ID   SERB_HALS3              Reviewed;         211 AA.
AC   B0R7U7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Phosphoserine phosphatase;
DE            Short=PSP;
DE            Short=PSPase;
DE            EC=3.1.3.3;
DE   AltName: Full=O-phosphoserine phosphohydrolase;
GN   Name=serB; OrderedLocusNames=OE_4405R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=R1M1;
RX   PubMed=19274099; DOI=10.1371/journal.pone.0004777;
RA   Aivaliotis M., Macek B., Gnad F., Reichelt P., Mann M., Oesterhelt D.;
RT   "Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium
RT   salinarum--a representative of the third domain of life.";
RL   PLoS ONE 4:E4777-E4777(2009).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser).
CC       {ECO:0000269|PubMed:19274099}.
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   -!- DISRUPTION PHENOTYPE: Strong increase of Ser protein phosphorylation.
CC       {ECO:0000269|PubMed:19274099}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000305}.
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DR   EMBL; AM774415; CAP14816.2; -; Genomic_DNA.
DR   RefSeq; WP_049892565.1; NC_010364.1.
DR   AlphaFoldDB; B0R7U7; -.
DR   SMR; B0R7U7; -.
DR   EnsemblBacteria; CAP14816; CAP14816; OE_4405R.
DR   GeneID; 1448811; -.
DR   GeneID; 5953380; -.
DR   KEGG; hsl:OE_4405R; -.
DR   HOGENOM; CLU_036368_4_3_2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000001321; 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; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00338; serB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Serine biosynthesis.
FT   CHAIN           1..211
FT                   /note="Phosphoserine phosphatase"
FT                   /id="PRO_0000428780"
FT   ACT_SITE        7
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   ACT_SITE        9
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         95..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
SQ   SEQUENCE   211 AA;  21053 MW;  A2EE4098BBD1DF94 CRC64;
     MTLVAFDFDG TLAESEMLDR IAARAGVGDE VAAITERAMR GELSYADSLR ERAQLVAGLP
     ESAAAAVYDG VRLRDGAGDL VAKLRDGGVR VVVLTGGFKP GVAAAFDAAG VAADGVVGNR
     LVAADGELTG AVEGPLVEGT KDDALRDACE AAGTTPAAAV AVGDGANDVP MLDAAGTAIG
     VDPKPGVDAH CDHTVSSMDA LGRVLDDHGI A