{"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"}}}