| IED ID |
IndEnz0001000503 |
| Enzyme Type ID |
amylase000503 |
| Protein Name |
Seed lectin alpha chain
|
| Gene Name |
|
| Organism |
Spatholobus parviflorus (Butea parviflora) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Viridiplantae
Streptophyta
Streptophytina
Embryophyta
Tracheophyta
Euphyllophyta
Spermatophyta
Magnoliopsida
Mesangiospermae
eudicotyledons
Gunneridae
Pentapetalae
rosids
fabids
Fabales
Fabaceae
Papilionoideae
50 kb inversion clade
NPAAA clade
indigoferoid/millettioid clade
Phaseoleae
Spatholobus
Spatholobus parviflorus (Butea parviflora)
|
| Enzyme Sequence |
AEETSFVFSKFKPLEPNLILQGDALVTVAGVLQLTNVDKNGVPEPSSLGRATYSAPINIWDSATGLVASFATSFRFTIYAPNIATIADGLAFFLAPVASAPDSGGGFLGLFDSAVSGSTYQTVAVEFDTYENTVFTDPPYTHIGFDVNSISSIKTVKWSLANGEAAKVLITYNSAVKLLVASLVYPSSKTSFILADIVDLSSVLPEWVRVGFSAATGASGGKIETHDVFSWSFASKLAGXXTKDSSFLDGG |
| Enzyme Length |
251 |
| Uniprot Accession Number |
P86352 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
BINDING 88; /note=Glucose; /evidence=ECO:0000250|UniProtKB:P02870; BINDING 106; /note=Glucose; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P02870; BINDING 217; /note=Glucose; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P02870; BINDING 218; /note=Glucose; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P02870 |
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
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| Enzyme Function |
FUNCTION: Galactose-binding lectin (PubMed:21889532, PubMed:23652482). Exhibits hemagglutination activity in a calcium- and magnesium-dependent manner (PubMed:23652482). Also binds to several carbohydrates including lactose, D-galactose and GalNAc in a calcium- and magnesium-dependent manner (PubMed:23652482). Likely to have antifungal activity as it is able to inhibit the activity of the A.flavus alpha-amylase (PubMed:24460654). {ECO:0000269|PubMed:21889532, ECO:0000269|PubMed:23652482, ECO:0000269|PubMed:24460654}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (15); Binding site (4); Chain (1); Helix (5); Metal binding (8); Turn (4) |
| Keywords |
3D-structure;Antimicrobial;Calcium;Fungicide;Lectin;Manganese;Metal-binding |
| Interact With |
|
| Induction |
|
| Subcellular Location |
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| Modified Residue |
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| Post Translational Modification |
|
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (2) |
| Cross Reference PDB |
3IPV;
4M3C;
|
| Mapped Pubmed ID |
- |
| Motif |
|
| Gene Encoded By |
|
| Mass |
26,373 |
| Kinetics |
|
| Metal Binding |
METAL 126; /note="Manganese"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 128; /note="Calcium"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 128; /note="Manganese"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 130; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 132; /note="Calcium"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 137; /note="Calcium"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 137; /note="Manganese"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C"; METAL 142; /note="Manganese; via tele nitrogen"; /evidence="ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C" |
| Rhea ID |
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| Cross Reference Brenda |
|