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Database: UniProt
Entry: A0A1K1YDN3_9GAMM
LinkDB: A0A1K1YDN3_9GAMM
Original site: A0A1K1YDN3_9GAMM 
ID   A0A1K1YDN3_9GAMM        Unreviewed;       414 AA.
AC   A0A1K1YDN3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN02745752_02196 {ECO:0000313|EMBL:SFX60130.1};
OS   Marinospirillum alkaliphilum DSM 21637.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinospirillum.
OX   NCBI_TaxID=1122209 {ECO:0000313|EMBL:SFX60130.1, ECO:0000313|Proteomes:UP000182350};
RN   [1] {ECO:0000313|EMBL:SFX60130.1, ECO:0000313|Proteomes:UP000182350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21637 {ECO:0000313|EMBL:SFX60130.1,
RC   ECO:0000313|Proteomes:UP000182350};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FPJW01000008; SFX60130.1; -; Genomic_DNA.
DR   RefSeq; WP_072326507.1; NZ_FPJW01000008.1.
DR   AlphaFoldDB; A0A1K1YDN3; -.
DR   STRING; 1122209.SAMN02745752_02196; -.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000182350; 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   InterPro; IPR001763; Rhodanese-like_dom.
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; 2.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS50206; RHODANESE_3; 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:UP000182350};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          10..87
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          270..302
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   ACT_SITE        200
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   414 AA;  45508 MW;  FD7818D313C7890F CRC64;
     MNTQDRSIVL INLSGHDRPG ITSAITEILA GYGVNILDIG QAVIHDTLAL GLLAHLPPQA
     QHSPVLQELL FKAHEWGMQI RFTPVAEASY EHWVAGQGKG RYIVTLLGRR ITAEQIARVT
     RTVAENGLNI DRIHRLSGRV SMSRLAEPGR ACVEFSVRGD TLDTAELRRH FLALAGELEV
     DIAVQEDNIY RRNRRLVVFD MDSTLIEAEV IDELAKEAGV GEQVAEITER AMCGELDFNE
     SFKARVALLK GLDASVLEKI AQRLPITEGA EKLVSTLKRL GYRTAILSGG FTYFGEYLQQ
     KLGIDEVHAN LLEVEDGKVT GRVVGRVVDG QRKAELLQEI ARNEGINLEQ AIAVGDGAND
     LPMLGLAGLG IAFRAKPLVR QNARHALSTL GLDAILYLIG FSDRDIDQEL HHNN
//
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