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Database: UniProt
Entry: A0A1Y3XBP4_9FIRM
LinkDB: A0A1Y3XBP4_9FIRM
Original site: A0A1Y3XBP4_9FIRM 
ID   A0A1Y3XBP4_9FIRM        Unreviewed;       200 AA.
AC   A0A1Y3XBP4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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=B5G06_08695 {ECO:0000313|EMBL:OUN82965.1};
OS   Flavonifractor sp. An52.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Flavonifractor.
OX   NCBI_TaxID=1965642 {ECO:0000313|EMBL:OUN82965.1, ECO:0000313|Proteomes:UP000195424};
RN   [1] {ECO:0000313|Proteomes:UP000195424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An52 {ECO:0000313|Proteomes:UP000195424};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUN82965.1}.
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DR   EMBL; NFIB01000019; OUN82965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3XBP4; -.
DR   Proteomes; UP000195424; 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:0016740; F:transferase activity; 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:UP000195424};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000313|EMBL:OUN82965.1}.
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   200 AA;  22399 MW;  FBEFEA56AB4D9A57 CRC64;
     MYITCLDMEG VLVPEIWIAF SEATGIPELR RTTRDEPDYN KLMQFRLDIL KEHGLGLKEI
     QNTIATIDPL PGAKEFLDEL RSFSQVIILS DTFEQFAQPL MKKLGWPTLM CNTLEVADDG
     TITGFQMRCP QSKLTTVKAL QSIGYDTIAA GDSFNDLGMI QASKAGFLFK STDQIKADHP
     ELPAYEEFPD LLAAIRNAMD
//
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