"accession" "counters" "cross_references" "description" "entry_id" "go_terms" "hierarchy" "integrated" "is_llm" "is_reviewed_llm" "is_updated_llm" "literature" "member_databases" "name" "overlaps_with" "representative_structure" "set_info" "source_database" "type" "wikipedia" "PF00701" "{'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}" "{}" "[{'text': '

This family has a TIM barrel structure.

', 'llm': False, 'checked': False, 'updated': False}]" "" "" "" "IPR002220" False False False "{'PUB00005245': {'PMID': 8081752, 'ISBN': None, 'volume': '2', 'issue': '5', 'year': 1994, 'title': 'The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli.', 'URL': None, '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': None, 'volume': '246', 'issue': '1', 'year': 1995, 'title': 'The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.', 'URL': None, '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'}}" "" "{'name': 'Dihydrodipicolinate synthetase family', 'short': 'DHDPS'}" "" "{'accession': '2pur', 'name': 'Structure of dihydrodipicolinate synthase mutant Thr44Ser at 1.7 A.'}" "{'accession': 'CL0036', 'name': 'TIM_barrel'}" "pfam" "domain" "[{'title': 'Dihydrodipicolinate_synthase', 'extract': '

4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction

pyruvate + L-aspartate-4-semialdehyde (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
', 'thumbnail': None}]"