SERB_SCHPO
ID SERB_SCHPO Reviewed; 298 AA.
AC O74382; P78910;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable phosphoserine phosphatase;
DE Short=PSP;
DE Short=PSPase;
DE EC=3.1.3.3;
DE AltName: Full=O-phosphoserine phosphohydrolase;
GN ORFNames=SPBC3H7.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13922.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D89261; BAA13922.1; ALT_FRAME; mRNA.
DR EMBL; CU329671; CAA20303.1; -; Genomic_DNA.
DR PIR; T40408; T40408.
DR PIR; T43186; T43186.
DR RefSeq; NP_595768.1; NM_001021669.2.
DR AlphaFoldDB; O74382; -.
DR SMR; O74382; -.
DR BioGRID; 277484; 69.
DR STRING; 4896.SPBC3H7.07c.1; -.
DR MaxQB; O74382; -.
DR PaxDb; O74382; -.
DR EnsemblFungi; SPBC3H7.07c.1; SPBC3H7.07c.1:pep; SPBC3H7.07c.
DR GeneID; 2540968; -.
DR KEGG; spo:SPBC3H7.07c; -.
DR PomBase; SPBC3H7.07c; -.
DR VEuPathDB; FungiDB:SPBC3H7.07c; -.
DR eggNOG; KOG1615; Eukaryota.
DR HOGENOM; CLU_036368_4_3_1; -.
DR InParanoid; O74382; -.
DR OMA; DYAVANQ; -.
DR PhylomeDB; O74382; -.
DR Reactome; R-SPO-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00198.
DR PRO; PR:O74382; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; ISO:PomBase.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..298
FT /note="Probable phosphoserine phosphatase"
FT /id="PRO_0000156884"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170..171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 32411 MW; 4BCBCE73E9013CA5 CRC64;
MVNAAIVVSS NRPNVLEQIS SLFRDGKTRS LGEQWTLVSG QLKGTFEDAK DACNRISATE
NVDCNCLSEA TFSTKKKLVV FDMDSTLIQQ ECIDELAAEA GIQKEVATIT SLAMNGEIDF
QESLRRRVSL LQGLSVDVIN KVIGKITFTP GAKQLCHCLK QMGATLVVAS GGFVPMAEYV
KGQLDLDYAY ANVLEFSDDG KFLTGKVQGA IVDGQRKASI LREKREELGL NKLETMAVGD
GANDLVMMAE SGLGIAFKAK PKVQLLADSK INLPSLQNAL YLLGIDEQQQ KKLLENKN
