ID PSP_THET2 Reviewed; 249 AA. AC Q72H00; DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-DEC-2020, entry version 92. DE RecName: Full=Phosphoserine phosphatase {ECO:0000303|PubMed:30430741}; DE Short=PSP {ECO:0000303|PubMed:30430741}; DE EC=3.1.3.3 {ECO:0000269|PubMed:30430741}; GN OrderedLocusNames=TT_C1695 {ECO:0000312|EMBL:AAS82037.1}; OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, PATHWAY, AND SUBUNIT. RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039; RX PubMed=30430741; DOI=10.1111/febs.14703; RA Chiba Y., Yoshida A., Shimamura S., Kameya M., Tomita T., Nishiyama M., RA Takai K.; RT "Discovery and analysis of a novel type of the serine biosynthetic enzyme RT phosphoserine phosphatase in Thermus thermophilus."; RL FEBS J. 286:726-736(2019). CC -!- FUNCTION: Catalyzes the last step of the phosphorylated serine CC biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to CC form L-serine. Is also able to dephosphorylate O-phospho-D-serine with CC similar efficiency. Displays a poor activity on L-phosphothreonine, and CC cannot use L-phosphotyrosine, pyridoxal phosphate, glucose 6-phosphate, CC or fructose 6-phosphate as substrates. {ECO:0000269|PubMed:30430741}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; CC Evidence={ECO:0000269|PubMed:30430741}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21209; CC Evidence={ECO:0000269|PubMed:30430741}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3; CC Evidence={ECO:0000269|PubMed:30430741}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24874; CC Evidence={ECO:0000305|PubMed:30430741}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:30430741}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:30430741}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.25 mM for O-phospho-L-serine (at pH 7.0 and 70 degrees Celsius) CC {ECO:0000269|PubMed:30430741}; CC Vmax=0.55 umol/min/mg enzyme (at pH 7.0 and 70 degrees Celsius) for CC the dephosphorylation of O-phospho-L-serine CC {ECO:0000269|PubMed:30430741}; CC Note=kcat is 1506 sec(-1) (at pH 7.0 and 70 degrees Celsius) for the CC dephosphorylation of O-phospho-L-serine. CC {ECO:0000269|PubMed:30430741}; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from CC 3-phospho-D-glycerate: step 3/3. {ECO:0000269|PubMed:30430741}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30430741}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show serine auxotrophy CC when grown in a synthetic MP medium, in contrast to wild type. Addition CC of L-serine to the medium restores growth of the deletion mutant. CC {ECO:0000269|PubMed:30430741}. CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC {ECO:0000255|HAMAP-Rule:MF_02240, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017221; AAS82037.1; -; Genomic_DNA. DR RefSeq; WP_011174058.1; NC_005835.1. DR SMR; Q72H00; -. DR STRING; 262724.TT_C1695; -. DR EnsemblBacteria; AAS82037; AAS82037; TT_C1695. DR KEGG; tth:TT_C1695; -. DR eggNOG; COG1011; Bacteria. DR HOGENOM; CLU_045011_8_0_0; -. DR OMA; DHTLWDF; -. DR OrthoDB; 1204073at2; -. DR UniPathway; UPA00135; UER00198. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IDA:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB. DR GO; GO:0006564; P:L-serine biosynthetic process; IMP:UniProtKB. DR Gene3D; 3.40.50.1000; -; 1. DR HAMAP; MF_02240; PSP; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR041492; HAD_2. DR InterPro; IPR023214; HAD_sf. DR Pfam; PF13419; HAD_2; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Cobalt; Hydrolase; Magnesium; Serine biosynthesis. FT CHAIN 1..249 FT /note="Phosphoserine phosphatase" FT /id="PRO_0000448615" SQ SEQUENCE 249 AA; 27436 MW; 444693D6D07DAD0E CRC64; MKLLLLDLDD TLLQDLPVSR AVLEDLGRKA GVEGFFARVK ARAEALFREA PFYPWAEAIG HSALEALWAR YSTPGLEALA AWAGPFRERV FREALEEAGG APERARELAE AFFRERRRYP LYPEAEAFLA EARRRGLALA LLTNGVPDLQ REKLVGAGLA HHFSLVLISG EVGIGKPDPR LFRMALCAFG VAPEEAAMVG DNPQKDVRGA RLAGVRAVWV DRGLRPEDPE ASPDLRVGDL REVFLAEAL //