THRH_PSESM
ID THRH_PSESM Reviewed; 237 AA.
AC Q883R9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000305|PubMed:25848029};
DE Short=PSP {ECO:0000250|UniProtKB:Q9I2Y2};
DE Short=PSPase {ECO:0000250|UniProtKB:Q9I2Y2};
DE EC=3.1.3.3 {ECO:0000269|PubMed:25848029};
GN OrderedLocusNames=PSPTO_2281 {ECO:0000312|EMBL:AAO55795.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000312|Proteomes:UP000002515};
RN [1] {ECO:0000312|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000312|EMBL:AAO55795.1,
RC ECO:0000312|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC -!- FUNCTION: Phosphoserine phosphatase that mediates dephosphorylation of
CC phospho-serine in the serine biosynthesis pathway. Also able to
CC dephosphorylate phospho-threonine (PubMed:25848029).
CC {ECO:0000269|PubMed:25848029}.
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:25848029};
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:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9I2Y2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thrH family. {ECO:0000305}.
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DR EMBL; AE016853; AAO55795.1; -; Genomic_DNA.
DR RefSeq; NP_792100.1; NC_004578.1.
DR AlphaFoldDB; Q883R9; -.
DR SMR; Q883R9; -.
DR STRING; 223283.PSPTO_2281; -.
DR DNASU; 1183932; -.
DR EnsemblBacteria; AAO55795; AAO55795; PSPTO_2281.
DR KEGG; pst:PSPTO_2281; -.
DR PATRIC; fig|223283.9.peg.2315; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_097498_0_0_6; -.
DR OMA; YNDTAML; -.
DR OrthoDB; 1755462at2; -.
DR PhylomeDB; Q883R9; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011863; HSK-PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02137; HSK-PSP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..237
FT /note="Phosphoserine phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435469"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9I2Y2"
FT ACT_SITE 41
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9I2Y2"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9I2Y2"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9I2Y2"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 122..123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9I2Y2"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 237 AA; 26933 MW; 1E4E946734B62F63 CRC64;
MAAMVTKSAV QWPLPEARVP LPLILNAVGE CAVEIACLDL EGVLVPEIWI AFAEKTGIES
LRATTRDIPD YDVLMKQRLR ILDEHGLKLA DIQAVISTLK PLEGAVEFVD WLRERFQVVI
LSDTFYEFSQ PLMRQLGFPT LLCHRLITDE TDRVVSYQLR QKDPKRQSVL AFKSLYYRII
AAGDSYNDTT MLGEADAGIL FHAPDNVIRE FPQFPAVHTF DELKKEFIKA SNRELVL
