Q43309 (1A14_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 1-aminocyclopropane-1-carboxylate synthase 4 Short name=ACC synthase 4 EC=4.4.1.14 Alternative name(s): S-adenosyl-L-methionine methylthioadenosine-lyase 4 | ||||||||
| Gene names |
| ||||||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Protein attributes
| Sequence length | 474 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. |
| Catalytic activity | S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine. Ref.7 |
| Cofactor | Pyridoxal phosphate. |
| Pathway | |
| Subunit structure | Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure By similarity. Interacts with XBAT32. Interacts (via its C-terminal region) with ETO1 and EOL1. Ref.8 Ref.9 |
| Tissue specificity | Expressed in roots, leaves and flowers. Ref.1 |
| Induction | By indole-3-acetic acid (IAA) and cycloheximide (CHX). By auxin. Ref.1 Ref.7 |
| Post-translational modification | Ubiquitinated by XBAT32. Ubiquitination probably leads to its subsequent degradation, thus controlling ethylene production. Ref.9 |
| Miscellaneous | The stability of ACS proteins, and the regulation of such stability, play a central role in ethylene biosynthesis. |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
| Biophysicochemical properties | Kinetic parameters: KM=15 µM for AdoMet Vmax=31.20 µM/h/mg enzyme pH dependence: Optimum pH is 7.8. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ethylene biosynthesis Fruit ripening |
| Ligand | Pyridoxal phosphate S-adenosyl-L-methionine |
| Molecular function | Lyase |
| PTM | Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cellular response to iron ion Inferred from expression pattern. Source: TAIR ethylene biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW ripeningInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 1-aminocyclopropane-1-carboxylate synthase activity Inferred from direct assay Ref.7. Source: TAIR identical protein bindingInferred from physical interaction. Source: IntAct pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 2 | EBI-2436015,EBI-2436015 | ||
| ACS6 | Q9SAR0 | 2 | EBI-2436015,EBI-2356658 | |
| ACS7 | Q9STR4 | 4 | EBI-2436015,EBI-2356842 | |
| ACS8 | Q9T065 | 2 | EBI-2436015,EBI-2357693 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 474 | 474 | 1-aminocyclopropane-1-carboxylate synthase 4 | PRO_0000123898 | |||||
Sites | |||||||||
| Binding site | 47 | 1 | Substrate By similarity | ||||||
| Binding site | 85 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 273 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "ACS4, a primary indoleacetic acid-responsive gene encoding 1-aminocyclopropane-1-carboxylate synthase in Arabidopsis thaliana. Structural characterization, expression in Escherichia coli, and expression characteristics in response to auxin." Abel S., Nguyen M.D., Chow W., Theologis A. J. Biol. Chem. 270:19093-19099(1995) [PubMed: 7642574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia. |
| [2] | Erratum Abel S., Nguyen M.D., Chow W., Theologis A. J. Biol. Chem. 270:26020-26020(1995) |
| [3] | "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C.Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [4] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [5] | "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. |
| [6] | "The 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis thaliana." Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A. Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992) [PubMed: 1438312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 50-81. |
| [7] | "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate synthase isozymes encoded by the Arabidopsis gene family." Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., Theologis A. J. Biol. Chem. 278:49102-49112(2003) [PubMed: 12968022] [Abstract] Cited for: ENZYME ACTIVITY, INDUCTION. |
| [8] | "The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate ethylene biosynthesis in Arabidopsis by controlling type-2 ACC synthase levels." Christians M.J., Gingerich D.J., Hansen M., Binder B.M., Kieber J.J., Vierstra R.D. Plant J. 57:332-345(2009) [PubMed: 18808454] [Abstract] Cited for: INTERACTION WITH ETO1 AND EOL1. |
| [9] | "Arabidopsis RING E3 ligase XBAT32 regulates lateral root production through its role in ethylene biosynthesis." Prasad M.E., Schofield A., Lyzenga W., Liu H., Stone S.L. Plant Physiol. 153:1587-1596(2010) [PubMed: 20511490] [Abstract] Cited for: INTERACTION WITH XBAT32, UBIQUITINATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U23481 mRNA. Translation: AAC49037.1. U23482 Genomic DNA. Translation: AAA85039.1. AC004786 Genomic DNA. Translation: AAC32428.1. AC005617 Genomic DNA. Translation: AAM15065.1. CP002685 Genomic DNA. Translation: AEC07360.1. AF332404 mRNA. Translation: AAG48767.1. |
| IPI | IPI00519589. |
| PIR | B84617. G46376. |
| RefSeq | NP_179866.1. NM_127846.1. |
| UniGene | At.1549. |
3D structure databases | |
| ProteinModelPortal | Q43309. |
| SMR | Q43309. Positions 4-431. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q43309. 7 interactions. |
| STRING | Q43309. |
Proteomic databases | |
| PRIDE | Q43309. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT2G22810.1; AT2G22810.1; AT2G22810. |
| GeneID | 816812. |
| GenomeReviews | Gene locus AT2G22810 in contig CT485783_GR. |
| KEGG | ath:AT2G22810. |
| NMPDR | fig|3702.1.peg.9299. |
Organism-specific databases | |
| GeneFarm | 4050. |
| TAIR | At2g22810. |
Phylogenomic databases | |
| eggNOG | KOG0256. |
| GeneTree | EPGT00070000028140. |
| HOGENOM | HBG317030. |
| InParanoid | Q43309. |
| OMA | SSCHCEE. |
| PhylomeDB | Q43309. |
| ProtClustDB | PLN02450. |
Gene expression databases | |
| ArrayExpress | Q43309. |
| Genevestigator | Q43309. |
| GermOnline | AT2G22810. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits. |
| KO | K01762. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| PRINTS | PR00753. ACCSYNTHASE. |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| PROSITE | PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | 1A14_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q43309 Secondary accession number(s): Q9S9C4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
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 |

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