ID D5X1R5_THIK1 Unreviewed; 293 AA.
AC D5X1R5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00015196};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN OrderedLocusNames=Tint_1691 {ECO:0000313|EMBL:ADG31061.1};
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG31061.1};
RN [1] {ECO:0000313|EMBL:ADG31061.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 {ECO:0000313|EMBL:ADG31061.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) 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}.
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DR EMBL; CP002021; ADG31061.1; -; Genomic_DNA.
DR AlphaFoldDB; D5X1R5; -.
DR STRING; 75379.Tint_1691; -.
DR KEGG; tin:Tint_1691; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_036368_4_0_4; -.
DR BioCyc; TINT75379:TINT_RS08480-MONOMER; -.
DR UniPathway; UPA00135; UER00198.
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 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; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 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, ECO:0000313|EMBL:ADG31061.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 293 AA; 31427 MW; 07AFDA8F1792CBD7 CRC64;
MYHLVIQRHT APLSQDNLDH LCHIAAPISL EKFADDHGPN RGHNGARLRD IRSAGPGMRR
ALDAYCREHH IDWAIVPAGL HLGDFKLLAM DMDSTLINIE TVDEIGAAVG KKDEIAAITA
AAMRGEIADY ATSLRQRVAL LSRVPLASLD KLYTDTLRLN SGAETLLAAA KAAGLKTQLV
TGGFTHFTDR LKQRLGFDRV AANVLGVKGE ALDGTLIGDI IDGEAKKKAV LAFCDDLGCD
PGEVLVIGDG ANDLPMMNAV GFSVAYHAKP KVREAATAAI DHGGLDSLLH WFE
//
