ID T0S5A9_LACLC Unreviewed; 220 AA.
AC T0S5A9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN ORFNames=LLT6_06590 {ECO:0000313|EMBL:EQC53706.1};
OS Lactococcus cremoris subsp. cremoris TIFN6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1234876 {ECO:0000313|EMBL:EQC53706.1, ECO:0000313|Proteomes:UP000015854};
RN [1] {ECO:0000313|EMBL:EQC53706.1, ECO:0000313|Proteomes:UP000015854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIFN6 {ECO:0000313|EMBL:EQC53706.1,
RC ECO:0000313|Proteomes:UP000015854};
RX PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA Kleerebezem M., Smid E.J.;
RT "Multifactorial diversity sustains microbial community stability.";
RL ISME J. 7:2126-2136(2013).
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:EQC53706.1}.
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DR EMBL; ATBB01000716; EQC53706.1; -; Genomic_DNA.
DR AlphaFoldDB; T0S5A9; -.
DR PATRIC; fig|1234876.3.peg.3037; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000015854; 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; 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: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:UP000015854};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 220 AA; 24081 MW; 7FA5CF96528B1BA1 CRC64;
MTVKGLLVMD VDSTLIEEEV IDLLGEKAGL GEKISEITEA AMSGELDFKE ALKERVALLS
GLRTTIFDEI YKEIHLTNGA TGLIETLHGR GWKVGVVSGG FHEIVDKLAV DLKLDYVFAN
RLAVQEGYLT GETYGTIVDK SFKLERLKQW AKENKLDLSE VVAVGDGAND IPMLNAAGLG
IAFCAKPAVK AAVAYHIDKR NLLMVLELLE KYTDKQSLIN
//
