ID A0A264Y5S0_9BACT Unreviewed; 414 AA.
AC A0A264Y5S0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 Name=serB {ECO:0000313|EMBL:OZT03420.1};
GN ORFNames=CHL74_10545 {ECO:0000313|EMBL:OZT03420.1};
OS Prevotella sp. 885.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2022527 {ECO:0000313|EMBL:OZT03420.1, ECO:0000313|Proteomes:UP000216632};
RN [1] {ECO:0000313|EMBL:OZT03420.1, ECO:0000313|Proteomes:UP000216632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=885 {ECO:0000313|EMBL:OZT03420.1,
RC ECO:0000313|Proteomes:UP000216632};
RA Efimov B.A., Chaplin A.V., Kochetkova T.O., Sokolova S.R., Ogneva L.V.,
RA Rebrikov D.V., Kondova I., Langermans J.A., Shkoporov A.N.;
RT "Description of Prevotella sp. 885 sp. nov., isolated from rhesus macaque
RT feces.";
RL Submitted (JUL-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|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:OZT03420.1}.
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; NOVE01000036; OZT03420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264Y5S0; -.
DR OrthoDB; 9790031at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000216632; 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; cd04870; ACT_PSP_1; 1.
DR CDD; cd04871; ACT_PSP_2; 1.
DR CDD; cd07500; HAD_PSP; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; PF13740; ACT_6; 1.
DR Pfam; PF12710; HAD; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS51671; ACT; 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:UP000216632};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 12..84
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 414 AA; 46352 MW; 49F38764155B35A4 CRC64;
MEKTEIKEEQ ILIRITGNDR PGLTASIMEI LASKDAKILD IAQADIHSTL SLGILIRINE
DDSGQVMKEL LFKTTELGVQ IGFEPVTDDQ YEMWVGQQGK NRYILTLIGR SLSAKQIEAA
TKIITKQGLN IDSILRLTGR MSIKHPEQNR RACIEFSLRG TPTDRTLMQE ELMKISSEME
IDVSFQKDNM YRRMRRLICF DMDSTLIQTE CIDELAERAG VGDEVKAITE SAMRGEIDFK
ESFTRRVALL KGLDSRVFEE IAQKMPITEG VDRLMAVLKR CGYKIAILSG GFTYFGEFLQ
RKYGIDYVYA NELEVDDNGI LTGRYVGEIV DGHRKAELLK LIAQVEKVNL AQTIAVGDGA
NDLPMLGEAG LGIAFHAKPR VVANAKQSLN TIGIDGVLYF LGFKDSYLGE QGKF
//
