ID   SERB_ARCFU              Reviewed;         344 AA.
AC   O28142;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Phosphoserine phosphatase;
DE            Short=PSP;
DE            Short=PSPase;
DE            EC=3.1.3.3;
DE   AltName: Full=O-phosphoserine phosphohydrolase;
GN   OrderedLocusNames=AF_2138;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 3/3.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000305}.
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DR   EMBL; AE000782; AAB89113.1; -; Genomic_DNA.
DR   PIR; B69517; B69517.
DR   AlphaFoldDB; O28142; -.
DR   SMR; O28142; -.
DR   STRING; 224325.AF_2138; -.
DR   EnsemblBacteria; AAB89113; AAB89113; AF_2138.
DR   KEGG; afu:AF_2138; -.
DR   eggNOG; arCOG01158; Archaea.
DR   HOGENOM; CLU_036368_4_0_2; -.
DR   OMA; FAAHAGC; -.
DR   PhylomeDB; O28142; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000002199; Chromosome.
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; -; 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   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00338; serB; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome; Serine biosynthesis.
FT   CHAIN           1..344
FT                   /note="Phosphoserine phosphatase"
FT                   /id="PRO_0000156890"
FT   DOMAIN          48..120
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   344 AA;  38515 MW;  2922DBBFD210BBD4 CRC64;
     MFVMFIVAEV DDEVCVKREV ERAAGEVGVH VSLTPFQRRE KAEKNLYVVT ILGKDRVGIV
     RDITRAFLDF GINIERTSLT AREELISIEF LVDLGQRDAA EVRKRLRREA ERLGLDIVMQ
     PYSTFNREKR LIVFDMDSTL VEAEIIDELA KEAGVGDEVS KLTERAMRGE IGFKEALEER
     VRLLKGLPVE VLERIYSRIK LTEGAKELVR SLKEAGYKVA VVSGGFSYFT DRLKEELGLD
     YAFGNELEIE NGRLTGRIKG RIIDASEKAR IVEEIARKEG ISPENVVAVG DGANDRLMIE
     RAGLGIAFNA KEVLKDVADG SISKENLVGL ASVLKLPAEF RKKV