Reviewed,
UniProtKB/Swiss-Prot Q1QGD4 (RBL1B_NITHX)
Last modified
January 19, 2010.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribulose bisphosphate carboxylase large chain 2 Short name=RuBisCO large subunit 2 EC=4.1.1.39 | ||||
| Gene names |
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| Encoded on | Plasmid 1 | ||||
| Organism | Nitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 323097 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Nitrobacter |
Protein attributes
| Sequence length | 488 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 MF_01338 |
| Catalytic activity | 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01338 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01338 |
| Subunit structure | Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP 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 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 Plasmid |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plastid Inferred from electronic annotation. Source: InterPro |
| 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 488 | 488 | Ribulose bisphosphate carboxylase large chain 2 HAMAP MF_01338 | PRO_0000251447 | |||||
Sites | |||||||||
| Active site | 180 | 1 | Proton acceptor By similarity | ||||||
| Active site | 298 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 206 | 1 | Magnesium; via carbamate group By similarity | ||||||
| Metal binding | 208 | 1 | Magnesium By similarity | ||||||
| Metal binding | 209 | 1 | Magnesium By similarity | ||||||
| Binding site | 128 | 1 | Substrate; in homodimeric partner By similarity | ||||||
| Binding site | 178 | 1 | Substrate By similarity | ||||||
| Binding site | 182 | 1 | Substrate By similarity | ||||||
| Binding site | 299 | 1 | Substrate By similarity | ||||||
| Binding site | 331 | 1 | Substrate By similarity | ||||||
| Binding site | 383 | 1 | Substrate By similarity | ||||||
| Site | 338 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 206 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of plasmid 1 of Nitrobacter hamburgensis X14." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. Richardson P.Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000320 Genomic DNA. Translation: ABE64713.1. |
| RefSeq | YP_571545.1. |
3D structure databases | |
| SMR | Q1QGD4. Positions 26-469. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1QGD4. |
Genome annotation databases | |
| GeneID | 4025375. |
| GenomeReviews | Gene locus Nham_4049 in contig CP000320_GR. |
| KEGG | nha:Nham_4049. |
| NMPDR | fig|323097.3.peg.4094. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1850. |
| HOGENOM | HBG405441. |
| OMA | QYFAYIA. |
Family and domain databases | |
| HAMAP | MF_01338. RuBisCO_L_type1. [Tree] |
| InterPro | IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. 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 | RBL1B_NITHX | ||||||||
| Accession | Primary (citable) accession number: Q1QGD4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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