SERB_POLSJ
ID SERB_POLSJ Reviewed; 236 AA.
AC Q12A06;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000305|PubMed:25848029};
DE Short=PSP {ECO:0000250|UniProtKB:Q58989};
DE Short=PSPase {ECO:0000250|UniProtKB:Q58989};
DE EC=3.1.3.3 {ECO:0000269|PubMed:25848029};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000250|UniProtKB:Q58989};
GN Name=serB {ECO:0000250|UniProtKB:P0AGB0};
GN OrderedLocusNames=Bpro_2720 {ECO:0000312|EMBL:ABE44636.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000312|Proteomes:UP000001983};
RN [1] {ECO:0000312|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000312|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
RN [2] {ECO:0000305}
RP 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 -!- 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 -!- 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 HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; CP000316; ABE44636.1; -; Genomic_DNA.
DR RefSeq; WP_011483634.1; NC_007948.1.
DR AlphaFoldDB; Q12A06; -.
DR SMR; Q12A06; -.
DR STRING; 296591.Bpro_2720; -.
DR EnsemblBacteria; ABE44636; ABE44636; Bpro_2720.
DR KEGG; pol:Bpro_2720; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_036368_4_3_4; -.
DR OMA; CINEPDL; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000001983; 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; IPR004469; PSP.
DR SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..236
FT /note="Phosphoserine phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435618"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 32
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 120..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 236 AA; 25646 MW; 8F3F45713036C43F CRC64;
MQPTEISPGL VVNVATPDLK LSDFKLIAFD MDSTLINIEC VDEIADAAGR KAEVAAITEA
AMRGEISDYK ESLRQRVALL KGVSVASMDE VYRTRLRLNP GAARLVQACK DAGLKVLLVS
GGFTFFTDRI RDELGIDYTR SNVLETTDGL LTGRMVDQPW GDICDGEEKR KMLLETCGQL
GISPRQAIAM GDGANDLPMM GEAGLSVAYH AKPRVREQAM VAINEGGLDR LLELVK
