Reviewed,
UniProtKB/Swiss-Prot Q42813 (RBL2_GONPO)
Last modified
January 19, 2010.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (1) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Ribulose 1,5-bisphosphate carboxylase, chloroplastic EC=4.1.1.39 | ||
| Gene names |
| ||
| Organism | Gonyaulax polyedra (Dinoflagellate) | ||
| Taxonomic identifier | 2913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Alveolata › Dinophyceae › Gonyaulacales › Gonyaulacaceae › Gonyaulax |
Protein attributes
| Sequence length | 547 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
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. |
| Catalytic activity | 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Plastid › chloroplast Probable. Note: In this organism the plastid is the result of a secondary endosymbiosis event, and thus is found within the endomembrane system, necessitating a complex targeting process 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 II RuBisCO are composed solely of large subunits By similarity. It is not clear if this is the true start of the protein or not; this is probably part of a polyprotein. This may be first cotranslationally imported into the ER up to a stop-transfer signal, so that the N-terminal region of the transit peptide is in the lumen of the ER while the rest of the protein remains in the cytoplasm. Maintaining this topology, proteins are directed to the Golgi and sorted into vesicles that will fuse with the outermost plastid membrane, exposing the transit peptide to the Toc/Tic apparatus, which draws the entire protein across the remaining membranes By similarity. |
| Sequence similarities | Belongs to the RuBisCO large chain family. Type II subfamily. |
| Caution | Note that unlike other eukaryotes, peridinin-containing dinoflagellates have a nuclear-encoded chloroplast-targeted form II RuBisCO. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis |
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase Monooxygenase Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW photorespirationInferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 48 | 48 | Chloroplast Potential | ||||||
| Chain | 49 – 547 | 499 | Ribulose 1,5-bisphosphate carboxylase, chloroplastic | PRO_0000042969 | |||||
Sites | |||||||||
| Active site | 227 | 1 | Proton acceptor By similarity | ||||||
| Active site | 348 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 252 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 254 | 1 | Magnesium By similarity | ||||||
| Metal binding | 255 | 1 | Magnesium By similarity | ||||||
| Binding site | 172 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 229 | 1 | Substrate By similarity | ||||||
| Binding site | 349 | 1 | Substrate By similarity | ||||||
| Binding site | 382 | 1 | Substrate By similarity | ||||||
| Binding site | 429 | 1 | Substrate By similarity | ||||||
| Site | 390 | 1 | Transition state stabilizer | ||||||
Amino acid modifications | |||||||||
| Modified residue | 252 | 1 | N6-carboxylysine | ||||||
Experimental info | |||||||||
| Sequence conflict | 169 – 171 | 3 | SIG → GTS in AAC37234. Ref.1 | ||||||
| Sequence conflict | 286 | 1 | E → A AA sequence Ref.1 | ||||||
| Sequence conflict | 345 | 1 | F → L in AAC37234. Ref.1 | ||||||
| Sequence conflict | 392 | 1 | V → E in AAC37234. Ref.1 | ||||||
| Sequence conflict | 410 | 1 | G → D in AAC37234. Ref.1 | ||||||
| Sequence conflict | 417 | 1 | K → E in AAC37234. Ref.1 | ||||||
| Sequence conflict | 421 | 1 | V → I in AAC37234. Ref.1 | ||||||
| Sequence conflict | 448 | 1 | N → Y in AAA98748. Ref.1 | ||||||
| Sequence conflict | 457 | 1 | T → A AA sequence Ref.1 | ||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "A nuclear-encoded form II RuBisCO in dinoflagellates." Morse D., Salois P., Markovic P., Hastings J.W. Science 268:1622-1624(1995) [PubMed: 7777861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 144-153; 282-304; 375-390 AND 437-461. Strain: 70. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L41063 mRNA. Translation: AAA98748.1. L38610 mRNA. Translation: AAC37234.1. |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.1.1.39. 74655. |
Family and domain databases | |
| InterPro | IPR020878. RuBisCo_large_chain_AS. 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] |
| PROSITE | PS00157. RUBISCO_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RBL2_GONPO | ||||||||
| Accession | Primary (citable) accession number: Q42813 Secondary accession number(s): Q42814 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
