MULTISPECIES: lipocalin-like domain-containing protein [Pseudomonas]
Protein Classification
carotenoid 1,2-hydratase; carotenoid 1,2-hydratase; carotenoid 1,2-hydratase; hydroxyneurosporene synthase family protein( domain architecture ID 10009496)
carotenoid 1,2-hydratase is a hydroxyneurosporene synthase (CrtC) family protein, which converts acyclic carotenes to the corresponding hydroxylated carotenoids; carotenoid 1,2-hydratase is a hydroxyneurosporene synthase (CrtC) family protein, which converts acyclic carotenes to the corresponding hydroxylated carotenoids; carotenoid 1,2-hydratase is a hydroxyneurosporene synthase (CrtC) family protein, which converts acyclic carotenes to the corresponding hydroxylated carotenoids; hydroxyneurosporene synthase (CrtC) family protein, which convert acyclic carotenes
CrtC N-terminal lipocalin domain; This family contains the members of the old Pfam family ...
64-236
6.76e-74
CrtC N-terminal lipocalin domain; This family contains the members of the old Pfam family DUF2006. Structural characterization of family member Swiss:Q82US3 (from DUF2006 now merged into this family) has revealed a lipocalin-like fold with domain duplication.
Pssm-ID: 429315 Cd Length: 175 Bit Score: 226.78 E-value: 6.76e-74
carotenoid 1,2-hydratase and similar proteins; Carotenoid 1,2-hydratase (EC 4.2.1.131; CrtC; ...
211-284
5.45e-04
carotenoid 1,2-hydratase and similar proteins; Carotenoid 1,2-hydratase (EC 4.2.1.131; CrtC; also known as acyclic carotenoid 1,2-hydratase, 1-hydroxyneurosporene hydratase, hydroxylycopene hydratase, hydroxyneurosporene synthase, lycopene hydratase, or neurosporene hydratase) is an enzyme with the systematic name lycopene hydro-lyase (1-hydroxy-1,2-dihydrolycopene-forming). It is involved in the biosynthesis of carotenoids such as lycopenes. It catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and that of lycopene to 1-HO-lycopene. Studies suggest that CrtC may be bound to the membrane through an anchor so that a close distance to the substrate, which is synthesized in the cell membranes, is facilitated.
Pssm-ID: 409193 Cd Length: 276 Bit Score: 41.05 E-value: 5.45e-04
CrtC N-terminal lipocalin domain; This family contains the members of the old Pfam family ...
64-236
6.76e-74
CrtC N-terminal lipocalin domain; This family contains the members of the old Pfam family DUF2006. Structural characterization of family member Swiss:Q82US3 (from DUF2006 now merged into this family) has revealed a lipocalin-like fold with domain duplication.
Pssm-ID: 429315 Cd Length: 175 Bit Score: 226.78 E-value: 6.76e-74
Lipocalin-like domain; This family contains the members of the old Pfam family DUF2006. ...
239-361
5.95e-49
Lipocalin-like domain; This family contains the members of the old Pfam family DUF2006. Structural characterization of family member Swiss:Q82US3 (from DUF2006 now merged into this family) has revealed a lipocalin-like fold with domain duplication. This entry represents the C-terminal domain of the pair.
Pssm-ID: 435773 Cd Length: 129 Bit Score: 160.86 E-value: 5.95e-49
carotenoid 1,2-hydratase and similar proteins; Carotenoid 1,2-hydratase (EC 4.2.1.131; CrtC; ...
211-284
5.45e-04
carotenoid 1,2-hydratase and similar proteins; Carotenoid 1,2-hydratase (EC 4.2.1.131; CrtC; also known as acyclic carotenoid 1,2-hydratase, 1-hydroxyneurosporene hydratase, hydroxylycopene hydratase, hydroxyneurosporene synthase, lycopene hydratase, or neurosporene hydratase) is an enzyme with the systematic name lycopene hydro-lyase (1-hydroxy-1,2-dihydrolycopene-forming). It is involved in the biosynthesis of carotenoids such as lycopenes. It catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and that of lycopene to 1-HO-lycopene. Studies suggest that CrtC may be bound to the membrane through an anchor so that a close distance to the substrate, which is synthesized in the cell membranes, is facilitated.
Pssm-ID: 409193 Cd Length: 276 Bit Score: 41.05 E-value: 5.45e-04
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.
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