3THI

THIAMINASE I FROM BACILLUS THIAMINOLYTICUS

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3thia_	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	SCOP2 Family	Phosphate binding protein-like	8020965	4000229	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Type 2 solute binding protein-like	8033345	3000083	SCOP2 (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	e3thiA2	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	e3thiA3	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

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	thiaminase (class 1) M-CSA #357	Thiaminase metabolises thiamine into two constituent parts, the pyrimidine unit, with the addition of a nucleophile, and hemineurine. In fern plants thiaminase is thought to provide protection from insect infestation, while in microorganisms and fish, in which the enzyme has also been found there is, as of yet no defined physiological role. Two classes of thiaminase exist, class 1 (EC:2.5.1.2) and class 2 (EC:3.5.99.2). The two classes share no sequence homology, although their catalytic mechanisms are thought to be very similar, utilising the same active site residues. One difference is their substrate specificity: class 1 thiaminases will catalyse the incorporation of several nucleophiles into the departing pyridimium moiety, while class 2 thiaminases will only utilise water as a nucleophile. The substrate divergence is thought to stem from the lack of homology in protein sequence.	Defined by 3 residues: CYS:A-105 [auth A-113]GLU:A-233 [auth A-241]ASP:A-264 [auth A-272] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.5.1.2 (PDB Primary Data) Search M-CSA Motif + EC 2.5.1.2

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.