Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAMP-binding_3rde4zxhA4 A: beta barrelsX: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)T: beta-barrel domain in acetyl-CoA synthetase-like proteinsF: AMP-binding_3rdECOD (1.6)
APP-bindinge4zxhA6 A: alpha bundlesX: ACP-likeH: Acyl-carrier protein (ACP) (From Topology)T: Acyl-carrier protein (ACP)F: PP-bindingECOD (1.6)
AAMP-binding_Ce4zxhA3 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)T: a+b domain in acetyl-CoA synthetase-like proteinsF: AMP-binding_CECOD (1.6)
ACondensation_Ne4zxhA7 A: a+b complex topologyX: CoA-dependent acyltransferases (From Topology)H: CoA-dependent acyltransferases (From Topology)T: CoA-dependent acyltransferasesF: Condensation_NECOD (1.6)
ACondensation_C_2e4zxhA1 A: a+b complex topologyX: CoA-dependent acyltransferases (From Topology)H: CoA-dependent acyltransferases (From Topology)T: CoA-dependent acyltransferasesF: Condensation_C_2ECOD (1.6)
AHydrolase_4_1e4zxhA8 A: a/b three-layered sandwichesX: alpha/beta-Hydrolases (From Topology)H: alpha/beta-Hydrolases (From Topology)T: alpha/beta-HydrolasesF: Hydrolase_4_1ECOD (1.6)
AAMP-binding_1ste4zxhA5 A: a/b three-layered sandwichesX: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)T: Rossmann-like domain in Acetyl-CoA synthetase-like proteinsF: AMP-binding_1stECOD (1.6)
AAMP-binding_2nde4zxhA9 A: a/b three-layered sandwichesX: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)T: Rossmann-like domain in Acetyl-CoA synthetase-like proteinsF: AMP-binding_2ndECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00501AMP-binding enzyme (AMP-binding)AMP-binding enzyme- Family
PF00975Thioesterase domain (Thioesterase)Thioesterase domainPeptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of v ...Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Domain
PF00668Condensation domain (Condensation)Condensation domain- Family
PF13193AMP-binding enzyme C-terminal domain (AMP-binding_C)AMP-binding enzyme C-terminal domainThis is a small domain that is found C terminal to Pfam:PF00501. It has a central beta sheet core that is flanked by alpha helices.Domain
PF00550Phosphopantetheine attachment site (PP-binding)Phosphopantetheine attachment siteA 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Domain