SERB_PONAB
ID SERB_PONAB Reviewed; 225 AA.
AC Q5RB83;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000250|UniProtKB:P78330};
DE Short=PSP {ECO:0000250|UniProtKB:P78330};
DE Short=PSPase {ECO:0000250|UniProtKB:P78330};
DE EC=3.1.3.3 {ECO:0000250|UniProtKB:P78330};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000250|UniProtKB:P78330};
GN Name=PSPH {ECO:0000250|UniProtKB:P78330};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the last irreversible step in the biosynthesis of
CC L-serine from carbohydrates, the dephosphorylation of O-phospho-L-
CC serine to L-serine. L-serine can then be used in protein synthesis, to
CC produce other amino acids, in nucleotide metabolism or in glutathione
CC synthesis, or can be racemized to D-serine, a neuromodulator. May also
CC act on O-phospho-D-serine. {ECO:0000250|UniProtKB:P78330}.
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:0000250|UniProtKB:P78330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21209;
CC Evidence={ECO:0000250|UniProtKB:P78330};
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:0000250|UniProtKB:P78330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24874;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P78330};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000250|UniProtKB:P78330}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P78330}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P78330}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; CR858770; CAH90977.1; -; mRNA.
DR RefSeq; NP_001128794.1; NM_001135322.1.
DR AlphaFoldDB; Q5RB83; -.
DR SMR; Q5RB83; -.
DR STRING; 9601.ENSPPYP00000019666; -.
DR GeneID; 100189699; -.
DR eggNOG; KOG1615; Eukaryota.
DR InParanoid; Q5RB83; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome; Serine biosynthesis.
FT CHAIN 1..225
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000156881"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 20..22
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 52
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 53
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 109..111
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 109..111
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 158
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 158
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 182
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 182
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P78330"
SQ SEQUENCE 225 AA; 25008 MW; BD5D72697747FA30 CRC64;
MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA
ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA
SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG
ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE
