UxaA family hydrolase similar to Chromohalobacter salexigens (2R)-sulfolactate sulfo-lyase subunit alpha (SuyA) that, together with SuyB, esulfonates sulfolactate to form pyruvate and sulfite
D-galactarate dehydratase / Altronate hydrolase, C terminus; Family members include the C ...
106-494
0e+00
D-galactarate dehydratase / Altronate hydrolase, C terminus; Family members include the C termini of D-galactarate dehydratase (EC:4.2.1.42) which is thought to catalyze the reaction D-galactarate = 5-keto-4-deoxy-D-glucarate + H2O, and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyzes D-altronate = 2-keto-2-deoxygluconate + H2O. As purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn2+ appears to be part of the enzyme active centre, but the function of the single bound Fe2+ ion is unknown. The hydratase has no Fe-S core.
Pssm-ID: 461252 Cd Length: 393 Bit Score: 638.30 E-value: 0e+00
Domains similar to fish antifreeze type III protein; Altronate dehydratase (EC 4.2.1.7) ...
2-81
7.97e-39
Domains similar to fish antifreeze type III protein; Altronate dehydratase (EC 4.2.1.7) converts D-altronate into 2-dehydro-3-deoxy-D-gluconate and is part of a bacterial pathway for the degradation of D-galacturonate. D-galactarate dehydratase (EC 4.2.1.42) eliminates water from D-galactarate to yield 5-dehydro-4-deoxy-D-glucarate, initializing the degradation of D-galactarate. The function of the SAF domain in these enzymes is not clear. It may participate in dimerization.
Pssm-ID: 212158 Cd Length: 80 Bit Score: 135.63 E-value: 7.97e-39
D-galactarate dehydratase / Altronate hydrolase, C terminus; Family members include the C ...
106-494
0e+00
D-galactarate dehydratase / Altronate hydrolase, C terminus; Family members include the C termini of D-galactarate dehydratase (EC:4.2.1.42) which is thought to catalyze the reaction D-galactarate = 5-keto-4-deoxy-D-glucarate + H2O, and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyzes D-altronate = 2-keto-2-deoxygluconate + H2O. As purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn2+ appears to be part of the enzyme active centre, but the function of the single bound Fe2+ ion is unknown. The hydratase has no Fe-S core.
Pssm-ID: 461252 Cd Length: 393 Bit Score: 638.30 E-value: 0e+00
Domains similar to fish antifreeze type III protein; Altronate dehydratase (EC 4.2.1.7) ...
2-81
7.97e-39
Domains similar to fish antifreeze type III protein; Altronate dehydratase (EC 4.2.1.7) converts D-altronate into 2-dehydro-3-deoxy-D-gluconate and is part of a bacterial pathway for the degradation of D-galacturonate. D-galactarate dehydratase (EC 4.2.1.42) eliminates water from D-galactarate to yield 5-dehydro-4-deoxy-D-glucarate, initializing the degradation of D-galactarate. The function of the SAF domain in these enzymes is not clear. It may participate in dimerization.
Pssm-ID: 212158 Cd Length: 80 Bit Score: 135.63 E-value: 7.97e-39
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
10-81
3.29e-08
SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.
Pssm-ID: 430140 [Multi-domain] Cd Length: 63 Bit Score: 50.25 E-value: 3.29e-08
Domains similar to fish antifreeze type III protein; SAF domains are found in a wide variety ...
12-47
1.52e-06
Domains similar to fish antifreeze type III protein; SAF domains are found in a wide variety of proteins with quite different functions. They are components of enzymes, such as D-altronate-dehydratases or sialic acid synthetases, of antifreeze proteins conserved in fish (where they bind to nascent ice crystals), and may act as periplasmic chaperones in bacterial flagella basal body P-ring formation.
Pssm-ID: 212157 [Multi-domain] Cd Length: 56 Bit Score: 45.15 E-value: 1.52e-06
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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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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