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Database: UniProt
Entry: A0A1E4UX60_9PSED
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ID   A0A1E4UX60_9PSED        Unreviewed;       404 AA.
AC   A0A1E4UX60;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=A7D25_14770 {ECO:0000313|EMBL:OEC34306.1};
OS   Pseudomonas sp. 21C1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1843690 {ECO:0000313|EMBL:OEC34306.1, ECO:0000313|Proteomes:UP000094259};
RN   [1] {ECO:0000313|EMBL:OEC34306.1, ECO:0000313|Proteomes:UP000094259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21C1 {ECO:0000313|EMBL:OEC34306.1,
RC   ECO:0000313|Proteomes:UP000094259};
RA   Souza V., Ponce-Soto G.Y.;
RT   "Genomic analysis from strains isolated from an enrichment experiment in
RT   Cuatro Cienegas.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OEC34306.1}.
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DR   EMBL; LXJR01000018; OEC34306.1; -; Genomic_DNA.
DR   RefSeq; WP_069519663.1; NZ_LXJR01000018.1.
DR   AlphaFoldDB; A0A1E4UX60; -.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000094259; 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; cd04870; ACT_PSP_1; 1.
DR   CDD; cd04871; ACT_PSP_2; 1.
DR   CDD; cd07500; HAD_PSP; 1.
DR   Gene3D; 3.30.70.260; -; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   InterPro; IPR049148; PSP_ACT.
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; PF13740; ACT_6; 1.
DR   Pfam; PF21086; ACT_PSP_2; 1.
DR   Pfam; PF12710; HAD; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS51671; ACT; 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   Reference proteome {ECO:0000313|Proteomes:UP000094259};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          6..81
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        196
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   404 AA;  43875 MW;  57CCB2C253DE84F7 CRC64;
     MREIVLINIT GEDRPGLTAA ITGVLASGGV TILDIGQAVI HDTLSFGILV EIPGTEQASS
     VLKDVLFTAY KLDQQVRFTP VTEADYQQWV AGQGKARHIV TLLTRKVTAE QLQRVSAITA
     RYDLNIDHID RLSGRMPLDT PLDQGKGCIE FSVRGEPQDP AALRAEFLSV AQALNVDIAF
     QRDSLFRRNR RLAVFDMDST LIEAEVIDEL AKAAGVGEQV SAITERAMRG ELDFAASFRE
     RLALLKGLPE TVLEDIGASL RLTEGAETLF AELKRLGYKT AILSGGFTYF AKQLQAKLGI
     DYVFANELQI VDGQVTGIAV EPIVDAQRKA DLLRELAAKE GLRLEQTIAV GDGANDLPML
     AIAGLGVAFR AKPLVKQSAK QAISTLGLDG ILYLLGFRDR DSLE
//
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