Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGAPDH-like 8058142 3000043 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ADapB_Ce5tjzA1 A: a+b two layersX: FwdE/GAPDH domain-likeH: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domainF: DapB_CECOD (1.6)
ADapB_Ne5tjzA2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: DapB_NECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF05173Dihydrodipicolinate reductase, C-terminus (DapB_C)Dihydrodipicolinate reductase, C-terminusDihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for bo ...Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.
Domain
PF01113Dihydrodipicolinate reductase, N-terminus (DapB_N)Dihydrodipicolinate reductase, N-terminusDihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for b ...Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
4-hydroxy-tetrahydrodipicolinate reductase