exodeoxyribonuclease V complex
Exodeoxyribonuclease V complex is a RecB-RecC-RecD enzyme complex that combines ATP-dependent DNA unwinding with exonucleolytic cleavage of DNA to produce 5'-phosphooligonucleotides. [GO:0009338]
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| RecBCD enzyme subunit RecB | Protein | part of | InterPro:IPR004586 | recB | RecB helicase-nuclease subunit of the exodeoxyribonuclease V complex.
| ||
| RecBCD enzyme subunit RecC | Protein | part of | InterPro:IPR006697 | recC | RecC subunit of the exodeoxyribonuclease V complex.
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| RecBCD enzyme subunit RecD | Protein | part of | InterPro:IPR006344 | recD | RecD helicase subunit of the exodeoxyribonuclease V complex.
|
Canonical examples
NCBITaxon:562Escherichia coli — Bacterial source of the RecB, RecC, and RecD subunits in the RecBCD:DNA crystal structure deposited as PDB:1W36. [PDB:1W36]
Functions
- exodeoxyribonuclease V activity
GO:0008854— RecBCD catalyzes ATP-dependent exonucleolytic cleavage of DNA to yield 5'-phosphooligonucleotides.GO:0008854GO:0008854 defines exodeoxyribonuclease V activity as ATP-dependent exonucleolytic DNA cleavage in either polarity to yield 5'-phosphooligonucleotides.InterPro:IPR006697InterPro describes the RecBCD enzyme as a multisubunit enzyme composed of RecB, RecC, and RecD.PDB:1W36PDB:1W36 contains the E. coli RecB, RecC, and RecD subunits bound to a DNA hairpin polymer entity.
Mechanism graphs
RecBCD processes DNA ends (FUNCTION)
The RecBCD complex uses its RecB, RecC, and RecD subunits to bind DNA and carry out the ATP-dependent exodeoxyribonuclease V reaction.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| exodeoxyribonuclease V complex | enables | exodeoxyribonuclease V activity |
|
| RecBCD enzyme subunit RecB | contributes to | exodeoxyribonuclease V activity |
|
| RecBCD enzyme subunit RecC | contributes to | exodeoxyribonuclease V activity |
|
| RecBCD enzyme subunit RecD | contributes to | exodeoxyribonuclease V activity |
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| exodeoxyribonuclease V complex | binds | DNA end |
|
| DNA end | is cleaved by | exodeoxyribonuclease V activity |
|
| exodeoxyribonuclease V activity | produces | 5'-phosphooligonucleotides |
|
Evidence
GO:0009338Gene Ontology cellular-component term for the exodeoxyribonuclease V complex.GO:0140535Gene Ontology cellular-component term for intracellular protein-containing complexes.GO:1902494Gene Ontology cellular-component term for catalytic complexes.GO:0008854Gene Ontology molecular-function term for exodeoxyribonuclease V activity.InterPro:IPR004586InterPro family for RecBCD enzyme subunit RecB.InterPro:IPR006697InterPro family for RecBCD enzyme subunit RecC.InterPro:IPR006344InterPro family for RecBCD enzyme subunit RecD.DOI:10.1038/nature02988Singleton et al. 2004, Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks, Nature.PMID:15538360PubMed identifier for Singleton et al. 2004 as reported by RCSB PDB:1W36 and NCBI ESummary.PMID:1618858PubMed identifier for Masterson et al. 1992, the reconstitution study cited by the GO:0009338 definition.PDB:1W36RCSB Protein Data Bank entry for the Escherichia coli RecBCD:DNA crystal structure from Singleton et al. 2004.
Curation history
2026-09-24T08:53:21Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-24T08:54:37Zcodex · EXPANDED_RECORD — Added RecBCD synonymy and GO catalytic-complex parentage, RecB/C/D components grounded to exact InterPro families and PDB:1W36 polymer entities, an Escherichia coli canonical example, exodeoxyribonuclease V activity evidence, and a compact DNA-processing function graph.2026-09-24T08:55:19Zcodex · TIGHTENED_WORDING — Removed broad bacterial wording from RecB, RecC, and RecD role prose while retaining the Escherichia coli canonical example.2026-09-24T09:05:42Zcodex · ADDRESS_REVIEW — #1472/#1473: removed weak RecBCD exact synonymy and removed unsupported assembly-essentiality assertions from the RecB, RecC, and RecD component rows.
Source: data/structures/other/exodeoxyribonuclease_v_complex.yaml