SERB_SHIFL
ID SERB_SHIFL Reviewed; 322 AA.
AC P0AGB2; P06862;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SF4420, S4691;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45834.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19608.1; -; Genomic_DNA.
DR RefSeq; NP_710127.1; NC_004337.2.
DR RefSeq; WP_001132955.1; NZ_WPGW01000013.1.
DR AlphaFoldDB; P0AGB2; -.
DR SMR; P0AGB2; -.
DR STRING; 198214.SF4420; -.
DR EnsemblBacteria; AAN45834; AAN45834; SF4420.
DR EnsemblBacteria; AAP19608; AAP19608; S4691.
DR GeneID; 1025178; -.
DR GeneID; 66671724; -.
DR KEGG; sfl:SF4420; -.
DR KEGG; sfx:S4691; -.
DR PATRIC; fig|198214.7.peg.5209; -.
DR HOGENOM; CLU_036368_4_0_6; -.
DR OMA; CINEPDL; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 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..322
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000156889"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 35043 MW; A09A43BD846B7DE6 CRC64;
MPNITWCDLP EDVSLWPGLP LSLSGDEVMP LDYHAGRSGW LLYGRGLDKQ RLTQYQSKLG
AAMVIVAAWC VEDYQVIRLA GSLTARATRL AHEAQLDVAP LGKIPHLRTP GLLVMDMDST
AIQIECIDEI AKLAGTGEMV AEVTERAMRG ELDFTASLRS RVATLKGADA NILQQVRENL
PLMPGLTQLV LKLETLGWKV AIASGGFTFF AEYLRDKLRL TAVVANELEI MDGKFTGNVI
GDIVDAQYKA KTLTRLAQEY EIPLAQTVAI GDGANDLPMI KAAGLGIAYH AKPKVNEKAE
VTIRHADLMG VFCILSGSLN QK
