P0CG99 (RIR1A_MYCS2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 26.
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 1 EC=1.17.4.1 Alternative name(s): Ribonucleotide reductase R1 subunit 1 | ||||
| Gene names |
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| Organism | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 246196 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 722 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. |
| Miscellaneous | Pupylation of this protein has been demonstrated, although it is unknown if the protein concerned is the product of this gene, of the identical gene MSMEG_2299 (AC P0CH00), or of both genes. |
| Sequence similarities | Belongs to the ribonucleoside diphosphate reductase large chain family. |
| Sequence caution | The sequence ABK71849.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond Isopeptide bond Ubl conjugation |
| 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 – 722 | 722 | Ribonucleoside-diphosphate reductase subunit alpha 1 | PRO_0000396103 | |||||||
Regions | |||||||||||
| Region | 185 – 186 | 2 | Substrate binding By similarity | ||||||||
| Region | 394 – 398 | 5 | Substrate binding By similarity | ||||||||
| Region | 596 – 600 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 394 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 396 | 1 | Cysteine radical intermediate By similarity | ||||||||
| Active site | 398 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 169 | 1 | Substrate By similarity | ||||||||
| Binding site | 214 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Site | 186 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 193 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 223 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 423 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 700 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 701 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 717 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
| Site | 720 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 186 ↔ 423 | Redox-active By similarity | |||||||||
| Cross-link | 310 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [2] | "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?" Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M. Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [3] | "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [4] | "Expansion of the mycobacterial 'PUPylome'." Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V., Barry C.E. III, Bark S., Dorrestein P.C. Mol. Biosyst. 6:376-385(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PUPYLATION AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000480 Genomic DNA. Translation: ABK71849.1. Different initiation. CP001663 Genomic DNA. Translation: AFP37470.1. |
| RefSeq | YP_006565765.1. NC_018289.1. YP_006567006.1. NC_018289.1. YP_885419.1. NC_008596.1. YP_886648.1. NC_008596.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABK71849; ABK71849; MSMEG_1019. |
| GeneID | 13428160. 13428758. 4531391. 4535428. |
| KEGG | msg:MSMEI_0990. msg:MSMEI_2241. msm:MSMEG_1019. msm:MSMEG_2299. |
| PATRIC | 18074490. VBIMycSme59918_1006. |
Phylogenomic databases | |
| HOGENOM | HOG000246165. |
| KO | K00525. |
Enzyme and pathway databases | |
| BioCyc | MSME246196:GJ4Y-1019-MONOMER. MSME246196:GJ4Y-2299-MONOMER. |
| UniPathway | UPA00326. |
Family and domain databases | |
| InterPro | IPR013346. NrdE_NrdA. IPR026459. RNR_1b_NrdE. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR013554. RNR_N. IPR008926. RNR_R1-su_N. [Graphical view] |
| Pfam | PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. PF08343. RNR_N. 1 hit. [Graphical view] |
| PRINTS | PR01183. RIBORDTASEM1. |
| SUPFAM | SSF48168. Ribonucleo_red_N. 1 hit. |
| TIGRFAMs | TIGR02506. NrdE_NrdA. 1 hit. TIGR04170. RNR_1b_NrdE. 1 hit. |
| PROSITE | PS00089. RIBORED_LARGE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RIR1A_MYCS2 | ||||||||
| Accession | Primary (citable) accession number: P0CG99 Secondary accession number(s): A0QR81, I7F7C8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
