SERB_IDILO
ID SERB_IDILO Reviewed; 220 AA.
AC Q5QXU4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000305|PubMed:25848029};
DE Short=PSP {ECO:0000250|UniProtKB:Q58989};
DE Short=PSPase {ECO:0000250|UniProtKB:Q58989};
DE EC=3.1.3.3 {ECO:0000269|PubMed:25848029};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000250|UniProtKB:Q58989};
GN Name=serB_2 {ECO:0000312|EMBL:AAV82708.1};
GN OrderedLocusNames=IL1876 {ECO:0000312|EMBL:AAV82708.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000312|Proteomes:UP000001171};
RN [1] {ECO:0000312|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000312|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
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 Evidence={ECO:0000269|PubMed:25848029};
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 Evidence={ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; AE017340; AAV82708.1; -; Genomic_DNA.
DR RefSeq; WP_011235108.1; NC_006512.1.
DR AlphaFoldDB; Q5QXU4; -.
DR SMR; Q5QXU4; -.
DR STRING; 283942.IL1876; -.
DR EnsemblBacteria; AAV82708; AAV82708; IL1876.
DR KEGG; ilo:IL1876; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_036368_4_3_6; -.
DR OMA; DYAVANQ; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000001171; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..220
FT /note="Phosphoserine phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435616"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 220 AA; 23501 MW; 60C08CC32DDFED5E CRC64;
MKHSSGLIVF DMDSTLIHIE CIDEIARLNN RYTKVSAITE AAMRGEIDFA ESLTQRVACL
EGIKESDLES LFSPIPFNPG AKELIQALQA AGWKTALVSG GFTWFANRVQ AALNLDAVVA
NQLEVADGCL TGKVLGDIVD AQVKAEQLQQ LAGHWNIPPD RTVAVGDGAN DGLMLKAAAV
GIAFNAKPAL QAIADYSVNS NNLLEILGCL KQSELIEPVI
