P07689 (RBS3_PEA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 77.
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: Ribulose bisphosphate carboxylase small chain 3A, chloroplastic Short name=RuBisCO small subunit 3A EC=4.1.1.39 | ||
| Gene names |
| ||
| Organism | Pisum sativum (Garden pea) | ||
| Taxonomic identifier | 3888 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum![]() |
Protein attributes
| Sequence length | 180 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity. |
| Catalytic activity | 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. |
| Subunit structure | 8 large chains + 8 small chains. |
| Subcellular location | |
| Sequence similarities | Belongs to the RuBisCO small chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis |
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological_process | photorespiration Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 57 | 57 | Chloroplast By similarity | ||||||||||||||||||||||||
| Chain | 58 – 180 | 123 | Ribulose bisphosphate carboxylase small chain 3A, chloroplastic | PRO_0000031542 | |||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Beta strand | 63 – 65 | 3 | |||||||||||||||||||||||||
| Turn | 71 – 74 | 4 | |||||||||||||||||||||||||
| Helix | 80 – 92 | 13 | |||||||||||||||||||||||||
| Beta strand | 96 – 104 | 9 | |||||||||||||||||||||||||
| Beta strand | 125 – 128 | 4 | |||||||||||||||||||||||||
| Helix | 138 – 150 | 13 | |||||||||||||||||||||||||
| Beta strand | 154 – 161 | 8 | |||||||||||||||||||||||||
| Beta strand | 163 – 165 | 3 | |||||||||||||||||||||||||
| Beta strand | 167 – 175 | 9 | |||||||||||||||||||||||||
Sequences
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References
| [1] | "Expression dynamics of the pea rbcS multigene family and organ distribution of the transcripts." Fluhr R., Moses P., Morelli G., Coruzzi G., Chua N.-H. EMBO J. 5:2063-2071(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Progress No. 9. |
| [2] | "Synthesis of the small subunit of ribulose-bisphosphate carboxylase from genes cloned into plasmids containing the SP6 promoter." Anderson S., Smith S.M. Biochem. J. 240:709-715(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Identification and characterization of cryptic polyadenylation sites in the 3' region of a pea ribulose-1,5-bisphosphate carboxylase small subunit gene." Hunt A.G. DNA 7:329-336(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-180. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X04333 Genomic DNA. Translation: CAA27864.1. M21375 Genomic DNA. Translation: AAA33683.2. | ||||||||||||
| PIR | RKPMS3. A27874. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P07689. | ||||||||||||
| SMR | P07689. Positions 58-180. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.30.190.10. 1 hit. | ||||||||||||
| InterPro | IPR024681. RuBisCO_sc. IPR000894. RuBisCO_sc_dom. IPR024680. RuBisCO_ssu_N. [Graphical view] | ||||||||||||
| Pfam | PF12338. RbcS. 1 hit. PF00101. RuBisCO_small. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00152. RUBISCOSMALL. | ||||||||||||
| SUPFAM | SSF55239. RuBisCO_small. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RBS3_PEA | ||||||||
| Accession | Primary (citable) accession number: P07689 Secondary accession number(s): P12467 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
