{"metadata":{"accession":"PF09118","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR015202","hierarchy":null,"name":{"name":"Galactose oxidase-like, Early set domain","short":"GO-like_E_set"},"description":[{"text":"<p>E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions.  Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology [[cite:PUB00014151]]. This domain is found in sugar-utilising enzymes, such as galactose oxidase or chitinase [[cite:PUB00028414],[cite:PUB00044942],[cite:PUB00080765],[cite:PUB00080766],[cite:PUB00003324]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00003324":{"PMID":8182749,"ISBN":null,"volume":"238","issue":"5","year":1994,"title":"Crystal structure of a free radical enzyme, galactose oxidase.","URL":null,"raw_pages":"794-814","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Ito N","Phillips SE","Yadav KD","Knowles PF."],"DOI_URL":"http://dx.doi.org/10.1006/jmbi.1994.1335"},"PUB00080765":{"PMID":12530525,"ISBN":null,"volume":"59","issue":"11","year":2002,"title":"Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the alpha-amylase family defined by the fifth conserved sequence region.","URL":null,"raw_pages":"1945-59","medline_journal":"Cell Mol Life Sci","ISO_journal":"Cell. Mol. Life Sci.","authors":["Oslancova A","Janecek S."],"DOI_URL":"http://dx.doi.org/10.1007/PL00012517"},"PUB00014151":{"PMID":11698678,"ISBN":null,"volume":"98","issue":"23","year":2001,"title":"Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.","URL":null,"raw_pages":"12932-7","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Firbank SJ","Rogers MS","Wilmot CM","Dooley DM","Halcrow MA","Knowles PF","McPherson MJ","Phillips SE."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.231463798"},"PUB00028414":{"PMID":11923309,"ISBN":null,"volume":"277","issue":"24","year":2002,"title":"Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other.","URL":null,"raw_pages":"21891-7","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Lee HS","Kim MS","Cho HS","Kim JI","Kim TJ","Choi JH","Park C","Lee HS","Oh BH","Park KH."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M201623200"},"PUB00044942":{"PMID":10825529,"ISBN":null,"volume":"1478","issue":"2","year":2000,"title":"Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.","URL":null,"raw_pages":"165-85","medline_journal":"Biochim Biophys Acta","ISO_journal":"Biochim. Biophys. Acta","authors":["Park KH","Kim TJ","Cheong TK","Kim JW","Oh BH","Svensson B."],"DOI_URL":"http://dx.doi.org/10.1016/S0167-4838(00)00041-8"},"PUB00080766":{"PMID":15239382,"ISBN":null,"volume":"30","issue":"2","year":2004,"title":"Pullulan degrading enzymes of bacterial origin.","URL":null,"raw_pages":"107-21","medline_journal":"Crit Rev Microbiol","ISO_journal":"Crit. Rev. Microbiol.","authors":["Doman-Pytka M","Bardowski J."],"DOI_URL":"http://dx.doi.org/10.1080/10408410490435115"}},"set_info":{"accession":"CL0159","name":"E-set"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":394,"interactions":0,"matches":11312,"pathways":0,"proteins":11271,"proteomes":3086,"sets":1,"structural_models":{"alphafold":8352},"structures":32,"taxa":5834},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":329,"alignment:full":7773},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}