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{
"metadata": {
"accession": "cd04309",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "cdd",
"member_databases": null,
"integrated": null,
"hierarchy": null,
"name": {
"name": "phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase",
"short": "HAD_PSP_eu"
},
"description": [
{
"text": "<p>Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. [[cite:PUB00029151], [cite:PUB00026963], [cite:PUB00135312], [cite:PUB00085863], [cite:PUB00054023]]</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00085863": {
"PMID": 16889794,
"ISBN": null,
"volume": "361",
"issue": "5",
"year": 2006,
"title": "Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes.",
"URL": null,
"raw_pages": "1003-34",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Burroughs AM",
"Allen KN",
"Dunaway-Mariano D",
"Aravind L."
],
"DOI_URL": "https://doi.org/10.1016/j.jmb.2006.06.049"
},
"PUB00135312": {
"PMID": 10196182,
"ISBN": null,
"volume": "274",
"issue": "16",
"year": 1999,
"title": "Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana.",
"URL": null,
"raw_pages": "11007-12",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Ho CL",
"Noji M",
"Saito K."
],
"DOI_URL": null
},
"PUB00029151": {
"PMID": 12777757,
"ISBN": null,
"volume": "59",
"issue": "Pt 6",
"year": 2003,
"title": "High-resolution structure of human phosphoserine phosphatase in open conformation.",
"URL": null,
"raw_pages": "971-7",
"medline_journal": "Acta Crystallogr D Biol Crystallogr",
"ISO_journal": "Acta Crystallogr. D Biol. Crystallogr.",
"authors": [
"Peeraer Y",
"Rabijns A",
"Verboven C",
"Collet JF",
"Van Schaftingen E",
"De Ranter C."
],
"DOI_URL": "http://dx.doi.org/10.1107/S0907444903005407"
},
"PUB00026963": {
"PMID": 12213811,
"ISBN": null,
"volume": "277",
"issue": "48",
"year": 2002,
"title": "Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase.",
"URL": null,
"raw_pages": "46651-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Kim HY",
"Heo YS",
"Kim JH",
"Park MH",
"Moon J",
"Kim E",
"Kwon D",
"Yoon J",
"Shin D",
"Jeong EJ",
"Park SY",
"Lee TG",
"Jeon YH",
"Ro S",
"Cho JM",
"Hwang KY."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M204866200"
},
"PUB00054023": {
"PMID": 10567362,
"ISBN": null,
"volume": "274",
"issue": "48",
"year": 1999,
"title": "Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases.",
"URL": null,
"raw_pages": "33985-90",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Collet JF",
"Stroobant V",
"Van Schaftingen E."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.274.48.33985"
}
},
"set_info": {
"accession": "cl21460",
"name": "HAD_like"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 2566,
"pathways": 0,
"proteins": 2564,
"proteomes": 1543,
"sets": 1,
"structural_models": {
"alphafold": 2341,
"bfvd": 0
},
"structures": 8,
"taxa": 5239
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3kd3",
"name": "Crystal structure of a phosphoserine phosphohydrolase-like protein from Francisella tularensis subsp. tularensis SCHU S4"
}
}
}
