5HY1 | pdb_00005hy1

high resolution structure of barbiturase

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5hy1a_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	automated matches	automated matches	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	YjgF-like	8090342	3001733	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	YjgF-like	8090341	3001733	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	YjgF-like	8090340	3001733	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)
A	Amido_AtzD_TrzD_1st	e5hy1A2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: Amido_AtzD_TrzD_1st	ECOD (1.6)
A	Amido_AtzD_TrzD_2nd	e5hy1A3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: Amido_AtzD_TrzD_2nd	ECOD (1.6)
A	Amido_AtzD_TrzD_3rd	e5hy1A1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: Amido_AtzD_TrzD_3rd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1330.170	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
A	3.30.1330.160	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Barbiturase	hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds barbiturase activity cation binding ion binding binding metal ion binding small molecule binding	pyrimidine-containing compound metabolic process catabolic process pyrimidine-containing compound catabolic process uracil metabolic process primary metabolic process pyrimidine nucleobase catabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process uracil catabolic process nucleobase-containing small molecule metabolic process nucleobase catabolic process nucleobase metabolic process small molecule metabolic process metabolic process pyrimidine-containing compound metabolic process catabolic process pyrimidine-containing compound catabolic process uracil metabolic process primary metabolic process pyrimidine nucleobase catabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process uracil catabolic process nucleobase-containing small molecule metabolic process nucleobase catabolic process nucleobase metabolic process small molecule metabolic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR043006	Cyanuric acid hydrolase/Barbiturase, repeating unit B	Homologous Superfamily
A	IPR043007	Cyanuric acid hydrolase/Barbiturase, repeating unit C	Homologous Superfamily
A	IPR014086	Cyanuric acid hydrolase/Barbiturase	Family
A	IPR043008	Cyanuric acid hydrolase/Barbiturase, repeating unit A	Homologous Superfamily

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.