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Database: UniProt
Entry: A0A1W1I1K1_9BACT
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ID   A0A1W1I1K1_9BACT        Unreviewed;       206 AA.
AC   A0A1W1I1K1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
GN   Name=thrH {ECO:0000313|EMBL:SLM46875.1};
GN   ORFNames=NSJP_0703 {ECO:0000313|EMBL:SLM46875.1};
OS   Nitrospira japonica.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=1325564 {ECO:0000313|EMBL:SLM46875.1, ECO:0000313|Proteomes:UP000192042};
RN   [1] {ECO:0000313|EMBL:SLM46875.1, ECO:0000313|Proteomes:UP000192042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Genome sequencing of Nitrospira japonica strain NJ11
RC   {ECO:0000313|EMBL:SLM46875.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001197};
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:0000256|ARBA:ARBA00000860};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR611863-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR611863-3};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
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DR   EMBL; LT828648; SLM46875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1I1K1; -.
DR   STRING; 1325564.NSJP_0703; -.
DR   KEGG; nja:NSJP_0703; -.
DR   OrthoDB; 9801134at2; -.
DR   Proteomes; UP000192042; Chromosome i.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.90.1470.10; thrh gene product, domain 2; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR011863; HSK-PSP.
DR   NCBIfam; TIGR02137; HSK-PSP; 1.
DR   PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR   PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF12710; HAD; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SLM46875.1};
KW   Kinase {ECO:0000313|EMBL:SLM46875.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192042};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000313|EMBL:SLM46875.1}.
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-1"
FT   ACT_SITE        12
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-1"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT   BINDING         93..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-3"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611863-2"
SQ   SEQUENCE   206 AA;  23408 MW;  004631AD944CA5A4 CRC64;
     MQKPVIACLD LEGVLVPEIW INVAQKTGIE ELKITTREMP DYDALMKRRL AILKEHSLAI
     ADIQAVIDKM GPLEGAPAFV AWLRERCQVI ILSDTFYQFA LPLMRQLDFP TLFCNQLEID
     PRGNILAHHM RMPNQKKHSV AAFKSLNFFT MAAGDAYNDT AMLGEADAGF FFRPPDHLPK
     EFPQFPVTQT YKELQMQFGK AGNLRP
//
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