ID A0A0F5W2B9_9ACTN Unreviewed; 403 AA.
AC A0A0F5W2B9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=TN53_08275 {ECO:0000313|EMBL:KKD08518.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD08518.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD08518.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD08518.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (JAN-2015) 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:KKD08518.1}.
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DR EMBL; JXTE01000009; KKD08518.1; -; Genomic_DNA.
DR RefSeq; WP_046257756.1; NZ_JXTE01000009.1.
DR AlphaFoldDB; A0A0F5W2B9; -.
DR PATRIC; fig|1415558.3.peg.9036; -.
DR OrthoDB; 9792539at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000033641; 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; 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; 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.
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:UP000033641};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 13..93
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 187
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 403 AA; 42822 MW; F36E03CFB5D7D4C3 CRC64;
MSASQTSDVP TLLVKIFGKD RPGITAGLFD TLAAYSVDVV DIEQVVTRGR MVLCALVTEP
SRGLEGDLRK TVHSWAESMK MQAEIISGLG DNRPRGLGRS LVTVLGHPLT AEATAATAAR
ITKAGGNIDR IFRLAKYPVT AVEFAVSGVE TEPLRTALVT DAAALGVDVA VVAAGLHRRA
QRLVVMDVDS TLIQDEVIEL FAAHADCEDE VAEVTAAAMR GELDFEQSLH ARVALLEGLD
ASVVDKVRTE VRLTPGARTL IRTLKRLGYQ VGVVSGGFTQ VTDDLKERLG LDFAQANTLE
IVDGKLTGRV TGEIVDRAGK ARLLRRFAAE AGVPLAQTVA IGDGANDLDM LNAAGLGVAF
NAKPVVREAA HTAVNVPFLD TVLYLLGVTR EEVEAADTHD EID
//
