Unsaturated glucuronyl hydrolase
Details
- Name
- Unsaturated glucuronyl hydrolase
- Synonyms
- 3.2.1.179
- Glycosaminoglycan hydrolase
- Glycuronidase
- UGL
- Unsaturated uronic acid hydrolase
- Gene Name
- ugl
- Organism
- Bacillus sp. (strain GL1)
- Amino acid sequence
>lcl|BSEQ0012214|Unsaturated glucuronyl hydrolase MWQQAIGDALGITARNLKKFGDRFPHVSDGSNKYVLNDNTDWTDGFWSGILWLCYEYTGD EQYREGAVRTVASFRERLDRFENLDHHDIGFLYSLSAKAQWIVEKDESARKLALDAADVL MRRWRADAGIIQAWGPKGDPENGGRIIIDCLLNLPLLLWAGEQTGDPEYRRVAEAHALKS RRFLVRGDDSSYHTFYFDPENGNAIRGGTHQGNTDGSTWTRGQAWGIYGFALNSRYLGNA DLLETAKRMARHFLARVPEDGVVYWDFEVPQEPSSYRDSSASAITACGLLEIASQLDESD PERQRFIDAAKTTVTALRDGYAERDDGEAEGFIRRGSYHVRGGISPDDYTIWGDYYYLEA LLRLERGVTGYWYERGR
- Number of residues
- 377
- Molecular Weight
- 42861.02
- Theoretical pI
- 4.93
- GO Classification
- Functionshydrolase activity, acting on glycosyl bondsProcessespolysaccharide catabolic processComponentscytoplasm
- General Function
- Hydrolase activity, acting on glycosyl bonds
- Specific Function
- Catalyzes the hydrolysis of oligosaccharides with unsaturated glucuronyl residues at the non-reducing terminal, to a sugar or an amino sugar, and an unsaturated D-glucuronic acid (GlcA), which is nonenzymatically converted immediately to alpha-keto acid.
- Pfam Domain Function
- Glyco_hydro_88 (PF07470)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0006173|1134 bp ATGTGGCAGCAAGCGATAGGCGACGCGCTCGGCATTACCGCCCGCAATCTCAAGAAATTC GGGGACCGTTTCCCCCATGTCAGCGACGGGAGCAACAAGTACGTGCTGAACGACAATACC GACTGGACAGACGGTTTCTGGTCCGGCATCCTGTGGCTCTGCTACGAATATACGGGAGAC GAGCAATACCGCGAGGGCGCCGTCCGGACGGTCGCGAGCTTCCGCGAACGTCTGGATCGT TTCGAGAATCTCGATCATCACGACATCGGCTTCCTATACTCGCTGTCGGCCAAGGCCCAA TGGATCGTCGAAAAGGACGAATCCGCGCGCAAGCTGGCGCTCGATGCCGCCGACGTGCTG ATGCGCCGCTGGCGCGCGGATGCGGGCATTATCCAGGCCTGGGGACCGAAGGGCGATCCG GAAAACGGCGGACGCATCATCATCGACTGCCTGCTGAATCTGCCGCTTTTGCTCTGGGCC GGCGAACAGACGGGCGATCCCGAATACCGCCGCGTCGCCGAGGCGCACGCGCTGAAAAGC CGCCGGTTCCTCGTGCGCGGCGACGATTCGAGCTATCATACGTTCTACTTCGACCCAGAA AACGGGAATGCCATCCGCGGCGGCACGCACCAGGGCAACACCGACGGCAGCACGTGGACG CGCGGCCAGGCTTGGGGCATCTACGGCTTCGCGTTGAACAGCCGCTATCTCGGCAATGCC GACCTGCTGGAGACGGCGAAGCGCATGGCGCGCCACTTCCTCGCCCGGGTGCCGGAGGAC GGCGTCGTGTATTGGGACTTCGAGGTGCCGCAGGAGCCGTCCTCGTACCGAGACAGCTCC GCGTCGGCCATCACGGCATGCGGCCTGCTCGAGATCGCGAGCCAGCTTGACGAGAGCGAC CCCGAGCGCCAGCGCTTCATCGACGCGGCGAAGACGACCGTGACGGCGCTGCGCGACGGC TACGCCGAGCGCGACGACGGCGAAGCCGAAGGCTTCATCCGCCGCGGCTCCTATCACGTG CGCGGCGGCATCTCGCCCGACGACTACACGATCTGGGGCGATTATTATTACCTGGAAGCG CTGCTGCGTCTGGAGCGCGGCGTGACGGGGTATTGGTACGAGCGCGGACGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9RC92 UniProtKB Entry Name UGL_BACGL GenBank Gene ID AB019619 - General References
- Hashimoto W, Kobayashi E, Nankai H, Sato N, Miya T, Kawai S, Murata K: Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch Biochem Biophys. 1999 Aug 15;368(2):367-74. [Article]
- Nakamichi Y, Maruyama Y, Mikami B, Hashimoto W, Murata K: Structural determinants in streptococcal unsaturated glucuronyl hydrolase for recognition of glycosaminoglycan sulfate groups. J Biol Chem. 2011 Feb 25;286(8):6262-71. doi: 10.1074/jbc.M110.182618. Epub 2010 Dec 8. [Article]
- Itoh T, Akao S, Hashimoto W, Mikami B, Murata K: Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution. J Biol Chem. 2004 Jul 23;279(30):31804-12. Epub 2004 May 17. [Article]
- Itoh T, Hashimoto W, Mikami B, Murata K: Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1. Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. [Article]
- Itoh T, Hashimoto W, Mikami B, Murata K: Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism. J Biol Chem. 2006 Oct 6;281(40):29807-16. Epub 2006 Aug 7. [Article]