4THI

THIAMINASE I FROM BACILLUS THIAMINOLYTICUS WITH COVALENTLY BOUND 4-AMINO-2,5-DIMETHYLPYRIMIDINE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
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	d4thia_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Thiaminase I	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Type 2 solute binding protein-like	8033345	3000083	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	thiaminase_BcmE	e4thiA1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: thiaminase_BcmE	ECOD (1.6)
A	SBP_bac_1_N_1	e4thiA2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_N_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01547	Bacterial extracellular solute-binding protein (SBP_bac_1)	Bacterial extracellular solute-binding protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN (THIAMINASE I)	thiamine pyridinylase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	catabolic process alcohol catabolic process pyrimidine-containing compound catabolic process organic hydroxy compound metabolic process thiamine-containing compound metabolic process alcohol metabolic process thiamine metabolic process cellular catabolic process water-soluble vitamin catabolic process small molecule metabolic process sulfur compound metabolic process water-soluble vitamin metabolic process pyrimidine-containing compound metabolic process primary alcohol catabolic process catabolic process alcohol catabolic process pyrimidine-containing compound catabolic process organic hydroxy compound metabolic process thiamine-containing compound metabolic process alcohol metabolic process thiamine metabolic process cellular catabolic process water-soluble vitamin catabolic process small molecule metabolic process sulfur compound metabolic process water-soluble vitamin metabolic process pyrimidine-containing compound metabolic process primary alcohol catabolic process thiamine-containing compound catabolic process vitamin metabolic process vitamin catabolic process sulfur compound catabolic process thiamine catabolic process organic hydroxy compound catabolic process metabolic process cellular process small molecule catabolic process primary alcohol metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR030901	Thiaminase-1	Family
A	IPR054393	Thiaminase-1, insert domain	Domain

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.