Q9LQ12 · 4CLL1_ARATH

Function

function

Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site189ATP (UniProtKB | ChEBI)
Binding site190ATP (UniProtKB | ChEBI)
Binding site191ATP (UniProtKB | ChEBI)
Binding site192ATP (UniProtKB | ChEBI)
Binding site193ATP (UniProtKB | ChEBI)
Binding site197ATP (UniProtKB | ChEBI)
Binding site237(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site258CoA (UniProtKB | ChEBI)
Binding site309(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site331(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site331ATP (UniProtKB | ChEBI)
Binding site332(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site332ATP (UniProtKB | ChEBI)
Binding site336(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site336ATP (UniProtKB | ChEBI)
Binding site420ATP (UniProtKB | ChEBI)
Binding site435ATP (UniProtKB | ChEBI)
Binding site437(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site441(E)-4-coumaroyl-AMP (UniProtKB | ChEBI)
Binding site443CoA (UniProtKB | ChEBI)
Binding site444CoA (UniProtKB | ChEBI)
Binding site526ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum
Molecular FunctionATP binding
Molecular Functionlong-chain fatty acid-CoA ligase activity
Molecular Functionmedium-chain fatty acid-CoA ligase activity
Biological Processfatty-acyl-CoA biosynthetic process
Biological Processpollen development
Biological Processsporopollenin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-coumarate--CoA ligase-like 1
  • EC number
  • Alternative names
    • 4-coumarate--CoA ligase isoform 10 (At4CL10)

Gene names

    • Name
      4CLL1
    • Synonyms
      ACOS5
    • ORF names
      F16P17.9
    • Ordered locus names
      At1g62940

Organism names

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

Accessions

  • Primary accession
    Q9LQ12

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002991741-5424-coumarate--CoA ligase-like 1

Proteomic databases

Expression

Tissue specificity

Mostly confined to anther tapetal cells.

Gene expression databases

Interaction

Subunit

Interacts with TKPR1, PKSA and PKSB.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9LQ12PKSA O236743EBI-30859465, EBI-30859485
BINARY Q9LQ12PKSB Q8LDM24EBI-30859465, EBI-30859537
BINARY Q9LQ12TKPR1 Q500U83EBI-30859465, EBI-4432350

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region260-331SBD1
Region332-399SBD2

Domain

Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    542
  • Mass (Da)
    59,169
  • Last updated
    2000-10-01 v1
  • Checksum
    8F055B6A1E0DF85B
MESQKQEDNEYIFRSLYPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKILSINKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY250836
EMBL· GenBank· DDBJ
AAP03019.1
EMBL· GenBank· DDBJ
mRNA
AY376734
EMBL· GenBank· DDBJ
AAQ86593.1
EMBL· GenBank· DDBJ
mRNA
AC011000
EMBL· GenBank· DDBJ
AAF75805.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE34025.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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