ID A0A0D1XJU8_EXOME Unreviewed; 398 AA.
AC A0A0D1XJU8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=PV10_08149 {ECO:0000313|EMBL:KIV88466.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV88466.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV88466.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV88466.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) 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; KN847525; KIV88466.1; -; Genomic_DNA.
DR RefSeq; XP_016220040.1; XM_016373129.1.
DR AlphaFoldDB; A0A0D1XJU8; -.
DR STRING; 212818.A0A0D1XJU8; -.
DR GeneID; 27325994; -.
DR VEuPathDB; FungiDB:PV10_08149; -.
DR HOGENOM; CLU_036368_5_1_1; -.
DR OMA; EWNVDVI; -.
DR OrthoDB; 789at2759; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000054302; 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; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 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 Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT REGION 29..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 398 AA; 43952 MW; F3646F59F6472261 CRC64;
MSHTNCIPKV QGQSARLVAT IFYNSLAPRH PHIHPDQSPQ AKPTEPLPVP EIAEGSAPTT
SIADYPLEPP APEPEPLDHL YGAYVSQLCL THFLATLDSL LIHNHASERR LTSSHRCLSP
DPVKPRVVEV TFNPPPNPEY LPFELITKHE SIYKFEREWN CEVILQQSTV FRRHKRLCVF
DMDSTLIQQE VIDEVAAFVG VKDKVAEITE RAMNGELDFA ASLKARVALL KGVPSDVFER
LKPHIVITPG ARELCKALKR LGYTLAVLSG GFQPLADWLA GELGLDHAFA NHLVSDPETK
TLTGELNPDY PIVDSQHKRN LLISLAAGKD IPLQQTMAVG DGANDIPMLK TAGLGVAWKA
KSKVQMEAPA RLNVAENMLD LVYLLGLTKH EVDELLQA
//
