LECA_SPAPA
ID LECA_SPAPA Reviewed; 251 AA.
AC P86352;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Seed lectin alpha chain {ECO:0000303|PubMed:21889532};
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]
RP FUNCTION.
RX PubMed=23652482; DOI=10.1007/s00894-013-1854-4;
RA Abhilash J., Dileep K.V., Palanimuthu M., Geethanandan K., Sadasivan C.,
RA Haridas M.;
RT "Metal ions in sugar binding, sugar specificity and structural stability of
RT Spatholobus parviflorus seed lectin.";
RL J. Mol. Model. 19:3271-3278(2013).
RN [2]
RP FUNCTION.
RX PubMed=24460654; DOI=10.1111/cbdd.12291;
RA Tintu I., Abhilash J., Dileep K.V., Augustine A., Haridas M., Sadasivan C.;
RT "A lectin from Spatholobus parviflorus inhibits Aspergillus flavus alpha-
RT amylase: enzyme kinetics and thermodynamic studies.";
RL Chem. Biol. Drug Des. 84:116-122(2014).
RN [3] {ECO:0007744|PDB:3IPV}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP MANGANESE, FUNCTION, AND SUBUNIT.
RC TISSUE=Seed {ECO:0000269|PubMed:21889532};
RX PubMed=21889532; DOI=10.1016/j.ijbiomac.2011.08.021;
RA Geethanandan K., Abhilash J., Bharath S.R., Sadasivan C., Haridas M.;
RT "X-ray structure of a galactose-specific lectin from Spatholobous
RT parviflorous.";
RL Int. J. Biol. Macromol. 49:992-998(2011).
RN [4] {ECO:0007744|PDB:4M3C}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP MANGANESE.
RA Surya S., Abhilash J., Geethanandan K., Sadasivan C., Haridas M.;
RT "Structure of a binary complex between homologous tetrameric legume lectins
RT from Butea monosperma and Spatholobus parviflorus seeds.";
RL Submitted (AUG-2013) to the PDB data bank.
CC -!- FUNCTION: Galactose-binding lectin (PubMed:21889532, PubMed:23652482).
CC Exhibits hemagglutination activity in a calcium- and magnesium-
CC dependent manner (PubMed:23652482). Also binds to several carbohydrates
CC including lactose, D-galactose and GalNAc in a calcium- and magnesium-
CC dependent manner (PubMed:23652482). Likely to have antifungal activity
CC as it is able to inhibit the activity of the A.flavus alpha-amylase
CC (PubMed:24460654). {ECO:0000269|PubMed:21889532,
CC ECO:0000269|PubMed:23652482, ECO:0000269|PubMed:24460654}.
CC -!- SUBUNIT: Heterotetramer consisting of heterodimers of alpha and beta
CC chains. {ECO:0000269|PubMed:21889532}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 3IPV; X-ray; 2.04 A; A/C=1-251.
DR PDB; 4M3C; X-ray; 2.50 A; E/G=1-251.
DR PDBsum; 3IPV; -.
DR PDBsum; 4M3C; -.
DR SMR; P86352; -.
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..251
FT /note="Seed lectin alpha chain"
FT /id="PRO_0000386446"
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:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21889532,
FT ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"
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 32..35
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:4M3C"
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 165..172
FT /evidence="ECO:0007829|PDB:3IPV"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3IPV"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3IPV"
FT STRAND 191..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"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:3IPV"
SQ SEQUENCE 251 AA; 26373 MW; E52BD3633A1C2A48 CRC64;
AEETSFVFSK FKPLEPNLIL QGDALVTVAG VLQLTNVDKN GVPEPSSLGR ATYSAPINIW
DSATGLVASF ATSFRFTIYA PNIATIADGL AFFLAPVASA PDSGGGFLGL FDSAVSGSTY
QTVAVEFDTY ENTVFTDPPY THIGFDVNSI SSIKTVKWSL ANGEAAKVLI TYNSAVKLLV
ASLVYPSSKT SFILADIVDL SSVLPEWVRV GFSAATGASG GKIETHDVFS WSFASKLAGX
XTKDSSFLDG G
