Reviewed,
UniProtKB/Swiss-Prot Q07N61 (RBL2_RHOP5)
Last modified
November 3, 2009.
Version 27.
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 Short name=RuBisCO EC=4.1.1.39 | ||||
| Gene names |
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| Organism | Rhodopseudomonas palustris (strain BisA53) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 316055 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas |
Protein attributes
| Sequence length | 460 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. 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_01339 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01339 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Miscellaneous | The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity. |
| Sequence similarities | Belongs to the RuBisCO large chain family. Type II subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbon dioxide fixation Photosynthesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 460 | 460 | Ribulose bisphosphate carboxylase HAMAP MF_01339 | PRO_1000067650 | |||||
Sites | |||||||||
| Active site | 167 | 1 | Proton acceptor By similarity | ||||||
| Active site | 288 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 192 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 194 | 1 | Magnesium By similarity | ||||||
| Metal binding | 195 | 1 | Magnesium By similarity | ||||||
| Binding site | 112 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 169 | 1 | Substrate By similarity | ||||||
| Binding site | 289 | 1 | Substrate By similarity | ||||||
| Binding site | 322 | 1 | Substrate By similarity | ||||||
| Binding site | 369 | 1 | Substrate By similarity | ||||||
| Site | 330 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 192 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Rhodopseudomonas palustris BisA53." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. Richardson P.Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000463 Genomic DNA. Translation: ABJ06623.1. | |
| RefSeq | YP_781603.1. |
3D structure databases | |
| SMR | Q07N61. Positions 2-458. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q07N61. |
Genome annotation databases | |
| GeneID | 4360364. |
| GenomeReviews | Gene locus RPE_2686 in contig CP000463_GR. |
| KEGG | rpe:RPE_2686. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q07N61. |
| OMA | LRLPGFF. |
Family and domain databases | |
| HAMAP | MF_01339. [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 | RBL2_RHOP5 | ||||||||
| Accession | Primary (citable) accession number: Q07N61 | ||||||||
| 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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