SERB_ECOLI
ID SERB_ECOLI Reviewed; 322 AA.
AC P0AGB0; P06862; Q2M5S9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphoserine phosphatase;
DE Short=PSP;
DE Short=PSPase;
DE EC=3.1.3.3;
DE AltName: Full=O-phosphoserine phosphohydrolase;
GN Name=serB; OrderedLocusNames=b4388, JW4351;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2997734; DOI=10.1093/nar/13.19.7025;
RA Neuwald A.F., Stauffer G.V.;
RT "DNA sequence and characterization of the Escherichia coli serB gene.";
RL Nucleic Acids Res. 13:7025-7039(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND COFACTOR.
RX PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia coli
RT haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(2006).
CC -!- FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser).
CC Also catalyzes the hydrolysis of phosphothreonine (P-Thr).
CC {ECO:0000269|PubMed:16990279}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also use other divalent metal
CC cations as Mn(2+), Co(2+) and Zn(2+). {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.097 mM for P-Ser (with magnesium ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=0.07 mM for imido-diphosphate (with magnesium ions as cofactor and
CC at pH 9) {ECO:0000269|PubMed:16990279};
CC KM=6.2 mM for acetyl-phosphate (with magnesium ions as cofactor and
CC at pH 9) {ECO:0000269|PubMed:16990279};
CC pH dependence:
CC Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; X03046; CAA26852.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97284.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77341.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78377.1; -; Genomic_DNA.
DR PIR; A24271; PAECS.
DR RefSeq; NP_418805.1; NC_000913.3.
DR RefSeq; WP_001132955.1; NZ_SSUV01000012.1.
DR AlphaFoldDB; P0AGB0; -.
DR SMR; P0AGB0; -.
DR BioGRID; 4262789; 119.
DR DIP; DIP-48100N; -.
DR IntAct; P0AGB0; 3.
DR STRING; 511145.b4388; -.
DR jPOST; P0AGB0; -.
DR PaxDb; P0AGB0; -.
DR PRIDE; P0AGB0; -.
DR EnsemblBacteria; AAC77341; AAC77341; b4388.
DR EnsemblBacteria; BAE78377; BAE78377; BAE78377.
DR GeneID; 66671724; -.
DR GeneID; 948913; -.
DR KEGG; ecj:JW4351; -.
DR KEGG; eco:b4388; -.
DR PATRIC; fig|1411691.4.peg.2297; -.
DR EchoBASE; EB0938; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_036368_4_0_6; -.
DR InParanoid; P0AGB0; -.
DR OMA; CINEPDL; -.
DR PhylomeDB; P0AGB0; -.
DR BioCyc; EcoCyc:PSERPHOSPHA-MON; -.
DR BioCyc; MetaCyc:PSERPHOSPHA-MON; -.
DR SABIO-RK; P0AGB0; -.
DR UniPathway; UPA00135; UER00198.
DR PRO; PR:P0AGB0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR GO; GO:0016791; F:phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IDA:EcoliWiki.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR InterPro; IPR041449; SerB_N.
DR Pfam; PF18429; DUF5609; 1.
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..322
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000156886"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 35043 MW; A09A43BD846B7DE6 CRC64;
MPNITWCDLP EDVSLWPGLP LSLSGDEVMP LDYHAGRSGW LLYGRGLDKQ RLTQYQSKLG
AAMVIVAAWC VEDYQVIRLA GSLTARATRL AHEAQLDVAP LGKIPHLRTP GLLVMDMDST
AIQIECIDEI AKLAGTGEMV AEVTERAMRG ELDFTASLRS RVATLKGADA NILQQVRENL
PLMPGLTQLV LKLETLGWKV AIASGGFTFF AEYLRDKLRL TAVVANELEI MDGKFTGNVI
GDIVDAQYKA KTLTRLAQEY EIPLAQTVAI GDGANDLPMI KAAGLGIAYH AKPKVNEKAE
VTIRHADLMG VFCILSGSLN QK
