Reviewed,
UniProtKB/Swiss-Prot P22859 (RBL1B_CHRVI)
Last modified
March 24, 2009.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribulose bisphosphate carboxylase large chain 2 Short name=RuBisCO large subunit 2 EC=4.1.1.39 | ||||
| Gene names |
| ||||
| Organism | Chromatium vinosum (Allochromatium vinosum) | ||||
| Taxonomic identifier | 1049 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium |
Protein attributes
| Sequence length | 471 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. HAMAP MF_01338 |
| 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. |
| 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. |
| Caution | In C.vinosum two similar set of genes code for RuBisCO large and small chains: the rbcL-rbcS and the rbcA-rbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbon dioxide fixation Photosynthesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycleInferred from electronic annotation. Source: UniProtKB-KW |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 471 | 470 | Ribulose bisphosphate carboxylase large chain 2 HAMAP MF_01338 | PRO_0000062622 | |||||
Sites | |||||||||
| Active site | 168 | 1 | Proton acceptor By similarity | ||||||
| Active site | 287 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 194 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 196 | 1 | Magnesium By similarity | ||||||
| Metal binding | 197 | 1 | Magnesium By similarity | ||||||
| Binding site | 116 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 166 | 1 | Substrate By similarity | ||||||
| Binding site | 170 | 1 | Substrate By similarity | ||||||
| Binding site | 288 | 1 | Substrate By similarity | ||||||
| Binding site | 320 | 1 | Substrate By similarity | ||||||
| Binding site | 372 | 1 | Substrate By similarity | ||||||
| Site | 327 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 194 | 1 | N6-carboxylysine By similarity | ||||||
| Disulfide bond | 240 | Interchain; in linked form By similarity | |||||||
Sequences
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References
| [1] | "Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum." Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K., Kobayashi K., Sugiura M. Gene 97:55-62(1991) [PubMed: 1899846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / D. |
| [2] | "Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum." Viale A.M., Kobayashi H., Akazawa T. J. Biol. Chem. 265:18386-18392(1990) [PubMed: 2211708] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26. |
Cross-references
Sequence databases | |
|---|---|
| D90204 Genomic DNA. Translation: BAA14229.1. | |
| PIR | RKKRL2. JQ0586. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GEH based on UniProtKB O93627. |
| SMR | P22859. Positions 5-467, 6-468. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.1.1.39. 2799. |
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 | RBL1B_CHRVI | ||||||||
| Accession | Primary (citable) accession number: P22859 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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