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{
"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."
}
}
}
