{"metadata":{"accession":"PF00701","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002220","hierarchy":null,"name":{"name":"Dihydrodipicolinate synthetase family","short":"DHDPS"},"description":[{"text":"<p>This family has a TIM barrel structure.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Dihydrodipicolinate_synthase","extract":"<p><b>4-Hydroxy-tetrahydrodipicolinate synthase</b> (EC 4.3.3.7, <b>dihydrodipicolinate synthase</b>, <b>dihydropicolinate synthetase</b>, <b>dihydrodipicolinic acid synthase</b>, <b><small>L</small>-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing)</b>, <i>dapA (gene)</i>) is an enzyme with the systematic name <b><small>L</small>-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4<i>S</i>)-4-hydroxy-2,3,4,5-tetrahydro-(2<i>S</i>)-dipicolinate-forming)</b>. This enzyme catalyses the following chemical reaction</p><dl><dd>pyruvate + <small>L</small>-aspartate-4-semialdehyde <span class=\"mwe-math-element mwe-math-element-inline\"><img src=\"https://wikimedia.org/api/rest_v1/media/math/render/svg/1c37b981df851b9e54e489e017b1481e37d418f3\" class=\"mwe-math-fallback-image-inline mw-invert skin-invert\" aria-hidden=\"true\" style=\"vertical-align:-0.338ex;width:2.324ex;height:1.843ex\" /></span> (2<i>S</i>,4<i>S</i>)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H<sub>2</sub>O</dd></dl>","thumbnail":null}],"literature":{"PUB00005245":{"PMID":8081752,"ISBN":null,"volume":"2","issue":"5","year":1994,"title":"The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli.","URL":null,"raw_pages":"361-9","medline_journal":"Structure","ISO_journal":"Structure","authors":["Izard T","Lawrence MC","Malby RL","Lilley GG","Colman PM."],"DOI_URL":"http://dx.doi.org/10.1016/S0969-2126(00)00038-1"},"PUB00003343":{"PMID":7853400,"ISBN":null,"volume":"246","issue":"1","year":1995,"title":"The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.","URL":null,"raw_pages":"227-39","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Mirwaldt C","Korndorfer I","Huber R."],"DOI_URL":"http://dx.doi.org/10.1006/jmbi.1994.0078"}},"set_info":{"accession":"CL0036","name":"TIM_barrel"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":213,"interactions":0,"matches":85700,"pathways":0,"proteins":85296,"proteomes":20132,"sets":1,"structural_models":{"alphafold":65329,"bfvd":1},"structures":269,"taxa":36567},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":9,"alignment:full":33664},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2pur","name":"Structure of dihydrodipicolinate synthase mutant Thr44Ser at 1.7 A."}}}