Reviewed,
UniProtKB/Swiss-Prot P58348 (RBL1_RHIME)
Last modified
November 3, 2009.
Version 60.
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 Short name=RuBisCO large subunit EC=4.1.1.39 | ||||||
| Gene names |
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| Encoded on | Plasmid pSymB (megaplasmid 2) | ||||||
| Organism | Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 382 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium |
Protein attributes
| Sequence length | 486 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_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 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 |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| Technical term | Complete proteome Plasmid |
| 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 – 486 | 486 | Ribulose bisphosphate carboxylase large chain HAMAP MF_01338 | PRO_0000062643 | |||||
Sites | |||||||||
| Active site | 178 | 1 | Proton acceptor By similarity | ||||||
| Active site | 296 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 204 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 206 | 1 | Magnesium By similarity | ||||||
| Metal binding | 207 | 1 | Magnesium By similarity | ||||||
| Binding site | 126 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 176 | 1 | Substrate By similarity | ||||||
| Binding site | 180 | 1 | Substrate By similarity | ||||||
| Binding site | 297 | 1 | Substrate By similarity | ||||||
| Binding site | 329 | 1 | Substrate By similarity | ||||||
| Binding site | 381 | 1 | Substrate By similarity | ||||||
| Site | 336 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 204 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti." Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A. Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001) [PubMed: 11481431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021. |
Cross-references
Sequence databases | |
|---|---|
| AL591985 Genomic DNA. Translation: CAC48591.1. | |
| PIR | G95865. |
| RefSeq | NP_436731.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BXN based on UniProtKB P09657. |
| SMR | P58348. Positions 14-480. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1236522. |
| GenomeReviews | Gene locus RB0191 in contig AL591985_GR. |
| KEGG | sme:SM_b20198. |
| NMPDR | fig|266834.1.peg.4826. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P58348. |
| OMA | QYFAYIA. |
Enzyme and pathway databases | |
| BioCyc | SMEL266834:SMB20198-MON. |
| BRENDA | 4.1.1.39. 142. |
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 | RBL1_RHIME | ||||||||
| Accession | Primary (citable) accession number: P58348 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
