enterochelin esterase is involved in the breakdown of the siderophore enterochelin to 2,3-dihydroxybenzoyl-L-serine units, which is necessary for the intracellular release of iron
Enterochelin esterase, N-terminal; This entry represents the N-terminal domain of enterochelin ...
30-160
8.52e-47
Enterochelin esterase, N-terminal; This entry represents the N-terminal domain of enterochelin esterase. The activity of the enzyme has been characterized. Fes catalyzes the hydrolysis of the 2,3-dihydroxy-N- benzoyl-L-serine trimer, enterochelin, forming 2,3- dihydroxybenzoylserine. It also catalyzes hydrolysis of free enterobactin and ferric enterobactin. Upon hydrolysis of ferric enterobactin by Fes, released iron is probably reduced by a second enzyme. Enterochelin esterase represents a family of non-peptidase homologs belonging to the MEROPS peptidase family S9, clan SC.
Pssm-ID: 432089 Cd Length: 121 Bit Score: 156.42 E-value: 8.52e-47
Enterochelin esterase, N-terminal; This entry represents the N-terminal domain of enterochelin ...
30-160
8.52e-47
Enterochelin esterase, N-terminal; This entry represents the N-terminal domain of enterochelin esterase. The activity of the enzyme has been characterized. Fes catalyzes the hydrolysis of the 2,3-dihydroxy-N- benzoyl-L-serine trimer, enterochelin, forming 2,3- dihydroxybenzoylserine. It also catalyzes hydrolysis of free enterobactin and ferric enterobactin. Upon hydrolysis of ferric enterobactin by Fes, released iron is probably reduced by a second enzyme. Enterochelin esterase represents a family of non-peptidase homologs belonging to the MEROPS peptidase family S9, clan SC.
Pssm-ID: 432089 Cd Length: 121 Bit Score: 156.42 E-value: 8.52e-47
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
177-393
6.64e-42
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 147.61 E-value: 6.64e-42
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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