Protein Family Models

This entry represents the C-terminal domain of Galactarate dehydratase (GarD). GarD catalyses the dehydration of galactarate to 5-dehydro-4-deoxy-D-galactarate. In the crystal structure, GarD forms dimers and each monomer consists of three domains: the N-terminal SAF domain (Pfam:PF08666) connected to the second domain (Pfam:PF04295) through a long linker and the C-terminal domain which represents the core of the protein. This domain adopts a variant of a Rossmann fold with an unusual crossover, consisting of seven-stranded parallel beta-sheets surrounded by nine alpha-helices [1]. This domain may contain a catalytic metal binding site [1]. [1]. 31811683. Structure of galactarate dehydratase, a new fold in an enolase involved in bacterial fitness after antibiotic treatment. Rosas-Lemus M, Minasov G, Shuvalova L, Wawrzak Z, Kiryukhina O, Mih N, Jaroszewski L, Palsson B, Godzik A, Satchell KJF;. Protein Sci. 2020;29:711-722. (from Pfam)

Date:

2024-10-16

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins. [1]. 15146494. The emergence of catalytic and structural diversity within the beta-clip fold. Iyer LM, Aravind L;. Proteins. 2004;55:977-991. (from Pfam)

Date:

2024-10-16

This entry includes D-galactarate dehydratase (GarD, EC:4.2.1.42) which catalyses the reaction D-galactarate = 5-keto-4-deoxy-D glucarate + H2O, [1] and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyses D-altronate = 2-keto-2- deoxygluconate + H2O [2]. As purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn2+ appears to be part of the enzyme active centre, but the function of the single bound Fe2+ ion is unknown. The hydratase has no Fe-S core [3]. GarD structure revealed that it is a dimer in solution; each monomer has three domains, an N-terminal SAF domain (Pfam:PF08666), a second domain represented in this entry and a C-terminal domain [5]. This domain consists of three parallel beta-strands, surrounded by three alpha-helices and it interacts with the C-terminal domain from the second chain to form a dimerisation surface [5]. [1]. 9772162. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA;. Biochemistry 1998;37:14369-14375. [2]. 9579062. A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element. Rivolta C, Soldo B, Lazarevic V, Joris B, Mauel C, Karamata D;. Microbiology 1. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

galactarate dehydratase (GalcD) catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate

Date:

2019-06-06

Galactarate dehydratase converts D-galactarate to 5-dehydro-4-deoxyglucarate which is subsequently acted on by GarL, tartronate semialdehyde reductase and glycerate kinase ([1], GenProp0714).

Gene:

garD

Date:

2021-08-12