Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ALip_prot_lig_Ce5iclA2 A: a+b two layersX: FAD-linked reductases, C-terminal domain-likeH: SufE/NifU (From Topology)T: SufE/NifUF: Lip_prot_lig_CECOD (1.6)
ABPL_LplA_LipB_1e5iclA1 A: a+b three layersX: Class II aaRS and biotin synthetases (From Topology)H: Class II aaRS and biotin synthetases (From Topology)T: Class II aaRS and biotin synthetasesF: BPL_LplA_LipB_1ECOD (1.6)
BLip_prot_lig_Ce5iclB2 A: a+b two layersX: FAD-linked reductases, C-terminal domain-likeH: SufE/NifU (From Topology)T: SufE/NifUF: Lip_prot_lig_CECOD (1.6)
BBPL_LplA_LipB_1e5iclB1 A: a+b three layersX: Class II aaRS and biotin synthetases (From Topology)H: Class II aaRS and biotin synthetases (From Topology)T: Class II aaRS and biotin synthetasesF: BPL_LplA_LipB_1ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF21948Lipoyl protein ligase A/B catalytic domain (LplA-B_cat)Lipoyl protein ligase A/B catalytic domainThis entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [1-5]. These proteins catalyse the transfer of the lipoyl group from ...This entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [1-5]. These proteins catalyse the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes. Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system.
Domain
A, B
PF10437Bacterial lipoate protein ligase C-terminus (Lip_prot_lig_C)Bacterial lipoate protein ligase C-terminusThis is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB Pfam:PF03099, furthe ...This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB Pfam:PF03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.
Domain