Reviewed,
UniProtKB/Swiss-Prot P24671 (RBL_ABIMA)
Last modified
June 16, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (1) |
 Third-party data |
 Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Ribulose bisphosphate carboxylase large chain Short name=RuBisCO large subunit EC=4.1.1.39 | ||
| Gene names |
| ||
| Encoded on | Plastid; Chloroplast | ||
| Organism | Abies magnifica (Red fir) | ||
| Taxonomic identifier | 3320 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Coniferopsida › Coniferales › Pinaceae › Abies |
Protein attributes
| Sequence length | 475 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
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 in the photorespiration process. 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. HAMAP MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01338 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subunit structure | Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity. |
| Subcellular location | |
| Post-translational modification | The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity. |
| Miscellaneous | The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity. |
| Sequence similarities | Belongs to the RuBisCO large chain family. Type I subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis |
| Cellular component | Chloroplast Plastid |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| PTM | Acetylation Disulfide bond Methylation |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW photorespirationInferred 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 | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monooxygenase activityInferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 2 | 2 | By similarity | PRO_0000031099 | |||||
| Chain | 3 – 475 | 473 | Ribulose bisphosphate carboxylase large chain HAMAP MF_01338 | PRO_0000031100 | |||||
Sites | |||||||||
| Active site | 175 | 1 | Proton acceptor By similarity | ||||||
| Active site | 294 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 201 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 203 | 1 | Magnesium By similarity | ||||||
| Metal binding | 204 | 1 | Magnesium By similarity | ||||||
| Binding site | 123 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 173 | 1 | Substrate By similarity | ||||||
| Binding site | 177 | 1 | Substrate By similarity | ||||||
| Binding site | 295 | 1 | Substrate By similarity | ||||||
| Binding site | 327 | 1 | Substrate By similarity | ||||||
| Binding site | 379 | 1 | Substrate By similarity | ||||||
| Site | 334 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 3 | 1 | N-acetylproline By similarity | ||||||
| Modified residue | 14 | 1 | N6,N6,N6-trimethyllysine By similarity | ||||||
| Modified residue | 201 | 1 | N6-carboxylysine By similarity | ||||||
| Disulfide bond | 247 | Interchain; in linked form By similarity | |||||||
Sequences
| ||||||||||||||||||
References
| [1] | Doerksen A.H., Strauss S., Price R. Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| X58391 Genomic DNA. Translation: CAA41280.1. | |
| PIR | RKKHLR. S14869. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1RBL based on UniProtKB P00880. |
| SMR | P24671. Positions 11-475. |
| ModBase | Search... |
Family and domain databases | |
| HAMAP | MF_01338. [Tree] |
| InterPro | IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view] |
| Gene3D | G3DSA:3.20.20.110. RuBisCO_large. 1 hit. G3DSA:3.30.70.150. RuBisCO_large. 1 hit. |
| Pfam | PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view] |
| PROSITE | PS00157. RUBISCO_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RBL_ABIMA | ||||||||
| Accession | Primary (citable) accession number: P24671 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
