ID U2K8K7_9FIRM Unreviewed; 199 AA.
AC U2K8K7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
GN ORFNames=RUMCAL_01865 {ECO:0000313|EMBL:ERJ94846.1};
OS Ruminococcus callidus ATCC 27760.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ94846.1, ECO:0000313|Proteomes:UP000016662};
RN [1] {ECO:0000313|EMBL:ERJ94846.1, ECO:0000313|Proteomes:UP000016662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ94846.1,
RC ECO:0000313|Proteomes:UP000016662};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUL-2013) 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:ERJ94846.1}.
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DR EMBL; AWVF01000234; ERJ94846.1; -; Genomic_DNA.
DR RefSeq; WP_021683362.1; NZ_KI260480.1.
DR AlphaFoldDB; U2K8K7; -.
DR STRING; 411473.RUMCAL_01865; -.
DR GeneID; 78476294; -.
DR PATRIC; fig|411473.3.peg.1528; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_097498_0_0_9; -.
DR OrthoDB; 9801134at2; -.
DR Proteomes; UP000016662; 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; PF12710; HAD; 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 Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:ERJ94846.1}.
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 199 AA; 22336 MW; 343D6B4817CC122A CRC64;
MNIVCLDLEG VLVPEIWIAF AEESGIPELK RTTRDEPDYD KLMHWRLGIL KEHGLGLKEI
QETISKIEPL EGAKAFLDKL RELTQVIIIS DTFTQFAGPL MKKLGYPTIF CNSLEVAPDG
EITGFKMRCE NSKLTTVKAL QSIGYDTIAS GDSHNDLAMI QASKAGFLFR STEQIKKDYP
ELPAFESYDD LLHAIQQAL
//
