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Database: UniProt
Entry: A0A165JV10_9BURK
LinkDB: A0A165JV10_9BURK
Original site: A0A165JV10_9BURK 
ID   A0A165JV10_9BURK        Unreviewed;       237 AA.
AC   A0A165JV10;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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   ORFNames=A1D30_18165 {ECO:0000313|EMBL:KZT14699.1};
OS   Acidovorax sp. GW101-3H11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT14699.1, ECO:0000313|Proteomes:UP000077219};
RN   [1] {ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA   Ray J., Price M., Deutschbauer A.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KZT14699.1, ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT14699.1,
RC   ECO:0000313|Proteomes:UP000077219};
RX   PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA   Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA   Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA   Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA   Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT   "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL   Nature 557:503-509(2018).
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:0000256|ARBA:ARBA00001197};
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:0000256|ARBA:ARBA00000860};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZT14699.1}.
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DR   EMBL; LUKZ01000019; KZT14699.1; -; Genomic_DNA.
DR   RefSeq; WP_063461885.1; NZ_LUKZ01000019.1.
DR   AlphaFoldDB; A0A165JV10; -.
DR   STRING; 1813946.A1D30_18165; -.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000077219; Unassembled WGS sequence.
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   CDD; cd07500; HAD_PSP; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; PF12710; HAD; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 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:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   ACT_SITE        31
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        33
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   237 AA;  25215 MW;  89134E257484542C CRC64;
     MTHATEFAPG LVVQGITPPL SLSAYKLIAF DMDSTLINIE CVDEIADAAG RKAEVAAITE
     AAMQGVITDY KESLRQRVAL LKGVTVQHME QVFTERLRFN PGAQELITAA KAAGLTTLLV
     SGGFTFFADR VKAGLGIDFA RSNMLEVQDG QLTGRMVDQA WGDICDGAEK RRTLLEVASL
     MGISPQQAIA VGDGANDLPM MGAAGLSVAY HAKPTVRAQA KVAINQGGLD RLLEVLR
//
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