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Database: UniProt
Entry: A0A3N1NZR0_9GAMM
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ID   A0A3N1NZR0_9GAMM        Unreviewed;       407 AA.
AC   A0A3N1NZR0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00015196};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN   ORFNames=EDC38_1922 {ECO:0000313|EMBL:ROQ21299.1};
OS   Marinimicrobium koreense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Marinimicrobium.
OX   NCBI_TaxID=306545 {ECO:0000313|EMBL:ROQ21299.1, ECO:0000313|Proteomes:UP000273643};
RN   [1] {ECO:0000313|EMBL:ROQ21299.1, ECO:0000313|Proteomes:UP000273643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16974 {ECO:0000313|EMBL:ROQ21299.1,
RC   ECO:0000313|Proteomes:UP000273643};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) 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|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000256|ARBA:ARBA00009184}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROQ21299.1}.
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DR   EMBL; RJUK01000001; ROQ21299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1NZR0; -.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000273643; Unassembled WGS sequence.
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   CDD; cd04870; ACT_PSP_1; 1.
DR   CDD; cd04871; ACT_PSP_2; 1.
DR   CDD; cd07500; HAD_PSP; 1.
DR   Gene3D; 3.30.70.260; -; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   InterPro; IPR049148; PSP_ACT.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   NCBIfam; TIGR00338; serB; 1.
DR   PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR   PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF13740; ACT_6; 1.
DR   Pfam; PF21086; ACT_PSP_2; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01137; C1.6.1:_Phosphoserine_Phosphat; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273643};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          6..80
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        197
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   407 AA;  44283 MW;  61F1799F9E7FF0C1 CRC64;
     MKDIVLINVF GDDKPGVTSS LAAELSGFGA SILDIGQAVI HDDLALGMLV ALEPGRATAE
     TLQSAIRTRA DDLGVRVRFE NIDHQRYQEW VEQQGKPRHI VTLLSRQVMA EQIAELTAVT
     VRHGLNIDHI NRLSGRVPLD ALDTHSSACV EFSVRGAPAD TQALRADLME LSTRLEVDIA
     FQKDTPYRRN RRLVCFDMDS TLIEAEVIDE LAKAAGVGDE VIAITEAAMR GELDFQQSFA
     KRLSLLKGLD ESVLEGIARN LRLTEGAEKL IATLKKLGYK TAILSGGFEY FGRFLQQRLG
     VDYVYANELE IVDGKVTGQV SGTVVDGARK AQLLKQLAER EGITPEQVIA VGDGANDLPM
     LNAAGLGIAF RAKPLVKASA EHAISTLGLD AILYLLGFRD REHGDLS
//
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