Protein Family Models

Date:

2024-08-14

This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2]. [1]. 8702766. Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold. Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K;. J Biol Chem 1996;271:20322-20330. [2]. 20485265. A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4. Osman C, Haag M, Wieland FT, Brugger B, Langer T;. EMBO J. 2010;29:1976-1987 (from Pfam)

Date:

2024-10-16

Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (PF00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.

Date:

2024-06-24

This HMM represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs (PMID:7966317). The subfamilies are defined (PMID:11601995) based on the location and the observed or predicted fold of a so-called 'capping domain' (PMID:10956028), or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. This model represents the variant 2 form of the still very broad HAD-IA family. In it, the third of the three defining catalytic motifs takes the form hhhhssxxx(x)D, where _s_ refers to a small amino acid and _h_ to a hydrophobic one.

Date:

2020-03-30