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AMY3 alpha-amylase-like 3 [ Arabidopsis thaliana (thale cress) ]

Gene ID: 843319, updated on 18-Sep-2024

Summary

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Official Symbol
AMY3
Official Full Name
alpha-amylase-like 3
Primary source
TAIR:AT1G69830
Locus tag
AT1G69830
See related
Araport:AT1G69830
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Arabidopsis thaliana (ecotype: Columbia)
Lineage
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Also known as
alpha-amylase-like 3; ALPHA-AMYLASE-LIKE 3; ATAMY3; T17F3.14; T17F3_14
Summary
Encodes a plastid-localized alpha-amylase. Expression is reduced in the SEX4 mutant. Loss of function mutations show normal diurnal pattern of starch accumulation/degradation. Expression follows circadian rhythms.
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Genomic context

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See AMY3 in Genome Data Viewer
Location:
chromosome: 1
Exon count:
13
Sequence:
Chromosome: 1; NC_003070.9 (26288228..26293173, complement)

Chromosome 1 - NC_003070.9Genomic Context describing neighboring genes Neighboring gene defensin-like protein Neighboring gene Defensin-like (DEFL) family protein Neighboring gene SPFH/Band 7/PHB domain-containing membrane-associated protein family Neighboring gene nitrate transporter 1:2

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003070.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic α-amylase. Seung D, et al. J Biol Chem, 2013 Nov 22. PMID 24089528, Free PMC Article
  2. The simultaneous abolition of three starch hydrolases blocks transient starch breakdown in Arabidopsis. Streb S, et al. J Biol Chem, 2012 Dec 7. PMID 23019330, Free PMC Article
  3. Regulation of Leaf Starch Degradation by Abscisic Acid Is Important for Osmotic Stress Tolerance in Plants. Thalmann M, et al. Plant Cell, 2016 Aug. PMID 27436713, Free PMC Article
  4. alpha-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves. Yu TS, et al. J Biol Chem, 2005 Mar 18. PMID 15637061
  5. Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase. Streb S, et al. Plant Cell, 2008 Dec. PMID 19074683, Free PMC Article

See all (11) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Study demonstrate that abscisic acid controls the activity of BAM1 and AMY3 in leaves under osmotic stress through the AREB/ABF-SnRK2 kinase-signaling pathway. We propose that differential regulation and isoform subfunctionalization define starch-adaptive plasticity, ensuring an optimal carbon supply for continued growth under an ever-changing environment.
    Title: Regulation of Leaf Starch Degradation by Abscisic Acid Is Important for Osmotic Stress Tolerance in Plants.
  2. Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic alpha-amylase.
    Title: Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic α-amylase.
  3. The additional loss of the chloroplastic alpha-amylase AMY3 partially reverts the phenotype of the quadruple DBE mutant, restoring starch granule biosynthesis.
    Title: Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase.
  4. alpha-amylase is not necessary for transitory starch breakdown in Arabidopsis leaves [AtAMY3]
    Title: alpha-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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NM_105651.5

Gene Ontology Provided by TAIR

Function Evidence Code Pubs
enables alpha-amylase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables alpha-amylase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables calcium ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within starch catabolic process TAS
Traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
located_in chloroplast HDA PubMed 
located_in chloroplast IDA
Inferred from Direct Assay
more info
 PubMed 
located_in chloroplast stroma HDA PubMed 
located_in extracellular region ISM
Inferred from Sequence Model
more info
  

General protein information

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Preferred Names
alpha-amylase-like 3
NP_564977.1
  • alpha-amylase-like 3 (AMY3); FUNCTIONS IN: alpha-amylase activity; INVOLVED IN: circadian rhythm, starch catabolic process; LOCATED IN: chloroplast stroma, chloroplast; EXPRESSED IN: 24 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Glycoside hydrolase, catalytic core (InterPro:IPR017853), Glycoside hydrolase, subgroup, catalytic core (InterPro:IPR013781), Glycosyl hydrolase, family 13, catalytic domain (InterPro:IPR006047), Alpha-amylase, C-terminal beta-sheet (InterPro:IPR012850); BEST Arabidopsis thaliana protein match is: alpha-amylase-like 2 (TAIR:AT1G76130.1); Has 11240 Blast hits to 11194 proteins in 2094 species: Archae - 95; Bacteria - 8555; Metazoa - 677; Fungi - 729; Plants - 646; Viruses - 0; Other Eukaryotes - 538 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003070.9 Reference assembly

    Range
    26288228..26293173 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_105651.5 → NP_564977.1  alpha-amylase-like 3 [Arabidopsis thaliana]

    See identical proteins and their annotated locations for NP_564977.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    Q94A41, Q9CAR6
    UniProtKB/TrEMBL
    A0A178WGF4, A0A5S9WTP4, A0A654EP66
    Conserved Domains (1) summary
    PLN02784
    Location:1 → 887
    PLN02784; alpha-amylase
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q94A41.1

Gene LinkOut

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