Q46E16 (RBL_METBF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 56.
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 Short name=RuBisCO EC=4.1.1.39 | ||||
| Gene names |
| ||||
| Organism | Methanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 269797 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina › ![]() |
Protein attributes
| Sequence length | 428 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01133 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01133 |
| 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 III RuBisCO are composed solely of large subunits By similarity. HAMAP-Rule MF_01133 |
| Sequence similarities | Belongs to the RuBisCO large chain family. Type III subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbon dioxide fixation |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | carbon fixation Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: HAMAP 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 – 428 | 428 | Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133 | PRO_1000065430 | |||||
Sites | |||||||||
| Active site | 151 | 1 | Proton acceptor By similarity | ||||||
| Active site | 270 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 177 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 179 | 1 | Magnesium By similarity | ||||||
| Metal binding | 180 | 1 | Magnesium By similarity | ||||||
| Binding site | 99 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 153 | 1 | Substrate By similarity | ||||||
| Binding site | 271 | 1 | Substrate By similarity | ||||||
| Binding site | 303 | 1 | Substrate By similarity | ||||||
| Binding site | 354 | 1 | Substrate By similarity | ||||||
| Site | 310 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 177 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes." Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R. J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fusaro / DSM 804. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000099 Genomic DNA. Translation: AAZ69876.1. |
| RefSeq | YP_304456.1. NC_007355.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2D69 based on UniProtKB O58677. |
| ProteinModelPortal | Q46E16. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 269797.Mbar_A0902. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAZ69876; AAZ69876; Mbar_A0902. |
| GeneID | 3625947. |
| KEGG | mba:Mbar_A0902. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1850. |
| HOGENOM | HOG000230831. |
| KO | K01601. |
| OMA | HRAMHAA. |
| ProtClustDB | PRK04208. |
Enzyme and pathway databases | |
| BioCyc | MBAR269797:GHUW-974-MONOMER. |
Family and domain databases | |
| Gene3D | 3.20.20.110. 1 hit. 3.30.70.150. 1 hit. |
| HAMAP | MF_01133. RuBisCO_L_type3. |
| InterPro | IPR017712. RuBisCO_III. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view] |
| 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. |
| TIGRFAMs | TIGR03326. rubisco_III. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RBL_METBF | ||||||||
| Accession | Primary (citable) accession number: Q46E16 | ||||||||
| 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
