Q0AHW1 (RBL_NITEC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 47.
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 Short name=RuBisCO large subunit EC=4.1.1.39 | ||||
| Gene names |
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| Organism | Nitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 335283 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas › ![]() |
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-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. |
| 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-Rule MF_01338 |
| 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 |
| 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 473 | 473 | Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338 | PRO_0000299966 | |||||
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
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References
| [1] | "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation." Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X. Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C91. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000450 Genomic DNA. Translation: ABI59071.1. |
| RefSeq | YP_747036.1. NC_008344.1. |
3D structure databases | |
| ProteinModelPortal | Q0AHW1. |
| SMR | Q0AHW1. Positions 16-460. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 335283.Neut_0804. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABI59071; ABI59071; Neut_0804. |
| GeneID | 4272958. |
| KEGG | net:Neut_0804. |
| PATRIC | 22718721. VBINitEut7577_1030. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1850. |
| HOGENOM | HOG000230831. |
| KO | K01601. |
| OMA | YKGRAYA. |
| ProtClustDB | PRK04208. |
Enzyme and pathway databases | |
| BioCyc | NEUT335283:GHT6-850-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 | 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RBL_NITEC | ||||||||
| Accession | Primary (citable) accession number: Q0AHW1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
