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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1bwza1 Alpha and beta proteins (a+b) Diaminopimelate epimerase-like Diaminopimelate epimerase-like Diaminopimelate epimerase Diaminopimelate epimerase (Haemophilus influenzae ) [TaxId: 727 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyDiaminopimelate epimerase-like8041937 3000573 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyDiaminopimelate epimerase-like8041936 3000573 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ADAP_epimerasee1bwzA1 A: a+b complex topologyX: Diaminopimelate epimerase-like (From Topology)H: Diaminopimelate epimerase-like (From Topology)T: Diaminopimelate epimerase-likeF: DAP_epimeraseECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.10.310.10 Alpha Beta Roll Diaminopimelate Epimerase Chain A, domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01678Diaminopimelate epimerase (DAP_epimerase)Diaminopimelate epimeraseDiaminopimelate epimerase contains two domains of the same alpha/beta fold, both contained in this family.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
PROTEIN (DIAMINOPIMELATE EPIMERASE)

InterPro: Protein Family Classification InterPro Database Homepage

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

ChainsEnzyme NameDescriptionCatalytic Residues
diaminopimelate epimerase  M-CSA #334

Diaminopimelate epimerase catalyses the isomerisation of L,L-dimaminopimelate to meso-DAP in the biosynthetic pathway leading from aspartate to lysine. It is a member of the broader family of PLP-independent amino acid racemases. Diaminopimelic acid is an essential component of bacterial cell wall biosynthesis. Diaminopimelate epimerase utilises a pair of cysteine residues in catalysis, as seen in other non-PLP dependent alpha-amino acid racemases. However, its specificity for a substrate with two stereo-centres separates the kinetic from data that presented by functionally related enzymes [PMID:16723397, PMID:10194362].

Defined by 5 residues: CYS:A-73HIS:A-159GLU:A-208CYS:A-217GLY:A-220
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