Protein Family Models

This family has been characterised as 3-octaprenyl-4- hydroxybenzoate carboxy-lyase enzymes [1]. This enzyme catalyses the third reaction in ubiquinone biosynthesis. For optimal activity the carboxy-lase was shown to require Mn2+ [1]. This entry represents the N-terminal domain. [1]. 782527. Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase. Leppik RA, Young IG, Gibson F;. Biochim Biophys Acta 1976;436:800-810. [2]. 23671667. Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa. Jacewicz A, Izumi A, Brunner K, Schnell R, Schneider G;. PLoS One. 2013;8:e63161. [3]. 25862228. Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae. Bhuiya MW, Lee SG, Jez JM, Yu O;. Appl Environ Microbiol. 2015;81:4216-4223. [4]. 26083754. New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Payne KA, White MD, Fisher K, Khara B, Bailey SS, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Beveridge R, Barran P, Rigby SE, Scrutton NS, Hay S, Leys D;. Nature. 2015;522:497-501. [5]. 28057757. Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis. Marshall SA, Fisher K, Ni Cheallaigh A, White MD, Payne KA, Parker DA, Rigby SE, Leys D;. J Biol Chem. 2017;292:4623-4637. [6]. 28857436. Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase. Payer SE, Marshall SA, Barland N, Sheng X, Reiter T, Dordic A, Steink. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family has been characterised as 3-octaprenyl-4- hydroxybenzoate carboxy-lyase enzymes [1]. This enzyme catalyses the third reaction in ubiquinone biosynthesis. For optimal activity the carboxy-lase was shown to require Mn2+ [1]. This entry represents the C-terminal domain. [1]. 782527. Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase. Leppik RA, Young IG, Gibson F;. Biochim Biophys Acta 1976;436:800-810. [2]. 23671667. Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa. Jacewicz A, Izumi A, Brunner K, Schnell R, Schneider G;. PLoS One. 2013;8:e63161. [3]. 25862228. Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae. Bhuiya MW, Lee SG, Jez JM, Yu O;. Appl Environ Microbiol. 2015;81:4216-4223. [4]. 26083754. New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Payne KA, White MD, Fisher K, Khara B, Bailey SS, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Beveridge R, Barran P, Rigby SE, Scrutton NS, Hay S, Leys D;. Nature. 2015;522:497-501. [5]. 28057757. Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis. Marshall SA, Fisher K, Ni Cheallaigh A, White MD, Payne KA, Parker DA, Rigby SE, Leys D;. J Biol Chem. 2017;292:4623-4637. [6]. 28857436. Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase. Payer SE, Marshall SA, Barland N, Sheng X, Reiter T, Dordic A, Steink. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family has been characterised as 3-octaprenyl-4- hydroxybenzoate carboxy-lyase enzymes [1]. This enzyme catalyses the third reaction in ubiquinone biosynthesis. For optimal activity the carboxy-lase was shown to require Mn2+ [1]. This entry represents the central RIFT-related domain. [1]. 782527. Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase. Leppik RA, Young IG, Gibson F;. Biochim Biophys Acta 1976;436:800-810. [2]. 23671667. Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa. Jacewicz A, Izumi A, Brunner K, Schnell R, Schneider G;. PLoS One. 2013;8:e63161. [3]. 25862228. Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae. Bhuiya MW, Lee SG, Jez JM, Yu O;. Appl Environ Microbiol. 2015;81:4216-4223. [4]. 26083754. New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Payne KA, White MD, Fisher K, Khara B, Bailey SS, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Beveridge R, Barran P, Rigby SE, Scrutton NS, Hay S, Leys D;. Nature. 2015;522:497-501. [5]. 28057757. Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis. Marshall SA, Fisher K, Ni Cheallaigh A, White MD, Payne KA, Parker DA, Rigby SE, Leys D;. J Biol Chem. 2017;292:4623-4637. [6]. 28857436. Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase. Payer SE, Marshall SA, Barland N, Sheng X, Reiter T, Dordic. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

4-hydroxy-3-polyprenylbenzoate decarboxylase catalyzes the decarboxylation of 3-octaprenyl-4-hydroxybenzoate to 2-octaprenylphenol

Date:

2017-03-17

Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol

Gene:

ubiD

Date:

2021-08-12

The member of this family in E. coli is UbiD, 3-octaprenyl-4-hydroxybenzoate carboxy-lyase. The family described by this HMM, however, is broad enough that it is likely to contain several different decarboxylases. Found in bacteria, archaea, and yeast, with two members in A. fulgidus. No homologs were detected besides those classified as orthologs. The member from H. pylori has a C-terminal extension of just over 100 residues that is shared in part by the Aquifex aeolicus homolog.

Date:

2021-04-27