ID A0A3S4AK94_9PEZI Unreviewed; 344 AA.
AC A0A3S4AK94;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=TT172_LOCUS2111 {ECO:0000313|EMBL:SPQ19692.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ19692.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ19692.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; OUUZ01000001; SPQ19692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4AK94; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000289323; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
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; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 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 ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 344 AA; 37960 MW; E7B614927D282B82 CRC64;
MAPSSSLDTF PLEPPAAEPE PLDHLYGSFV SPMCIASFLH LMSTFPLPAG STDLTSAHRC
LKLDAKQDHH PVVVELTVSP APSVDYLSLA DLRKHELIYR FEREWNVDVA LRDDSLWRRY
PRLVVFDMDS TLITQEVIDL LAATIKDPPD LAARVADITH RAMLGELEFD SAFRERVKLL
TGLPGDIFHE LRPVLEVTNG VRPLLRALKR LGIKTAVLSG GFLPLTSWLA GELGIDYAHA
NEVVVDEVTG RLTGDVKGRI VGKERKRELL IEIAEKEGIP LEQVVAVGDG ANDLLMMDAA
GLGVAWNAKP RVQMEASARL NGDSLLDLLY LFGFTDEEIQ QLIA
//
