Protein Family Models

HpaB Swiss:Q57160 encodes part of the 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli [2]. HpaB is part of a heterodimeric enzyme that also requires HpaC. The enzyme is NADH-dependent and uses FAD as the redox chromophore. This family also includes PvcC Swiss:O30372 may play a role in one of the proposed hydroxylation steps of pyoverdine chromophore biosynthesis [1]. [1]. 10383985. The pvc gene cluster of Pseudomonas aeruginosa: role in. synthesis of the pyoverdine chromophore and regulation by PtxR. and PvdS.. Stintzi A, Johnson Z, Stonehouse M, Ochsner U, Meyer JM, Vasil. ML, Poole K;. J Bacteriol 1999;181:4118-4124.. [2]. 8077235. Molecular characterization of 4-hydroxyphenylacetate. 3-hydroxylase of Escherichia coli. A two-protein component. enzyme.. Prieto MA, Garcia JL;. J Biol Chem 1994;269:22823-22829. (from Pfam)

Date:

2024-08-14

HpaB Swiss:Q57160 encodes part of the 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli [2]. HpaB is part of a heterodimeric enzyme that also requires HpaC. The enzyme is NADH-dependent and uses FAD as the redox chromophore. This family also includes PvcC Swiss:O30372 may play a role in one of the proposed hydroxylation steps of pyoverdine chromophore biosynthesis [1]. [1]. 10383985. The pvc gene cluster of Pseudomonas aeruginosa: role in. synthesis of the pyoverdine chromophore and regulation by PtxR. and PvdS.. Stintzi A, Johnson Z, Stonehouse M, Ochsner U, Meyer JM, Vasil. ML, Poole K;. J Bacteriol 1999;181:4118-4124.. [2]. 8077235. Molecular characterization of 4-hydroxyphenylacetate. 3-hydroxylase of Escherichia coli. A two-protein component. enzyme.. Prieto MA, Garcia JL;. J Biol Chem 1994;269:22823-22829. (from Pfam)

Date:

2024-08-14

4-hydroxyphenylacetate (HPA) 3-hydroxylase family protein may catalyze the hydroxylation of 4-HPA, leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA), and is similar to Pseudomonas aeruginosa pyoverdin chromophore biosynthetic protein PvcC

Date:

2021-03-25

Pyrrole-2-carboxylate monooxygenase from Rhodococcus sp. is composed of a large protein showing no activity by its own and a small protein catalyzing the NADH-dependent and FAD-dependent reduction of cytochrome c. Both components are required for utilizing pyrrole-2-carboxylate as the source of carbon, nitrogen, and energy.

Date:

2019-03-26