B7JVW5 (B7JVW5_CYAP8) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 35.
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 | Cyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1)) [Complete proteome] [HAMAP] EMBL ACK65654.1 | ||||||
| Taxonomic identifier | 41431 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Cyanothece![]() |
Protein attributes
| Sequence length | 472 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 in the photorespiration process. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity. HAMAP-Rule MF_01338 |
| Post-translational modification | The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover 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 Photorespiration 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 ACK65654.1 Monooxygenase HAMAP-Rule MF_01338 Oxidoreductase |
| PTM | Disulfide bond HAMAP-Rule MF_01338 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | photorespiration 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: 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 | 172 | 1 | Proton acceptor By similarity HAMAP-Rule MF_01338 | ||||||
| Active site | 291 | 1 | Proton acceptor By similarity HAMAP-Rule MF_01338 | ||||||
| Metal binding | 198 | 1 | Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338 | ||||||
| Metal binding | 200 | 1 | Magnesium By similarity HAMAP-Rule MF_01338 | ||||||
| Metal binding | 201 | 1 | Magnesium By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 120 | 1 | Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 170 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 174 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 292 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 324 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Binding site | 376 | 1 | Substrate By similarity HAMAP-Rule MF_01338 | ||||||
| Site | 331 | 1 | Transition state stabilizer By similarity HAMAP-Rule MF_01338 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 198 | 1 | N6-carboxylysine By similarity HAMAP-Rule MF_01338 | ||||||
| Disulfide bond | 244 | Interchain; in linked form By similarity HAMAP-Rule MF_01338 | |||||||
Sequences
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References
| [1] | "Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria." Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B. MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 8801. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001287 Genomic DNA. Translation: ACK65654.1. |
| RefSeq | YP_002371810.1. NC_011726.1. |
3D structure databases | |
| ProteinModelPortal | B7JVW5. |
| SMR | B7JVW5. Positions 9-466. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 41431.PCC8801_1602. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACK65654; ACK65654; PCC8801_1602. |
| GeneID | 7105640. |
| KEGG | cyp:PCC8801_1602. |
| PATRIC | 21575449. VBICyaSp125535_1757. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1850. |
| HOGENOM | HOG000230831. |
| KO | K01601. |
| OMA | FTQDWAS. |
| ProtClustDB | PRK04208. |
Enzyme and pathway databases | |
| BioCyc | CSP41431:GHLK-1613-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 | B7JVW5_CYAP8 | ||||||||
| Accession | Primary (citable) accession number: B7JVW5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
