F7YAX8 (F7YAX8_MESOW) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 13.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338 Short name=RuBisCO large subunit HAMAP-Rule MF_01338 EC=4.1.1.39 HAMAP-Rule MF_01338 | ||||
| Gene names |
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| Organism | Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 536019 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium › ![]() |
Protein attributes
| Sequence length | 487 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-Rule MF_01338 |
| Catalytic activity | 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338 |
| Subunit structure | Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338 |
| 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-Rule MF_01338 |
| Sequence similarities | Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle HAMAP-Rule MF_01338 Carbon dioxide fixation HAMAP-Rule MF_01338 Photosynthesis HAMAP-Rule MF_01338 |
| Ligand | Magnesium HAMAP-Rule MF_01338 Metal-binding HAMAP-Rule MF_01338 |
| Molecular function | Lyase HAMAP-Rule MF_01338 EMBL AEH89954.1 Monooxygenase HAMAP-Rule MF_01338 Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | reductive pentose-phosphate cycle 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 178 | 1 | Proton acceptor By similarity HAMAP-Rule MF_01338 | ||||||
| Active site | 296 | 1 | Proton acceptor By similarity HAMAP-Rule MF_01338 | ||||||
| Metal binding | 204 | 1 | Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338 | ||||||
| Metal binding | 206 | 1 | Magnesium By similarity HAMAP-Rule MF_01338 | ||||||
| Metal binding | 207 | 1 | Magnesium By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 126 | 1 | Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 176 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 180 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 297 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 329 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 381 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Site | 336 | 1 | Transition state stabilizer By similarity HAMAP-Rule MF_01338 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 204 | 1 | N6-carboxylysine By similarity HAMAP-Rule MF_01338 | ||||||
Sequences
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References
| [1] | "Complete sequence of Mesorhizobium opportunistum WSM2075." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P. Woyke T.Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LMG 24607 / HAMBI 3007 / WSM2075. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002279 Genomic DNA. Translation: AEH89954.1. |
| RefSeq | YP_004614048.1. NC_015675.1. |
3D structure databases | |
| ProteinModelPortal | F7YAX8. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEH89954; AEH89954; Mesop_5541. |
| GeneID | 10829406. |
| KEGG | mop:Mesop_5541. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K01601. |
Enzyme and pathway databases | |
| BioCyc | MOPP536019:GH56-5602-MONOMER. |
Family and domain databases | |
| Gene3D | 3.20.20.110. 1 hit. 3.30.70.150. 1 hit. |
| HAMAP | MF_01338. RuBisCO_L_type1. |
| InterPro | IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. 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. |
| PROSITE | PS00157. RUBISCO_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | F7YAX8_MESOW | ||||||||
| Accession | Primary (citable) accession number: F7YAX8 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
