Annotations: 6D3I

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth G]	SCOP2B Superfamily	Clavaminate synthase-like	8080572	3001848	SCOP2B (2022-06-29)
C [auth D]	SCOP2B Superfamily	Clavaminate synthase-like	8080572	3001848	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Clavaminate synthase-like	8080572	3001848	SCOP2B (2022-06-29)
D [auth J]	SCOP2B Superfamily	Clavaminate synthase-like	8080572	3001848	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth G]	TauD	e6d3iG1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)
C [auth D]	TauD	e6d3iD1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)
A	TauD	e6d3iA1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)
D [auth J]	TauD	e6d3iJ1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth G]	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)
C [auth D]	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)
A	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)
D [auth J]	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth G], C [auth D], D [auth J]	PF02668	Taurine catabolism dioxygenase TauD, TfdA family (TauD)	Taurine catabolism dioxygenase TauD, TfdA family	This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli Swiss:P37610 is a alpha-ketoglutarate-dependent taurine dioxygenase [1]. This enzyme catalyses the oxygenolytic release of sulfite from taurine [1]. ...	This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli Swiss:P37610 is a alpha-ketoglutarate-dependent taurine dioxygenase [1]. This enzyme catalyses the oxygenolytic release of sulfite from taurine [1]. TfdA from Burkholderia sp. Swiss:Q45423 is a 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase [2]. TfdA from Alcaligenes eutrophus JMP134 Swiss:P10088 is a 2,4-dichlorophenoxyacetate monooxygenase [3]. Also included are gamma-Butyrobetaine hydroxylase enzymes EC:1.14.11.1 [4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth G], C [auth D], D [auth J]	ftv7 dioxygenase	oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen 2-oxoglutarate-dependent dioxygenase activity catalytic activity dioxygenase activity cation binding ion binding binding metal ion binding small molecule binding	catabolic process metabolic process cellular process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth G], C [auth D], D [auth J]	IPR003819	TauD/TfdA-like domain	Domain
A, B [auth G], C [auth D], D [auth J]	IPR042098	Taurine dioxygenase TauD-like superfamily	Homologous Superfamily
A, B [auth G], C [auth D], D [auth J]	IPR051323	Alpha-ketoglutarate-dependent sulfate ester dioxygenase-like	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.