Q9S9U6 · 1A111_ARATH

Function

function

1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.

Miscellaneous

The stability of ACS proteins, and the regulation of such stability, play a central role in ethylene biosynthesis.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
25 μMAdoMet
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
25.2 μM/h/mg

pH Dependence

Optimum pH is 8.

Pathway

Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site45substrate
Binding site83substrate

GO annotations

AspectTerm
Molecular Function1-aminocyclopropane-1-carboxylate synthase activity
Molecular Functionpyridoxal phosphate binding
Biological Processethylene biosynthetic process
Biological Processfruit ripening

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1-aminocyclopropane-1-carboxylate synthase 11
  • EC number
  • Short names
    ACC synthase 11
  • Alternative names
    • S-adenosyl-L-methionine methylthioadenosine-lyase 11

Gene names

    • Name
      ACS11
    • ORF names
      T17A2.2
    • Ordered locus names
      At4g08040

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9S9U6

Proteomes

Organism-specific databases

Genome annotation databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001239051-4601-aminocyclopropane-1-carboxylate synthase 11
Modified residue267N6-(pyridoxal phosphate)lysine

Post-translational modification

May be processed at its C-terminus.

Proteomic databases

Expression

Tissue specificity

Expressed in roots.

Induction

By indole-3-acetic acid (IAA) and cycloheximide (CHX).

Gene expression databases

Interaction

Subunit

Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure (By similarity).
Interacts with GRF3

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    460
  • Mass (Da)
    51,799
  • Last updated
    2000-05-01 v1
  • Checksum
    1A056347680E7E2F
MLSSKVVGDSHGQDSSYFLGWQEYEKNPFHESFNTSGIVQMGLAENQLSFDLIEKWLEEHPEVLGLKKNDESVFRQLALFQDYHGLPAFKDAMAKFMGKIRENKVKFDTNKMVLTAGSTSANETLMFCLANPGDAFLIPAPYYPGFDRDLKWRTGVEIVPIHCVSSNGYKITEDALEDAYERALKHNLNVKGVLITNPSNPLGTSTTREELDLLLTFTSTKKIHMVSDEIYSGTVFDSPEFTSVLEVAKDKNMGLDGKIHVVYSLSKDLGLPGFRVGLIYSNNEKVVSAATKMSSFGLISSQTQHLLANLLSDERFTTNYLEENKKRLRERKDRLVSGLKEAGISCLKSNAGLFCWVDLRHLLKSNTFEAEHSLWTKIVCEVGLNISPGSSCHCDEPGWFRVCFANMSDQTMEVAMDRVKGFVDNNNGGKQKRTMWDTRRRSLINKWVSKLSSVTCESER

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF160183
EMBL· GenBank· DDBJ
AAD48074.1
EMBL· GenBank· DDBJ
Genomic DNA
AL161509
EMBL· GenBank· DDBJ
CAB81141.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE82593.1
EMBL· GenBank· DDBJ
Genomic DNA
AF332405
EMBL· GenBank· DDBJ
AAG48768.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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