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Database: UniProt
Entry: A0A0A0JNK3_9MICO
LinkDB: A0A0A0JNK3_9MICO
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ID   A0A0A0JNK3_9MICO        Unreviewed;       411 AA.
AC   A0A0A0JNK3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN   ORFNames=N803_08345 {ECO:0000313|EMBL:KGN38728.1};
OS   Knoellia subterranea KCTC 19937.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN38728.1, ECO:0000313|Proteomes:UP000030011};
RN   [1] {ECO:0000313|EMBL:KGN38728.1, ECO:0000313|Proteomes:UP000030011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN38728.1,
RC   ECO:0000313|Proteomes:UP000030011};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia subterranea.";
RL   Submitted (AUG-2013) 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:KGN38728.1}.
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DR   EMBL; AVPK01000002; KGN38728.1; -; Genomic_DNA.
DR   RefSeq; WP_035903122.1; NZ_AVPK01000002.1.
DR   AlphaFoldDB; A0A0A0JNK3; -.
DR   STRING; 1385521.N803_08345; -.
DR   eggNOG; COG0560; Bacteria.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000030011; 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; 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; PF12710; HAD; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 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:UP000030011};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          100..170
FT                   /note="Phosphoserine phosphatase ACT"
FT                   /evidence="ECO:0000259|Pfam:PF21086"
FT   REGION          392..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   411 AA;  43288 MW;  30165CC89F221EF8 CRC64;
     MTTPTTPDQS PTLLVTLTGD DRPGVTSALF DAVAPTGALV LDLEQVVVRG QLTLGVLLRP
     SGHVSDVREA VGRVAEDLDL SVTIADGRGD NRRRPTGRAA VVVLGAPLRA RAVAAVSRSV
     AAHGANIDRI RRLSRYPVTT LEFDVSGADL HSLRRELSLV AAEESVDIAV SPAGLARRGR
     RLVVMDVDST LIQDEVIELL ARHAGREAEV AAVTERAMAG ELDFAESLHA RVATLAGLDA
     SVLEEVRQAV RLTPGARTLV RTLKRLGFTV ALVSGGFIEI VQPIADELSI DHARANRLEV
     VDGRLTGRVV GGVVDREGKA AALREFAEEA GLPLARTVAI GDGANDLDML GTAGLGIAFN
     AKQVVREQAD TAVNVPYLDA VLHLLGITRE EIEEADDADG TPTPAPAVEH G
//
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