SERB_CAMJD
ID SERB_CAMJD Reviewed; 207 AA.
AC A7H590;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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:0000312|EMBL:ABS43618.1};
GN OrderedLocusNames=JJD26997_1689 {ECO:0000312|EMBL:ABS43618.1};
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109 {ECO:0000312|Proteomes:UP000002302};
RN [1] {ECO:0000312|Proteomes:UP000002302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97 {ECO:0000312|Proteomes:UP000002302};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000768; ABS43618.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H590; -.
DR SMR; A7H590; -.
DR PRIDE; A7H590; -.
DR EnsemblBacteria; ABS43618; ABS43618; JJD26997_1689.
DR KEGG; cjd:JJD26997_1689; -.
DR HOGENOM; CLU_036368_4_3_7; -.
DR OMA; CINEPDL; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000002302; 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 Serine biosynthesis.
FT CHAIN 1..207
FT /note="Phosphoserine phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435615"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 96..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 207 AA; 22966 MW; CF9FC5D03B43E97F CRC64;
MIKLCVFDFD ATLMDGETID ILATAHGKGN QISEITRYAM AGELDFFESL QKRVSFLKGM
SYKKVLELGS TLPLMHGAHE LIQYLKSKNI QIVIFSGGFH EGIDPAMQKL GINLGFANYL
HHKNDILTGL IGGEIMFSNS KGLMLQRLKS FLNLKTDEVM CVGDGANDLA MFNESGLKIA
FCAKEILRSQ ADICIDIKDL KEIIKVI
