ID E1X0Q8_HALMS Unreviewed; 398 AA.
AC E1X0Q8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=BMS_1543 {ECO:0000313|EMBL:CBW26396.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW26396.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
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; FQ312005; CBW26396.1; -; Genomic_DNA.
DR RefSeq; WP_014244179.1; NC_016620.1.
DR AlphaFoldDB; E1X0Q8; -.
DR STRING; 862908.BMS_1543; -.
DR KEGG; bmx:BMS_1543; -.
DR PATRIC; fig|862908.3.peg.1469; -.
DR eggNOG; COG0560; Bacteria.
DR eggNOG; COG3830; Bacteria.
DR HOGENOM; CLU_036368_0_0_7; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000008963; Chromosome.
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; cd07500; HAD_PSP; 1.
DR Gene3D; 3.30.70.260; -; 1.
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 PRINTS; PR00119; CATATPASE.
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:UP000008963};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 11..89
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 398 AA; 43547 MW; 5722B89CD21F0536 CRC64;
MPKELNGKDV LIKVSGPDHP GITSELMSII KKTNNSLLDM GQSVTHGLLS LSFVINIANE
NTEQDHVLKD LLFAANNLNL TLDYKVVEPK AKSQKTEKFI LNCVSVEPLS AAFVCDISTI
LSKHGINIKR IDKVSPNEFK SLEISTQVPI GMNWQEVKAE LLKTSNGHQV DVAFLKDDIF
RRSKRLIVFD MDSTLIQTEV IDELADACGV GDEIRKITEE AMNGEIDFDE SLIKRVSKLK
GLEASKMKDI LDSLPLTPGV EDFIHTIKTL GYKVAVISGG FTFFANALKE KLGLDYAFAN
ELEIVNGKLT GNVVGTIINA EQKALLVKLI AQQESISLEQ VVAIGDGAND LPMLATAGLG
IAFHAKEVVK KEAEQHMSHG PMTSILYFLG ITDSSELL
//
