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{
"metadata": {
"accession": "IPR049943",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR11680": "SERINE HYDROXYMETHYLTRANSFERASE"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR049943",
"name": "Serine hydroxymethyltransferase-like",
"type": "Family",
"children": [
{
"accession": "IPR001085",
"name": "Serine hydroxymethyltransferase",
"type": "Family",
"children": []
},
{
"accession": "IPR030979",
"name": "Fluorothreonine transaldolase",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Serine hydroxymethyltransferase-like",
"short": "Ser_HO-MeTrfase-like"
},
"description": [
{
"text": "<p>This entry includes serine hydroxymethyltransferases, transaldolases and other uncharacterised proteins.</p>\n\n<p>Serine hydroxymethyltransferase is a pyridoxal phosphate (PLP) requiring enzyme whose physiological role is to catalyse the formation of single carbon groups for a number of biosynthetic pathways. It catalyses the reversible interconversion of serine and glycine with tetrahydrofolate serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Serine hydroxymethyltransferase adopts an α/β structure consisting of a mixed β-sheet and α-helices packed on both sides of it [[cite:PUB00028352]].</p>\n\n<p>This entry also includes L-threonine:uridine-5'-aldehyde transaldolase and fluorothreonine transaldolase. L-threonine:uridine-5'-aldehyde transaldolase is involved in the biosynthesis of the capuramycin-type nucleoside antibiotic A-102395 [[cite:PUB00153411]]. This enzyme catalyses the condensation of L-threonine and uridine-5'-aldehyde to form 5'-C-glycyluridine [[cite:PUB00153411], [cite:PUB00153412]]. Fluorothreonine transaldolase catalyses the final step in 4-fluorothreonine biosynthesis. Mediates a L-threonine/fluoroaceldehyde to 4-fluoro-L-threonine/acetaldehyde crossover reaction. It can also convert chloroacetaldehyde into 4-chloro-L-threonine [[cite:PUB00089683]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00028352": {
"PMID": 10656824,
"ISBN": null,
"volume": "296",
"issue": "1",
"year": 2000,
"title": "Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate.",
"URL": null,
"raw_pages": "155-68",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Scarsdale JN",
"Radaev S",
"Kazanina G",
"Schirch V",
"Wright HT."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1999.3453"
},
"PUB00153411": {
"PMID": 25855790,
"ISBN": null,
"volume": "290",
"issue": "22",
"year": 2015,
"title": "The Biosynthesis of Capuramycin-type Antibiotics: IDENTIFICATION OF THE A-102395 BIOSYNTHETIC GENE CLUSTER, MECHANISM OF SELF-RESISTANCE, AND FORMATION OF URIDINE-5'-CARBOXAMIDE.",
"URL": null,
"raw_pages": "13710-24",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Cai W",
"Goswami A",
"Yang Z",
"Liu X",
"Green KD",
"Barnard-Britson S",
"Baba S",
"Funabashi M",
"Nonaka K",
"Sunkara M",
"Morris AJ",
"Spork AP",
"Ducho C",
"Garneau-Tsodikova S",
"Thorson JS",
"Van Lanen SG."
],
"DOI_URL": "https://doi.org/10.1074/jbc.M115.646414"
},
"PUB00153412": {
"PMID": 29343643,
"ISBN": null,
"volume": "115",
"issue": "5",
"year": 2018,
"title": "Pyridoxal-5'-phosphate as an oxygenase cofactor: Discovery of a carboxamide-forming, α-amino acid monooxygenase-decarboxylase.",
"URL": null,
"raw_pages": "974-979",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc Natl Acad Sci U S A",
"authors": [
"Huang Y",
"Liu X",
"Cui Z",
"Wiegmann D",
"Niro G",
"Ducho C",
"Song Y",
"Yang Z",
"Van Lanen SG."
],
"DOI_URL": "https://doi.org/10.1073/pnas.1718667115"
},
"PUB00089683": {
"PMID": 19101471,
"ISBN": null,
"volume": "15",
"issue": "12",
"year": 2008,
"title": "In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase.",
"URL": null,
"raw_pages": "1268-76",
"medline_journal": "Chem Biol",
"ISO_journal": "Chem. Biol.",
"authors": [
"Deng H",
"Cross SM",
"McGlinchey RP",
"Hamilton JT",
"O'Hagan D."
],
"DOI_URL": "https://doi.org/10.1016/j.chembiol.2008.10.012"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR015424",
"name": "Pyridoxal phosphate-dependent transferase",
"type": "homologous_superfamily"
},
{
"accession": "IPR015422",
"name": "Pyridoxal phosphate-dependent transferase, small domain",
"type": "homologous_superfamily"
},
{
"accession": "IPR015421",
"name": "Pyridoxal phosphate-dependent transferase, major domain",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 48911,
"pathways": 29,
"proteins": 48911,
"proteomes": 20919,
"sets": 0,
"structural_models": {
"alphafold": 38895,
"bfvd": 0
},
"structures": 177,
"taxa": 39593
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.1.2",
"url": "https://enzyme.expasy.org/EC/2.1.2"
},
{
"accession": "2.1.2.1",
"url": "https://enzyme.expasy.org/EC/2.1.2.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6smw",
"name": "A. thaliana serine hydroxymethyltransferase isoform 2 (AtSHMT2) in complex with pemetrexed"
}
}
}
