O23553 · BAM3_ARATH
- ProteinBeta-amylase 3, chloroplastic
- GeneBAM3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids548 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Beta-amylase activity. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan.
Catalytic activity
Activity regulation
Redox regulation; active in reducing conditions, inactive in oxidizing conditions.
pH Dependence
Optimum pH is 6-7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 127 | substrate | ||||
Sequence: D | ||||||
Binding site | 167 | substrate | ||||
Sequence: H | ||||||
Binding site | 175 | substrate | ||||
Sequence: D | ||||||
Active site | 259 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 371 | substrate | ||||
Sequence: K | ||||||
Binding site | 376 | substrate | ||||
Sequence: H | ||||||
Binding site | 418 | substrate | ||||
Sequence: T | ||||||
Active site | 456 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 457-458 | substrate | ||||
Sequence: NA | ||||||
Binding site | 489 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Molecular Function | amylopectin maltohydrolase activity | |
Molecular Function | beta-amylase activity | |
Biological Process | maltose biosynthetic process | |
Biological Process | response to cold | |
Biological Process | starch catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-amylase 3, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO23553
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Slightly retarded growth rate and reduced starch breakdown in leaves during the night.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-49 | Chloroplast | ||||
Sequence: MELTLNSSSSLIKRKDAKSSRNQESSSNNMTFAKMKPPTYQFQAKNSVK | ||||||
Chain | PRO_0000393418 | 50-548 | Beta-amylase 3, chloroplastic | |||
Sequence: EMKFTHEKTFTPEGETLEKWEKLHVLSYPHSKNDASVPVFVMLPLDTVTMSGHLNKPRAMNASLMALKGAGVEGVMVDAWWGLVEKDGPMNYNWEGYAELIQMVQKHGLKLQVVMSFHQCGGNVGDSCSIPLPPWVLEEISKNPDLVYTDKSGRRNPEYISLGCDSVPVLRGRTPIQVYSDFMRSFRERFEGYIGGVIAEIQVGMGPCGELRYPSYPESNGTWRFPGIGEFQCYDKYMKSSLQAYAESIGKTNWGTSGPHDAGEYKNLPEDTEFFRRDGTWNSEYGKFFMEWYSGKLLEHGDQLLSSAKGIFQGSGAKLSGKVAGIHWHYNTRSHAAELTAGYYNTRNHDGYLPIAKMFNKHGVVLNFTCMEMKDGEQPEHANCSPEGLVKQVQNATRQAGTELAGENALERYDSSAFGQVVATNRSDSGNGLTAFTYLRMNKRLFEGQNWQQLVEFVKNMKEGGHGRRLSKEDTTGSDLYVGFVKGKIAENVEEAALV |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in vascular tissue of cotyledons, leaves, petioles, stems, petals, siliques and roots, particularly in phloem, as well as in photosynthetic tissues.
Induction
By cold stress. Light-mediated circadian regulation; highest levels at dawn and at dusk in long days (LD) but only at dusk in short days (SD). Repressed by trehalose in a ABI4-dependent manner, this effect is reversed in the presence of sucrose.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MELTLNSSSSLIKRKDAKSSRNQESSSNNMTFAKMK | ||||||
Compositional bias | 22-36 | Polar residues | ||||
Sequence: NQESSSNNMTFAKMK |
Sequence similarities
Belongs to the glycosyl hydrolase 14 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length548
- Mass (Da)61,353
- Last updated2010-04-20 v3
- ChecksumA5794EDC8427FE30
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 22-36 | Polar residues | ||||
Sequence: NQESSSNNMTFAKMK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ250341 EMBL· GenBank· DDBJ | CAB58423.1 EMBL· GenBank· DDBJ | mRNA | ||
Z97342 EMBL· GenBank· DDBJ | CAB46051.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AL161545 EMBL· GenBank· DDBJ | CAB80980.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002687 EMBL· GenBank· DDBJ | AEE83848.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY052315 EMBL· GenBank· DDBJ | AAK96508.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AY061898 EMBL· GenBank· DDBJ | AAL31225.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AY087592 EMBL· GenBank· DDBJ | AAM65134.1 EMBL· GenBank· DDBJ | mRNA |