"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"
"IPR003462"	"{'subfamilies': 0, 'domain_architectures': 81, 'interactions': 0, 'matches': 27049, 'pathways': 7, 'proteins': 27013, 'proteomes': 10838, 'sets': 0, 'structural_models': {'alphafold': 20481, 'bfvd': 0}, 'structures': 31, 'taxa': 20455}"	"{}"	"[{'text': '<p>This entry represents the ornithine cyclodeaminase-Mu (OCD-MU) family of proteins which are widely distributed and contain proteins with diverse functions [[cite:PUB00163388]]. It includes the bacterial ornithine cyclodeaminase enzyme family, which catalyse the deamination of ornithine to proline [[cite:PUB00009476]]. The family also includes archaeal alanine dehydrogenase [[cite:PUB00017767]] and mu-crystallin, a mammalian homologue of bacterial ornithine cyclodeaminase [[cite:PUB00009477]], which is the major component of the eye lens in several Australian marsupials. mRNA for mu-crystallin has also been found in human retina  [[cite:PUB00009477]].</p>\n\n<p>This entry also includes protein SAR DEFICIENT 4 (SARD4) from Arabidopsis. SARD4  is involved in the biosynthesis of pipecolate (Pip), a metabolite that orchestrates defense amplification, positive regulation of salicylic acid (SA) biosynthesis, and priming to guarantee effective local resistance induction and the establishment of systemic acquired resistance (SAR) [[cite:PUB00086414]]. It does not possess ornithine cyclodeaminase activity in vitro [[cite:PUB00086415]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	"{'accession': 'IPR003462', 'name': 'Ornithine cyclodeaminase/mu-crystallin', 'type': 'Family', 'children': [{'accession': 'IPR014334', 'name': 'Ectoine utilization protein EutC', 'type': 'Family', 'children': []}, {'accession': 'IPR023866', 'name': '2,3-diaminopropionate biosynthesis protein SbnB', 'type': 'Family', 'children': []}, {'accession': 'IPR028609', 'name': 'Alanine dehydrogenase, archaeal-type', 'type': 'Family', 'children': [{'accession': 'IPR012742', 'name': 'Alanine dehydrogenase, Archaeoglobus-type', 'type': 'Family', 'children': []}]}]}"	""	False	False	False	"{'PUB00009476': {'PMID': 2644238, 'ISBN': None, 'volume': '171', 'issue': '2', 'year': 1989, 'title': 'Ornithine cyclodeaminase from octopine Ti plasmid Ach5: identification, DNA sequence, enzyme properties, and comparison with gene and enzyme from nopaline Ti plasmid C58.', 'URL': None, 'raw_pages': '847-54', 'medline_journal': 'J Bacteriol', 'ISO_journal': 'J. Bacteriol.', 'authors': ['Schindler U', 'Sans N', 'Schroder J.'], 'DOI_URL': 'http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2644238&action=stream&blobtype=pdf'}, 'PUB00009477': {'PMID': 1384048, 'ISBN': None, 'volume': '89', 'issue': '19', 'year': 1992, 'title': 'mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina.', 'URL': None, 'raw_pages': '9292-6', 'medline_journal': 'Proc Natl Acad Sci U S A', 'ISO_journal': 'Proc. Natl. Acad. Sci. U.S.A.', 'authors': ['Kim RY', 'Gasser R', 'Wistow GJ.'], 'DOI_URL': 'http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1384048'}, 'PUB00017767': {'PMID': 15516582, 'ISBN': None, 'volume': '186', 'issue': '22', 'year': 2004, 'title': 'A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin.', 'URL': None, 'raw_pages': '7680-9', 'medline_journal': 'J Bacteriol', 'ISO_journal': 'J. Bacteriol.', 'authors': ['Schroder I', 'Vadas A', 'Johnson E', 'Lim S', 'Monbouquette HG.'], 'DOI_URL': 'http://dx.doi.org/10.1128/JB.186.22.7680-7689.2004'}, 'PUB00086414': {'PMID': 27758894, 'ISBN': None, 'volume': '28', 'issue': '10', 'year': 2016, 'title': 'Characterization of a Pipecolic Acid Biosynthesis Pathway Required for Systemic Acquired Resistance.', 'URL': None, 'raw_pages': '2603-2615', 'medline_journal': 'Plant Cell', 'ISO_journal': 'Plant Cell', 'authors': ['Ding P', 'Rekhter D', 'Ding Y', 'Feussner K', 'Busta L', 'Haroth S', 'Xu S', 'Li X', 'Jetter R', 'Feussner I', 'Zhang Y.'], 'DOI_URL': 'https://doi.org/10.1105/tpc.16.00486'}, 'PUB00086415': {'PMID': 24237637, 'ISBN': None, 'volume': '13', 'issue': None, 'year': 2013, 'title': 'Functional characterization of an ornithine cyclodeaminase-like protein of Arabidopsis thaliana.', 'URL': None, 'raw_pages': '182', 'medline_journal': 'BMC Plant Biol', 'ISO_journal': 'BMC Plant Biol.', 'authors': ['Sharma S', 'Shinde S', 'Verslues PE.'], 'DOI_URL': 'https://doi.org/10.1186/1471-2229-13-182'}, 'PUB00163388': {'PMID': 34557391, 'ISBN': None, 'volume': '31', 'issue': None, 'year': 2021, 'title': 'Imine reduction by an Ornithine cyclodeaminase/μ-crystallin homolog purified from <i>Candida parapsilosis</i> ATCC 7330.', 'URL': None, 'raw_pages': 'e00664', 'medline_journal': 'Biotechnol Rep (Amst)', 'ISO_journal': 'Biotechnol Rep (Amst)', 'authors': ['Uma Mahesh VNM', 'Chadha A.'], 'DOI_URL': 'https://doi.org/10.1016/j.btre.2021.e00664'}}"	"{'panther': {'PTHR13812': 'KETIMINE REDUCTASE MU-CRYSTALLIN'}, 'pirsf': {'PIRSF001439': 'Ornithine cyclodeaminase'}, 'pfam': {'PF02423': 'Ornithine cyclodeaminase/mu-crystallin family'}}"	"{'name': 'Ornithine cyclodeaminase/mu-crystallin', 'short': 'ODC_Mu_crystall'}"	"[{'accession': 'IPR036291', 'name': 'NAD(P)-binding domain superfamily', 'type': 'homologous_superfamily'}, {'accession': 'IPR023401', 'name': 'Ornithine cyclodeaminase, N-terminal', 'type': 'homologous_superfamily'}]"	"{'accession': '4mp8', 'name': 'Staphyloferrin B precursor biosynthetic enzyme SbnB bound to malonate and NAD+'}"	""	"interpro"	"family"	""