O31875 (NRDEB_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 79.
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 nrdEB subunit alpha EC=1.17.4.1 Alternative name(s): Ribonucleotide reductase large subunit Cleaved into the following chain: | ||||||
| Gene names |
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| Organism | Bacillus subtilis | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 1084 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. |
| Post-translational modification | This protein undergoes protein self-splicing that involves post-translational excision of the intervening region (intein) followed by peptide ligation Probable. |
| Sequence similarities | Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 DOD-type homing endonuclease domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | Autocatalytic cleavage Disulfide bond Protein splicing |
| Technical term | Allosteric enzyme Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | DNA replication Inferred from electronic annotation. Source: UniProtKB-KW intein-mediated protein splicingInferred from electronic annotation. Source: InterPro |
| Cellular component | ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW endonuclease activityInferred from electronic annotation. Source: InterPro ribonucleoside-diphosphate reductase activityInferred 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 – 380 | 380 | Ribonucleoside-diphosphate reductase nrdEB subunit alpha, 1st part | PRO_0000377530 | |||||||
| Chain | 381 – 765 | 385 | Bsu nrdEB intein | PRO_0000377531 | |||||||
| Chain | 766 – 1084 | 319 | Ribonucleoside-diphosphate reductase nrdEB subunit alpha, 2nd part | PRO_0000377532 | |||||||
Regions | |||||||||||
| Domain | 503 – 654 | 152 | DOD-type homing endonuclease | ||||||||
| Region | 168 – 169 | 2 | Substrate binding By similarity | ||||||||
| Region | 964 – 968 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 379 | 1 | Proton acceptor Potential | ||||||||
| Active site | 381 | 1 | Cysteine radical intermediate Potential | ||||||||
| Active site | 768 | 1 | Proton acceptor Potential | ||||||||
| Binding site | 152 | 1 | Substrate By similarity | ||||||||
| Binding site | 197 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Site | 169 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 176 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 206 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 793 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 1067 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 1068 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 1079 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
| Site | 1082 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 169 ↔ 793 | Redox-active By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [2] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO C-TERMINUS. |
| [3] | "An 8 kb nucleotide sequence at the 3' flanking region of the sspC gene (184 degrees) on the Bacillus subtilis 168 chromosome containing an intein and an intron." Ghim S.-Y., Choi S.-K., Shin B.-S., Park S.-H. DNA Res. 5:121-126(1998) [PubMed: 9679200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-1084. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL009126 Genomic DNA. Translation: CAB13898.2. AF012906 Genomic DNA. Translation: AAB92484.1. |
| PIR | H69926. |
| RefSeq | NP_389888.2. NC_000964.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PEQ based on UniProtKB Q08698. |
| ProteinModelPortal | O31875. |
| SMR | O31875. Positions 374-466, 731-766. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000004072; EBBACP00000004072; EBBACG00000004064. |
| GeneID | 939475. |
| GenomeReviews | Gene locus BSU20060 in contig AL009126_GR. |
| KEGG | bsu:BSU20060. |
| PATRIC | 18975859. VBIBacSub10457_2120. |
Organism-specific databases | |
| GenoList | BSU20060. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00050000001799. |
| HOGENOM | HBG348953. |
| OMA | ELDINEM. |
| PhylomeDB | O31875. |
| ProtClustDB | CLSK739693. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU20060-MONOMER. |
Family and domain databases | |
| InterPro | IPR003586. Hedgehog_hint_C. IPR003587. Hedgehog_hint_N. IPR006142. INTEIN. IPR004042. Intein_endonuc. IPR006141. Intein_splice_site. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR008926. Ribnucl_Rdtase_R1-su_N. IPR013554. Ribonucl_Rdtase_N. [Graphical view] |
| KO | K00525. |
| Pfam | PF02867. Ribonuc_red_lgC. 2 hits. PF00317. Ribonuc_red_lgN. 1 hit. PF08343. RNR_N. 1 hit. [Graphical view] |
| PRINTS | PR00379. INTEIN. |
| SMART | SM00305. HintC. 1 hit. SM00306. HintN. 1 hit. [Graphical view] |
| SUPFAM | SSF48168. Ribonucleo_red_N. 1 hit. |
| TIGRFAMs | TIGR01443. Intein_Cterm. 1 hit. TIGR01445. Intein_Nterm. 1 hit. |
| PROSITE | PS50818. INTEIN_C_TER. 1 hit. PS50819. INTEIN_ENDONUCLEASE. 1 hit. PS50817. INTEIN_N_TER. 1 hit. PS00089. RIBORED_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NRDEB_BACSU | ||||||||
| Accession | Primary (citable) accession number: O31875 Secondary accession number(s): Q7BVQ5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Intein-containing proteins List of intein-containing protein entries |
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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