Q9MB95 (1A11_PRUMU) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 59.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 1-aminocyclopropane-1-carboxylate synthase 1 Short name=ACC synthase 1 EC=4.4.1.14 Alternative name(s): S-adenosyl-L-methionine methylthioadenosine-lyase | ||
| Gene names |
| ||
| Organism | Prunus mume (Japanese apricot) (Armeniaca mume) | ||
| Taxonomic identifier | 102107 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Maloideae › Amygdaleae › Prunus |
Protein attributes
| Sequence length | 492 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants. |
| Catalytic activity | S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine. |
| Cofactor | Pyridoxal phosphate. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ethylene biosynthesis Fruit ripening |
| Ligand | Pyridoxal phosphate S-adenosyl-L-methionine |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological process | ethylene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ripeningInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groupsInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Expression of ACC synthase is enhanced earlier than that of ACC oxidase during fruit ripening of mume (Prunus mume)." Mita S., Kirita C., Kato M., Hyodo H. Physiol. Plantarum 107:319-328(1999) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB031026 mRNA. Translation: BAA90549.1. |
3D structure databases | |
| ProteinModelPortal | Q9MB95. |
| SMR | Q9MB95. Positions 12-433. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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. |
| 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 | 1A11_PRUMU | ||||||||
| Accession | Primary (citable) accession number: Q9MB95 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with