5-dehydro-4-deoxy-D-glucuronate isomerase catalyzes the interconversion of 4-deoxy-L-threo-5-hexosulose uronate to 3-deoxy-D-glycero-2,5-hexodiulosonate
Escherichia coli 5-keto-4-deoxyuronate isomerase (KduI) and related proteins, C-terminal cupin ...
160-267
1.26e-75
Escherichia coli 5-keto-4-deoxyuronate isomerase (KduI) and related proteins, C-terminal cupin domain; 5-keto-4-deoxyuronate isomerase (KduI; EC 5.3.1.17), also called 5-dehydro-4-deoxy-D-glucuronate isomerase or 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase, catalyzes the interconversion of 5-keto-4-deoxyuronate and 2,5-diketo-3-dexoygluconate in the breakdown of pectin. KduI is a bicupin; this model describes the C-terminal cupin domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380448 Cd Length: 108 Bit Score: 225.66 E-value: 1.26e-75
KduI/IolB family; This family includes the 5-keto 4-deoxyuronate isomerase enzyme EC:5.3.1.17 ...
26-269
6.28e-43
KduI/IolB family; This family includes the 5-keto 4-deoxyuronate isomerase enzyme EC:5.3.1.17 that is involved in pectin degradation. This family aldo includes bacterial Myo-inositol catabolism (IolB) proteins. The Bacillus subtilis inositol operon (iolABCDEFGHIJ) is involved in myo-inositol catabolism. Glucose repression of the iol operon induced by inositol is exerted through catabolite repression mediated by CcpA and the iol induction system mediated by IolR. The exact function of IolB is unknown. Members of this family possess a Cupin like structure.
Pssm-ID: 398565 Cd Length: 260 Bit Score: 146.99 E-value: 6.28e-43
Escherichia coli 5-keto-4-deoxyuronate isomerase (KduI) and related proteins, C-terminal cupin ...
160-267
1.26e-75
Escherichia coli 5-keto-4-deoxyuronate isomerase (KduI) and related proteins, C-terminal cupin domain; 5-keto-4-deoxyuronate isomerase (KduI; EC 5.3.1.17), also called 5-dehydro-4-deoxy-D-glucuronate isomerase or 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase, catalyzes the interconversion of 5-keto-4-deoxyuronate and 2,5-diketo-3-dexoygluconate in the breakdown of pectin. KduI is a bicupin; this model describes the C-terminal cupin domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380448 Cd Length: 108 Bit Score: 225.66 E-value: 1.26e-75
5-keto-4-deoxyuronate isomerase (KduI) and related proteins, N-terminal cupin domain; ...
36-133
9.18e-45
5-keto-4-deoxyuronate isomerase (KduI) and related proteins, N-terminal cupin domain; 5-keto-4-deoxyuronate isomerase (KduI; EC 5.3.1.17), also called 5-dehydro-4-deoxy-D-glucuronate isomerase or 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase, catalyzes the interconversion of 5-keto-4-deoxyuronate and 2,5-diketo-3-dexoygluconate in the breakdown of pectin. KduI is a bicupin; this model describes the N-terminal cupin domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380428 [Multi-domain] Cd Length: 100 Bit Score: 146.43 E-value: 9.18e-45
KduI/IolB family; This family includes the 5-keto 4-deoxyuronate isomerase enzyme EC:5.3.1.17 ...
26-269
6.28e-43
KduI/IolB family; This family includes the 5-keto 4-deoxyuronate isomerase enzyme EC:5.3.1.17 that is involved in pectin degradation. This family aldo includes bacterial Myo-inositol catabolism (IolB) proteins. The Bacillus subtilis inositol operon (iolABCDEFGHIJ) is involved in myo-inositol catabolism. Glucose repression of the iol operon induced by inositol is exerted through catabolite repression mediated by CcpA and the iol induction system mediated by IolR. The exact function of IolB is unknown. Members of this family possess a Cupin like structure.
Pssm-ID: 398565 Cd Length: 260 Bit Score: 146.99 E-value: 6.28e-43
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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