ID M7UR71_BOTF1 Unreviewed; 482 AA.
AC M7UR71;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BcDW1_1941 {ECO:0000313|EMBL:EMR89483.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR89483.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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; KB707748; EMR89483.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UR71; -.
DR STRING; 1290391.M7UR71; -.
DR HOGENOM; CLU_036368_5_1_1; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000012045; 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; 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 REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 271
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 482 AA; 52719 MW; 3220F1E68CDC7876 CRC64;
MAENEASARP GRPSLGNNVR SRSYLQEHQQ YRPPQQDGHH GIDSIVEGIQ GSAISSPTKS
FTQFNGVPSP QHPPKIVDSG LNHTLSHANC QPAPNTISDR MIATLIYKTK SPRVSVTDYP
PDRSPSPASS PSRSSVTSTS RAIPPNLAPV RTLSNFPLEP PPPDPEPLDH LYGSYISQLC
LTSFLHLIQS LPSRSGSDFL SSSHRCLDNP EHPSIVELTF SPIPDPTYLD LQDLRKHELL
YRFEREWNVD VILQHDTVLR RYPRLVVFDM DSTLIEQEVI DLIAASIGVE DAVSAITARA
MNGELDFSAS LRERAKLLKG VDADIFTKLR SVITPTKGAA ELIRALKRMG VKTAVLSGGF
IPLTQWLADH LGIDYAFANT LESDPSTNQL TGEVLGSIVN AEKKRDLLLE IAKKENVALD
QVVAMGDGAN DLLMMGVAGL GVAWNAKPVV QMEAQARLNG ESMLDLLHIF GLTAEEIKIL
IS
//
