Reviewed,
UniProtKB/Swiss-Prot Q9S725 (4CL2_ARATH)
Last modified
February 9, 2010.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 4-coumarate--CoA ligase 2 Short name=4CL 2 EC=6.2.1.12 Alternative name(s): 4-coumarate--CoA ligase isoform 2 Short name=At4CL2 4-coumaroyl-CoA synthase 2 | ||||||
| Gene names |
| ||||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 556 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Produces CoA thioesters of a variety of hydroxy- and methoxy-substituted cinnamic acids, which are used to synthesize several phenylpropanoid-derived compounds, including anthocyanins, flavonoids, isoflavonoids, coumarins, lignin, suberin and wall-bound phenolics. |
| Catalytic activity | ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA. Ref.1 |
| Pathway | |
| Tissue specificity | Preferentially expressed in roots. Ref.1 |
| Induction | By wounding, UV irradiation, and pathogen attack. Ref.1 Ref.11 |
| Domain | Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity. Ref.8 |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
| Biophysicochemical properties | Kinetic parameters: KM=6630 µM for cinnamate KM=252 µM for 4-coumarate KM=20 µM for caffeate |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phenylpropanoid metabolism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phenylpropanoid metabolic process Ref.1 Traceable author statement. Source: TAIR |
| Molecular function | 4-coumarate-CoA ligase activity Ref.1 Inferred from direct assay. Source: TAIR ATP bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 556 | 556 | 4-coumarate--CoA ligase 2 | PRO_0000193028 | |||||
Regions | |||||||||
| Nucleotide binding | 203 – 211 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 346 – 351 | 6 | ATP By similarity | ||||||
| Region | 276 – 345 | 70 | SBD1 | ||||||
| Region | 346 – 413 | 68 | SBD2 | ||||||
Sites | |||||||||
| Binding site | 434 | 1 | ATP By similarity | ||||||
| Binding site | 449 | 1 | ATP By similarity | ||||||
| Binding site | 540 | 1 | ATP By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 211 | 1 | K → S: Drastically reduces the activity. Ref.6 | ||||||
| Mutagenesis | 293 | 1 | M → A or P: Affects the substrate specificity. Ref.7 Ref.10 | ||||||
| Mutagenesis | 320 | 1 | K → L or A: Affects the substrate specificity. Ref.7 Ref.10 | ||||||
| Mutagenesis | 401 | 1 | E → Q: Slighlty reduces the substrate specificity. Ref.6 | ||||||
| Mutagenesis | 403 | 1 | C → A: Significantly reduces the substrate specificity. Ref.6 | ||||||
| Mutagenesis | 449 | 1 | R → Q: Drastically reduces the activity. Ref.6 | ||||||
| Mutagenesis | 457 | 1 | K → S: Drastically reduces the activity. Ref.6 | ||||||
| Mutagenesis | 540 | 1 | K → N: Abolishes the activity. Ref.6 | ||||||
| Sequence conflict | 247 | 1 | L → W in AAD47192. Ref.1 | ||||||
| Sequence conflict | 247 | 1 | L → W in AAD47193. Ref.1 | ||||||
| Sequence conflict | 265 | 1 | V → I in AAD47192. Ref.1 | ||||||
| Sequence conflict | 265 | 1 | V → I in AAD47193. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms." Ehlting J., Buettner D., Wang Q., Douglas C.J., Somssich I.E., Kombrink E. Plant J. 19:9-20(1999) [PubMed: 10417722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION, ENZYME ACTIVITY. Strain: cv. Columbia. |
| [2] | "Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase genes." Lawrence P.K. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. |
| [3] | "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [4] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [5] | "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. Shinozaki K.Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 498-556. Strain: cv. Columbia. |
| [6] | "Mutational analysis of 4-coumarate:CoA ligase identifies functionally important amino acids and verifies its close relationship to other adenylate-forming enzymes." Stuible H.-P., Buettner D., Ehlting J., Hahlbrock K., Kombrink E. FEBS Lett. 467:117-122(2000) [PubMed: 10664468] [Abstract] Cited for: MUTAGENESIS OF LYS-211; GLU-401; CYS-403; ARG-449; LYS-457 AND LYS-540. |
| [7] | "Identification of the substrate specificity-conferring amino acid residues of 4-coumarate:coenzyme A ligase allows the rational design of mutant enzymes with new catalytic properties." Stuible H.-P., Kombrink E. J. Biol. Chem. 276:26893-26897(2001) [PubMed: 11323416] [Abstract] Cited for: MUTAGENESIS OF MET-293 AND LYS-320. |
| [8] | "Identification of 4-coumarate:coenzyme A ligase (4CL) substrate recognition domains." Ehlting J., Shin J.J.K., Douglas C.J. Plant J. 27:455-465(2001) [PubMed: 11576429] [Abstract] Cited for: SUBSTRATE-BINDING DOMAINS. |
| [9] | "Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases." Shockey J.M., Fulda M.S., Browse J. Plant Physiol. 132:1065-1076(2003) [PubMed: 12805634] [Abstract] Cited for: GENE FAMILY ORGANIZATION. |
| [10] | "The substrate specificity-determining amino acid code of 4-coumarate:CoA ligase." Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D., Kombrink E., Stuible H.-P. Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003) [PubMed: 12819348] [Abstract] Cited for: GENE FAMILY ORGANIZATION, SUBSTRATE RECOGNITION SITES, MUTAGENESIS OF MET-293 AND LYS-320. |
| [11] | "Multiple cis-regulatory elements regulate distinct and complex patterns of developmental and wound-induced expression of Arabidopsis thaliana 4CL gene family members." Soltani B.M., Ehlting J., Hamberger B., Douglas C.J. Planta 224:1226-1238(2006) [PubMed: 16738863] [Abstract] Cited for: INDUCTION BY WOUNDING. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF106085 Genomic DNA. Translation: AAD47192.1. AF106086 mRNA. Translation: AAD47193.1. AY376728 mRNA. Translation: AAQ86587.1. AB023045 Genomic DNA. Translation: BAB01716.1. AY099695 mRNA. Translation: AAM20546.1. BT000296 mRNA. Translation: AAN15615.1. AK220883 mRNA. Translation: BAD94282.1. |
| IPI | IPI00526400. |
| RefSeq | NP_188761.1. |
| UniGene | At.57587 |
3D structure databases | |
| SMR | Q9S725. Positions 38-553. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9S725. |
Proteomic databases | |
| PRIDE | Q9S725. |
Genome annotation databases | |
| GeneID | 821678. |
| GenomeReviews | Gene locus AT3G21240 in contig BA000014_GR. |
| KEGG | ath:AT3G21240. |
| NMPDR | fig|3702.1.peg.14358. |
Organism-specific databases | |
| TAIR | At3g21240. |
Phylogenomic databases | |
| HOGENOM | HBG547964. |
| InParanoid | Q9S725. |
| OMA | CFIDAET. |
| PhylomeDB | Q9S725. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:AT3G21240-MONOMER. |
| BRENDA | 6.2.1.12. 302. |
Gene expression databases | |
| ArrayExpress | Q9S725. |
| Genevestigator | Q9S725. |
| GermOnline | AT3G21240. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. [Graphical view] |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | 4CL2_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9S725 Secondary accession number(s): Q53Z06, Q56ZS8, Q9LU35 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


