P74240 (RIR1_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 96.
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: Ribonucleoside-diphosphate reductase subunit alpha EC=1.17.4.1 Alternative name(s): Ribonucleotide reductase | ||||
| Gene names |
| ||||
| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 1111708 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 767 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity. |
| Catalytic activity | 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. |
| Enzyme regulation | Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity. |
| Pathway | |
| Subunit structure | Tetramer of two alpha and two beta subunits By similarity. |
| Sequence similarities | Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Allosteric enzyme Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 767 | 767 | Ribonucleoside-diphosphate reductase subunit alpha | PRO_0000187222 | |||||||
Regions | |||||||||||
| Domain | 31 – 120 | 90 | ATP-cone | ||||||||
| Region | 243 – 244 | 2 | Substrate binding By similarity | ||||||||
| Region | 460 – 464 | 5 | Substrate binding By similarity | ||||||||
| Region | 631 – 635 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 460 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 462 | 1 | Cysteine radical intermediate By similarity | ||||||||
| Active site | 464 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 228 | 1 | Substrate By similarity | ||||||||
| Binding site | 272 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Site | 244 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 251 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 281 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 478 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 745 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 746 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 762 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
| Site | 765 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 244 ↔ 478 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000022 Genomic DNA. Translation: BAA18334.1. |
| PIR | S75875. |
| RefSeq | NP_441654.1. NC_000911.1. YP_005651712.1. NC_017277.1. YP_007451536.1. NC_020286.1. |
3D structure databases | |
| ProteinModelPortal | P74240. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P74240. 3 interactions. |
| STRING | 1148.slr1164. |
Proteomic databases | |
| PaxDb | P74240. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAA18334; BAA18334; BAA18334. |
| GeneID | 12254367. 14617199. 954980. |
| KEGG | syn:slr1164. syy:SYNGTS_1759. |
| PATRIC | 23840765. VBISynSp132158_1937. |
Phylogenomic databases | |
| eggNOG | COG0209. |
| HOGENOM | HOG000057034. |
| KO | K00525. |
| OMA | RTHDLFT. |
| ProtClustDB | CLSK893219. |
Enzyme and pathway databases | |
| UniPathway | UPA00326. |
Family and domain databases | |
| InterPro | IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR008926. RNR_R1-su_N. [Graphical view] |
| Pfam | PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 2 hits. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view] |
| PRINTS | PR01183. RIBORDTASEM1. |
| SUPFAM | SSF48168. Ribonucleo_red_N. 1 hit. |
| TIGRFAMs | TIGR02506. NrdE_NrdA. 1 hit. |
| PROSITE | PS51161. ATP_CONE. 1 hit. PS00089. RIBORED_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RIR1_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: P74240 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
