Agglutinates human erythrocytes,
CC and requires Ca(2+) and Mn(2+) ions for full agglutinating activity.
CC Has antifungal activity against Fusarium sp., A.niger and A.flavus.
CC {ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Tetramer consisting of heterodimers of alpha and beta chains.
CC {ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Appears during seed development and remains in
CC mature seeds. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR PDB; 3IPV; X-ray; 2.04 A; B/D=1-239.
DR PDB; 4M3C; X-ray; 2.50 A; F/H=1-239.
DR PDBsum; 3IPV; -.
DR PDBsum; 4M3C; -.
DR AlphaFoldDB; P86353; -.
DR SMR; P86353; -.
DR UniLectin; P86353; -.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IEA:GOC.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Calcium; Fungicide; Lectin; Manganese;
KW Metal-binding.
FT CHAIN 1..239
FT /note="Seed lectin beta chain"
FT /id="PRO_0000386447"
FT BINDING 88
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 106
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 217
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 218
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3IPV"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3IPV"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3IPV"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:3IPV"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:3IPV"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3IPV"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3IPV"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:3IPV"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 206..216
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:3IPV"
SQ SEQUENCE 239 AA; 25249 MW; 93C77BBD5DC0FDCD CRC64;
AEETSFVFSK FKPLEPNLIL QGDALVTVAG VLQLTNVDSN GVPEPSSLGR ATYSAPINIW
DSATGLVASF ATSFRFTIYA PNIATIADGL AFFLAPVASA PDSGGGFLGL FDSAVGDTTY
QTVAVEFDTY ENTVFTDPPY THIGFDVNSI SSIKTVKWSL ANGEAAKVLI TYNSAVKLLV
ASLVYPSSKT SFILADIVDL SSVLPEWVRV GFSAATGASK GYIETHDVFS WSFASKLAG
