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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad3thia_ 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

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyPhosphate binding protein-like 8020965 4000229 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyType 2 solute binding protein-like 8033345 3000083 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
Athiaminase_BcmEe3thiA2 A: a/b three-layered sandwichesX: Periplasmic binding protein-like II (From Topology)H: Periplasmic binding protein-like II (From Topology)T: Periplasmic binding protein-like IIF: thiaminase_BcmEECOD (1.6)
ASBP_bac_1_N_1e3thiA3 A: a/b three-layered sandwichesX: Periplasmic binding protein-like II (From Topology)H: Periplasmic binding protein-like II (From Topology)T: Periplasmic binding protein-like IIF: SBP_bac_1_N_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.190.10 Alpha Beta 3-Layer(aba) Sandwich D-Maltodextrin-Binding Protein domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01547Bacterial extracellular solute-binding protein (SBP_bac_1)Bacterial extracellular solute-binding protein- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
PROTEIN (THIAMINASE I)

InterPro: Protein Family Classification InterPro Database Homepage

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

ChainsEnzyme NameDescriptionCatalytic Residues
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]
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