ID   SERB_HAEIN              Reviewed;         314 AA.
AC   P44997;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=HI_1033;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser).
CC       {ECO:0000250}.
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; L42023; AAC22693.1; -; Genomic_DNA.
DR   PIR; I64108; I64108.
DR   RefSeq; NP_439193.1; NC_000907.1.
DR   RefSeq; WP_010869109.1; NC_000907.1.
DR   AlphaFoldDB; P44997; -.
DR   SMR; P44997; -.
DR   STRING; 71421.HI_1033; -.
DR   EnsemblBacteria; AAC22693; AAC22693; HI_1033.
DR   KEGG; hin:HI_1033; -.
DR   PATRIC; fig|71421.8.peg.1077; -.
DR   eggNOG; COG0560; Bacteria.
DR   HOGENOM; CLU_036368_4_0_6; -.
DR   OMA; CINEPDL; -.
DR   PhylomeDB; P44997; -.
DR   BioCyc; HINF71421:G1GJ1-1073-MON; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   InterPro; IPR041449; SerB_N.
DR   Pfam; PF18429; DUF5609; 1.
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   Reference proteome; Serine biosynthesis.
FT   CHAIN           1..314
FT                   /note="Phosphoserine phosphatase"
FT                   /id="PRO_0000156888"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34720 MW;  ED565F9C78CE0FB1 CRC64;
     MQIQCFESIT QKYPQFPTAL LANEEPIQNG EPFILYGTKL DITKLEKFQQ KCGQNFQIFD
     VWMVAKNIIV LLKGQWFSDF IKFTHDVEVD IAKLDFSPKL SQAGLLVMDM DSTAIQIECI
     DEIAKLAGVG ELVSAITESA MRGELDFEQS LRCRVGTLKG APESILQQVR ENLPLMSGLV
     ETIQTLQKYG WKTAIASGGF TYFADYLKAL LQLDFAASNQ FDIEDGKLTG LVKGDVVDAQ
     YKAKTLQHLL EEYGIDSRHS IAIGDGANDL AMMNVAGLGV AFHAKPKVQP QAQIVVNFAD
     LTALLCLLSA NDRI