Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATPP_enzyme_Me2uz1A1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: DHS-like NAD/FAD-binding domainF: TPP_enzyme_MECOD (1.6)
ATPP_enzyme_Ce2uz1A2 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_CECOD (1.6)
ATPP_enzyme_Ne2uz1A3 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_NECOD (1.6)
DTPP_enzyme_Me2uz1D1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: DHS-like NAD/FAD-binding domainF: TPP_enzyme_MECOD (1.6)
DTPP_enzyme_Ce2uz1D2 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_CECOD (1.6)
DTPP_enzyme_Ne2uz1D3 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_NECOD (1.6)
CTPP_enzyme_Me2uz1C1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: DHS-like NAD/FAD-binding domainF: TPP_enzyme_MECOD (1.6)
CTPP_enzyme_Ce2uz1C2 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_CECOD (1.6)
CTPP_enzyme_Ne2uz1C3 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_NECOD (1.6)
BTPP_enzyme_Me2uz1B1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: DHS-like NAD/FAD-binding domainF: TPP_enzyme_MECOD (1.6)
BTPP_enzyme_Ce2uz1B2 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_CECOD (1.6)
BTPP_enzyme_Ne2uz1B3 A: a/b three-layered sandwichesX: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)T: Thiamin diphosphate-binding fold (THDP-binding)F: TPP_enzyme_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, D
PF00205Thiamine pyrophosphate enzyme, central domain (TPP_enzyme_M)Thiamine pyrophosphate enzyme, central domainThe central domain of TPP enzymes contains a 2-fold Rossman fold.Domain
A, D
PF02775Thiamine pyrophosphate enzyme, C-terminal TPP binding domain (TPP_enzyme_C)Thiamine pyrophosphate enzyme, C-terminal TPP binding domain- Domain
A, D
PF02776Thiamine pyrophosphate enzyme, N-terminal TPP binding domain (TPP_enzyme_N)Thiamine pyrophosphate enzyme, N-terminal TPP binding domain- Domain
B, C
PF00205Thiamine pyrophosphate enzyme, central domain (TPP_enzyme_M)Thiamine pyrophosphate enzyme, central domainThe central domain of TPP enzymes contains a 2-fold Rossman fold.Domain
B, C
PF02775Thiamine pyrophosphate enzyme, C-terminal TPP binding domain (TPP_enzyme_C)Thiamine pyrophosphate enzyme, C-terminal TPP binding domain- Domain
B, C
PF02776Thiamine pyrophosphate enzyme, N-terminal TPP binding domain (TPP_enzyme_N)Thiamine pyrophosphate enzyme, N-terminal TPP binding domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, D
BENZALDEHYDE LYASE -
B, C
BENZALDEHYDE LYASE -