ID A0A1H3NHS6_9ACTN Unreviewed; 419 AA.
AC A0A1H3NHS6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05660209_03955 {ECO:0000313|EMBL:SDY88220.1};
OS Geodermatophilus africanus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137993 {ECO:0000313|EMBL:SDY88220.1, ECO:0000313|Proteomes:UP000198921};
RN [1] {ECO:0000313|EMBL:SDY88220.1, ECO:0000313|Proteomes:UP000198921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45422 {ECO:0000313|EMBL:SDY88220.1,
RC ECO:0000313|Proteomes:UP000198921};
RA de Groot N.N.;
RL Submitted (OCT-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; FNOT01000013; SDY88220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3NHS6; -.
DR STRING; 1137993.SAMN05660209_03955; -.
DR OrthoDB; 9792539at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000198921; 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; cd07500; HAD_PSP; 1.
DR Gene3D; 3.30.70.260; -; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; 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 Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 122..194
FT /note="Phosphoserine phosphatase ACT"
FT /evidence="ECO:0000259|Pfam:PF21086"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 419 AA; 43078 MW; 07FC517154EC168F CRC64;
MPLDPAPRTS PTAVPTPRAL LTVSGGDRPG VTAKLFAALA AAGGERPPVE VVDVEQVVVH
GQLVLGVVVG ALPAEGGPVG EGRFLAALER LAVEVSEATG VRVQVESADD TGLDAAPEGR
PHHVILLGRP VPPEAVAGAA SAIAGIGGNI EAIRRLSDYP VTSFELTVSG AEATALRTAL
ASVATTTGAD IAVEQVGLAR RSKRLIVLDV DSTLVRGEVI DELAARAGRA AEVARITAAA
MNGELDFAQS LRARVAALAG LPVEVLDEVR AALVLTPGAR TLIRTLKRLG FRCGIVSGGF
TQITDPLAEE LGLDFAAANT LEVADGRLTG GLVGEIVDRA GKARALVRFA DEYGIPLDQT
VAVGDGANDL DMLNAAGLGI AFNAKPYVRE QAHTALNQPY LDAVLQVLGF TRDEVLDAV
//
