ID   SERB_YEAST              Reviewed;         309 AA.
AC   P42941; D6VUZ1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   10-JUN-2026, entry version 187.
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=SER2; OrderedLocusNames=YGR208W; ORFNames=G7744;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RA   Song J.M., Cheung E., Rabinowitz J.C.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8904340;
RX   DOI=10.1002/(sici)1097-0061(19960315)12:3%3c273::aid-yea898%3e3.0.co;2-1;
RA   Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA   Rodrigues-Pousada C.;
RT   "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT   reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT   yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT   flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT   phosphohydrolase, and five new ORFs.";
RL   Yeast 12:273-280(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869; DOI=10.1038/387s081;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-serine + H2O = 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=O-phospho-D-serine + H2O = 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   -!- MISCELLANEOUS: Present with 13800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000305}.
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DR   EMBL; U36473; AAA79062.1; -; Genomic_DNA.
DR   EMBL; Z49133; CAA89001.1; -; Genomic_DNA.
DR   EMBL; Z72993; CAA97235.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08302.1; -; Genomic_DNA.
DR   PIR; S53931; S53931.
DR   RefSeq; NP_011724.1; NM_001181337.1.
DR   AlphaFoldDB; P42941; -.
DR   SMR; P42941; -.
DR   BioGRID; 33461; 288.
DR   DIP; DIP-2085N; -.
DR   FunCoup; P42941; 670.
DR   IntAct; P42941; 17.
DR   STRING; 4932.YGR208W; -.
DR   iPTMnet; P42941; -.
DR   PaxDb; 4932-YGR208W; -.
DR   PeptideAtlas; P42941; -.
DR   EnsemblFungi; YGR208W_mRNA; YGR208W; YGR208W.
DR   GeneID; 853122; -.
DR   KEGG; sce:YGR208W; -.
DR   AGR; SGD:S000003440; -.
DR   SGD; S000003440; SER2.
DR   VEuPathDB; FungiDB:YGR208W; -.
DR   eggNOG; KOG1615; Eukaryota.
DR   HOGENOM; CLU_036368_4_0_1; -.
DR   InParanoid; P42941; -.
DR   OMA; LSMFKHA; -.
DR   OrthoDB; 27226at2759; -.
DR   BioCyc; YEAST:YGR208W-MONOMER; -.
DR   BRENDA; 3.1.3.3; 984.
DR   Reactome; R-SCE-977347; Serine metabolism.
DR   UniPathway; UPA00135; UER00198.
DR   BioGRID-ORCS; 853122; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P42941; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P42941; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IMP:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IMP:SGD.
DR   CDD; cd07500; HAD_PSP; 1.
DR   FunFam; 3.40.50.1000:FF:000283; Phosphoserine phosphatase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR050582; HAD-like_SerB.
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; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01137; C1.6.1:_Phosphoserine_Phosphat; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome; Serine biosynthesis.
FT   CHAIN           1..309
FT                   /note="Phosphoserine phosphatase"
FT                   /id="PRO_0000156885"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  34207 MW;  11CD560B3A96172B CRC64;
     MSKFVITCIA HGENLPKETI DQIAKEITES SAKDVSINGT KKLSARATDI FIEVAGSIVQ
     KDLKNKLTNV IDSHNDVDVI VSVDNEYRQA KKLFVFDMDS TLIYQEVIEL IAAYAGVEEQ
     VHEITERAMN NELDFKESLR ERVKLLQGLQ VDTLYDEIKQ KLEVTKGVPE LCKFLHKKNC
     KLAVLSGGFI QFAGFIKDQL GLDFCKANLL EVDTDGKLTG KTLGPIVDGQ CKSETLLQLC
     NDYNVPVEAS CMVGDGGNDL PAMATAGFGI AWNAKPKVQK AAPCKLNTKS MTDILYILGY
     TDDEIYNRQ
//