5XEY

Discovery and structural analysis of a phloretin hydrolase from the opportunistic pathogen Mycobacterium abscessus


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF18089e5xeyA1 A: a+b two layersX: TBP-likeH: Bet v1-like (From Topology)T: Bet v1-likeF: PF18089ECOD (1.6)
BPF18089e5xeyB1 A: a+b two layersX: TBP-likeH: Bet v1-like (From Topology)T: Bet v1-likeF: PF18089ECOD (1.6)
CPF18089e5xeyC1 A: a+b two layersX: TBP-likeH: Bet v1-like (From Topology)T: Bet v1-likeF: PF18089ECOD (1.6)
DPF18089e5xeyD1 A: a+b two layersX: TBP-likeH: Bet v1-like (From Topology)T: Bet v1-likeF: PF18089ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF18089DAPG hydrolase PhiG domain (DAPG_hydrolase)DAPG hydrolase PhiG domainThis domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG present in Pseudomonas fluorescens. 2,4-diacetylphloroglucinol hydrolase is the gene product of PhiG that is responsible for cleaving toxic 2,4-diacetylphloroglucinol (DAPG). The small ...This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG present in Pseudomonas fluorescens. 2,4-diacetylphloroglucinol hydrolase is the gene product of PhiG that is responsible for cleaving toxic 2,4-diacetylphloroglucinol (DAPG). The small N-terminal region of the domain is involved in dimerization through hydrogen bonding of the dimer interface. The C-terminal catalytic region resembles the tetracenomycin aromatase/cyclase and has a Bet v1-like fold. DAPG PhiG is the first discovered hydrolase whose catalytic domain belongs to the Bet v1-like fold, rather than the classical alpha/beta-fold hydrolases [1].
Domain

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D
IPR041526DAPG hydrolase, PhiG domainDomain