Protein Family Models

This domain is found in 3-hydroxybutyryl-CoA dehydrogenase present in E. coli. 3-hydroxybutyryl-CoA dehydrogenase catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA, in which acetoacetyl-CoA is reduced to 3-hydroxybutyryl-CoA. This domain is a reduced Rossmann-fold domain and, unlike the first Rossmann-fold domain, it is missing the catalytic residues and an NAD(H) binding cleft [1] [2]. [1]. 25112316. Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium butyricum and its mutations that enhance reaction kinetics. Kim EJ, Kim J, Ahn JW, Kim YJ, Chang JH, Kim KJ;. J Microbiol Biotechnol. 2014;24:1636-1643. [2]. 10840044. Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ;. J Biol Chem. 2000;275:27186-27196. (from Pfam)

Date:

2024-10-16

The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. (from Pfam)

Date:

2024-08-14

The term 3-hydroxyacyl-CoA dehydrogenase, corresponding to EC 1.1.1.35, covers a range of specificities, as the acyl group is not specified. Beta-hydroxyacyl dehydrogenase is a synonym. There may be mulitple members of the family in a single genome, e.g. FadB, FabJ, and PaaH from Escherichia coli K-12.

Date:

2024-10-16

This family also includes lambda crystallin. Some proteins include two copies of this domain. [1]. 3479790. Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution. Birktoft JJ, Holden HM, Hamlin R, Xuong NH, Banaszak LJ;. Proc Natl Acad Sci U S A 1987;84:8262-8266. (from Pfam)

Date:

2024-10-16

This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring [1]. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN [2]. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the PF02737 and PF00725 families.

Gene:

paaH

Date:

2024-07-08