P0C916 (RBL1A_THIFE) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 11.
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 large chain 1 Short name=RuBisCO large subunit 1 EC=4.1.1.39 | ||||
| Gene names |
| ||||
| Organism | Thiobacillus ferrooxidans (Acidithiobacillus ferrooxidans) | ||||
| Taxonomic identifier | 920 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus |
Protein attributes
| Sequence length | 473 AA. |
| Sequence status | Complete. |
| 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. 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. HAMAP MF_01338 |
| 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. HAMAP MF_01338 |
| Sequence similarities | Belongs to the RuBisCO large chain family. Type I subfamily. |
| Caution | In T.ferroxidans two similar set of genes code for RuBisCO large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbon dioxide fixation |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plastid Inferred from electronic annotation. Source: InterPro |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activityInferred 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 473 | 473 | Ribulose bisphosphate carboxylase large chain 1 HAMAP MF_01338 | PRO_0000062657 | |||||
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 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans." Kusano T., Takeshima T., Inoue C., Sugawara K. J. Bacteriol. 173:7313-7323(1991) [PubMed: 1718945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Fe1. |
| [2] | "Specific binding of Thiobacillus ferrooxidans RbcR to the intergenic sequence between the rbc operon and the rbcR gene." Kusano T., Sugawara K. J. Bacteriol. 175:1019-1025(1993) [PubMed: 8432695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. Strain: Fe1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D90113 Genomic DNA. Translation: BAA14141.1. D11141 Genomic DNA. Translation: BAA01916.1. |
| PIR | RKBCLT. A41323. |
3D structure databases | |
| ProteinModelPortal | P0C916. |
| SMR | P0C916. Positions 16-460. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_01338. RuBisCO_L_type1. [Tree] |
| InterPro | IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. 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] |
| SUPFAM | SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit. |
| PROSITE | PS00157. RUBISCO_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RBL1A_THIFE | ||||||||
| Accession | Primary (citable) accession number: P0C916 Secondary accession number(s): P28895, Q9X5Z0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with