taurine dioxygenase complex

GO:1990205 · Other · Multiprotein complex · Proposed

A protein complex capable of catalyzing the conversion of taurine and alpha-ketoglutarate to sulfite, aminoacetaldehyde and succinate under sulfur or cysteine starvation conditions. Its expression is repressed by the presence of sulfate or cysteine. In E. coli it is a homodimer or homotetramer of the protein TauD. [GO:1990205]

Synonyms: 2-aminoethanesulfonate dioxygenase complex; alpha-ketoglutarate-dependent taurine dioxygenase complex; TauD complex

Part of: GO:0005829 — cytosol (no local record)

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Stoichiometry	Essential	Role
alpha-ketoglutarate-dependent taurine dioxygenase TauD	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	tauD	2 copies per E. coli TauD dimer in PDB:1OS7 biological assembly 1	UNKNOWN	Iron- and 2-oxoglutarate-dependent taurine dioxygenase subunit that homooligomerizes to release sulfite from taurine during sulfur starvation. `GO:1990205` GO:1990205 defines the E. coli taurine dioxygenase complex as a TauD homodimer or homotetramer. `UniProtKB:P37610` UniProtKB maps reviewed E. coli K-12 TauD to GO:1990205. `PDB:1OS7` RCSB maps PDB:1OS7 polymer entity 1 to UniProtKB:P37610 and describes the TauD biological assemblies as homodimeric.

Organism-specific protein examples

Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.

alpha-ketoglutarate-dependent taurine dioxygenase TauD

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P37610`	Alpha-ketoglutarate-dependent taurine dioxygenase	tauD	Escherichia coli K-12 (`NCBITaxon:83333`)	REVIEWED
Role and evidence (2 references) Reviewed E. coli K-12 TauD accession for the taurine dioxygenase subunit represented by GO:1990205. `UniProtKB:P37610` UniProtKB P37610 is the reviewed E. coli K-12 entry for TauD. `PMID:9287300` Eichhorn et al. 1997 characterized E. coli TauD as the alpha-ketoglutarate-dependent taurine dioxygenase.

Canonical examples

NCBITaxon:562 Escherichia coli — E. coli source of the ligand-bound homodimeric TauD structure deposited as PDB:1OS7. [PDB:1OS7]

Functions

taurine dioxygenase activity GO:0000908 — The E. coli TauD complex oxidatively converts taurine and 2-oxoglutarate to aminoacetaldehyde, sulfite, succinate, and carbon dioxide.
- GO:0000908 GO:0000908 is the molecular-function term for taurine dioxygenase activity.
- PMID:9287300 Eichhorn et al. 1997 purified and characterized alpha-ketoglutarate-dependent taurine dioxygenase from E. coli.

Physical properties

SUBUNIT_COUNT: 2 (E. coli TauD homodimer in PDB:1OS7 biological assembly 1) [PDB:1OS7]

Discussions

CURATION_TODO (OPEN): Resolve an exact source-neutral family grounding for TauD taurine dioxygenase. The first record represents TauD by its reviewed E. coli gene name and avoids mapping it to InterPro:IPR051323 or InterPro:IPR003819 because those entries also cover non-TauD dioxygenases.
INTERPRETATION (RESOLVED): Should the taurine dioxygenase complex assert one fixed dimer or tetramer stoichiometry? No. GO:1990205 defines E. coli TauD as a homodimer or homotetramer, while PDB:1OS7 contains separate homodimeric biological assemblies. This record cites the PDB-specific dimer measurement but leaves the class-level TauD homo-oligomer boundary flexible.

Evidence

GO:1990205 Gene Ontology cellular-component term for the taurine dioxygenase complex and source of the synonymy.
GO:1990204 GO:1990205 is an is-a descendant of GO:1990204 oxidoreductase complex.
GO:0005829 — cytosol QuickGO reports GO:1990205 as part of the cytosol.
GO:0000908 Gene Ontology molecular-function term for taurine dioxygenase activity.
InterPro:IPR051323 InterPro family entry for alpha-ketoglutarate-dependent sulfate ester dioxygenase-like proteins; this broad family was not used as exact grounding for TauD.
InterPro:IPR003819 InterPro domain entry for the TauD/TfdA-like domain; this broad domain was not used as exact grounding for TauD.
UniProtKB:P37610 UniProtKB reviewed E. coli K-12 TauD entry.
PDB:1OS7 RCSB Protein Data Bank entry for ligand-bound E. coli TauD homodimeric structures.
PMID:9287300 PubMed identifier for Eichhorn et al. 1997, the Journal of Biological Chemistry TauD biochemical characterization paper.
DOI:10.1074/jbc.272.37.23031 DOI for Eichhorn et al. 1997, 'Characterization of alpha-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli'.
PMID:12741810 PubMed identifier for O'Brien et al. 2003, the Biochemistry structural paper cited by GO:1990205 and PDB:1OS7.
DOI:10.1021/bi0341096 DOI for O'Brien et al. 2003, 'Substrate-Induced Conformational Changes in Escherichia coli Taurine/alpha-Ketoglutarate Dioxygenase and Insight into the Oligomeric Structure'.

Curation history

2026-10-01T23:18:05Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-10-01T23:19:41Z codex · EXPANDED_RECORD — Added GO exact and narrow synonymy, GO:1990204 oxidoreductase-complex parentage, cytosol parthood, a reviewed-label-only TauD component with an E. coli K-12 UniProt example, an E. coli PDB:1OS7 homodimer example, taurine dioxygenase activity, PDB-specific dimer subunit count, and PMID/DOI evidence.
2026-10-01T23:20:10Z codex · REFINED_EVIDENCE_SCOPE — Narrowed the E. coli canonical-example note so its PDB:1OS7 reference only supports the ligand-bound homodimeric TauD structure.
2026-10-01T23:36:50Z codex · REFINED_GROUNDING_NOTES — Narrowed TauD grounding notes to the verified broad InterPro entries found during PR review, removing unsupported Pfam and NCBIfam wording.

Source: data/structures/other/taurine_dioxygenase_complex.yaml