ID   A9II39_BORPD            Unreviewed;       285 AA.
AC   A9II39;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00015196};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN   Name=serB {ECO:0000313|EMBL:CAP42032.1};
GN   OrderedLocusNames=Bpet1693 {ECO:0000313|EMBL:CAP42032.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448 / CIP
OS   107267 / Se-1111R).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42032.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP42032.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448 / CIP 107267 / Se-1111R
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-D-serine + H2O = 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:0000256|ARBA:ARBA00048523};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-serine + H2O = 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:0000256|ARBA:ARBA00048138};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604469-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604469-3};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000256|ARBA:ARBA00009184}.
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DR   EMBL; AM902716; CAP42032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9II39; -.
DR   STRING; 94624.Bpet1693; -.
DR   KEGG; bpt:Bpet1693; -.
DR   eggNOG; COG0560; Bacteria.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR025138; DUF4072.
DR   InterPro; IPR050582; HAD-like_SerB.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   NCBIfam; TIGR00338; serB; 1.
DR   PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR   PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF13284; DUF4072; 1.
DR   Pfam; PF12710; HAD; 1.
DR   SFLD; SFLDG01137; C1.6.1:_Phosphoserine_Phosphat; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRSR:PIRSR604469-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAP42032.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604469-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604469-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001225};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|PIRSR:PIRSR604469-2}.
FT   DOMAIN          6..53
FT                   /note="DUF4072"
FT                   /evidence="ECO:0000259|Pfam:PF13284"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        84
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   BINDING         82..84
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-3"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-3"
FT   BINDING         114
FT                   /ligand="O-phospho-L-serine"
FT                   /ligand_id="ChEBI:CHEBI:57524"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         172..174
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         172..174
FT                   /ligand="O-phospho-L-serine"
FT                   /ligand_id="ChEBI:CHEBI:57524"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         217
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         217
FT                   /ligand="O-phospho-L-serine"
FT                   /ligand_id="ChEBI:CHEBI:57524"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-3"
FT   BINDING         243
FT                   /ligand="O-phospho-L-serine"
FT                   /ligand_id="ChEBI:CHEBI:57524"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
FT   BINDING         243
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-2"
SQ   SEQUENCE   285 AA;  30271 MW;  0261187D0F47FD9B CRC64;
     MPAHHLVIQS PALSAAQTEQ LAALAQAQGV MQLGATAARL LDVAHDDALR AQVTAWGEQH
     GVDTAFVPAG VRLSQCKVLA MDMDSTLINI ECIDEIAGVV GVKPKVAEIT EAAMRGEIKD
     FAESLRRRVA LLAGAPAAAL EQVYADKLRL NPGAERLVST ARAAGLKVLL VSGGFTFFTE
     RLRERLQLDS AHANTLEIRD GVLTGKVLGD ILDADAKLAH LRAFAQAHGA TPEQIIALGD
     GANDLKMLGA ARYAVAYRAK PIVRQQTPYA LNVSSLDGVL NWFEG
//