ID A0A1H3J7U4_9FIRM Unreviewed; 208 AA.
AC A0A1H3J7U4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
GN ORFNames=SAMN02910414_01366 {ECO:0000313|EMBL:SDY35498.1};
OS Lachnobacterium bovis DSM 14045.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnobacterium.
OX NCBI_TaxID=1122142 {ECO:0000313|EMBL:SDY35498.1, ECO:0000313|Proteomes:UP000183918};
RN [1] {ECO:0000313|EMBL:SDY35498.1, ECO:0000313|Proteomes:UP000183918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14045 {ECO:0000313|EMBL:SDY35498.1,
RC ECO:0000313|Proteomes:UP000183918};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNPG01000014; SDY35498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3J7U4; -.
DR STRING; 1122142.SAMN02910414_01366; -.
DR Proteomes; UP000183918; 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:UP000183918};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-1"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-1"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 95..96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
SQ SEQUENCE 208 AA; 23802 MW; 4938019F70152076 CRC64;
MKKNEMFIVC LDLEGVLVPE IWIEFAKETG IEELKKTTRD EPDYDKLMKY RLDILKKNSL
GLKEIQETIS KIDPMDGAKE FLDELRSFAQ VIIVSDTFYQ FAQPLMKKLG YPTIFCNNLI
VGENGQIDDY QMRVENTKLT TVRALQTAGF ETVASGDSYN DLSMIKASKA GFLFRSTDEI
KKSNPEIKAL ETYEELLSEI KKVVSKNN
//
