PSP_THET2
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 25-MAY-2022, entry version 96.
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 ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
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=ATCC BAA-163 / DSM 7039 / HB27;
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}.
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DR EMBL; AE017221; AAS82037.1; -; Genomic_DNA.
DR RefSeq; WP_011174058.1; NC_005835.1.
DR AlphaFoldDB; Q72H00; -.
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:0036424; F:L-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 InterPro; IPR044266; PSP_YsaA.
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
