ID A0A1E4UYS1_9PSED Unreviewed; 205 AA.
AC A0A1E4UYS1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
GN ORFNames=A7D25_12170 {ECO:0000313|EMBL:OEC34852.1};
OS Pseudomonas sp. 21C1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1843690 {ECO:0000313|EMBL:OEC34852.1, ECO:0000313|Proteomes:UP000094259};
RN [1] {ECO:0000313|EMBL:OEC34852.1, ECO:0000313|Proteomes:UP000094259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21C1 {ECO:0000313|EMBL:OEC34852.1,
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|PIRSR:PIRSR611863-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR611863-3};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
CC -!- 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:OEC34852.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LXJR01000012; OEC34852.1; -; Genomic_DNA.
DR RefSeq; WP_069519145.1; NZ_LXJR01000012.1.
DR AlphaFoldDB; A0A1E4UYS1; -.
DR OrthoDB; 9801134at2; -.
DR Proteomes; UP000094259; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.90.1470.10; thrh gene product, domain 2; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011863; HSK-PSP.
DR NCBIfam; TIGR02137; HSK-PSP; 1.
DR PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
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 ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-1"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-1"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 90..91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
SQ SEQUENCE 205 AA; 23555 MW; B6445FB2CD70E0C7 CRC64;
MEIACLDLEG VLVPEIWIAF AEKTGIDALK ATTRDIPDYD VLMQQRLRIL DEHGLKLRDI
QEVIATLKPL EGAVEFVDWL RERFQVVILS DTFYEFSQPL MRQLGFPTLL CHKLITDDSD
RVVSYQLRQK DPKRQSVIAF KSLYYRVIAA GDSYNDTTML SEAHAGILFH APDNVIREFP
QFPAVHTFAD LKQEFLKASN RPLSL
//
