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Database: UniProt
Entry: A0A2C5XKS4_9PEZI
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ID   A0A2C5XKS4_9PEZI        Unreviewed;       304 AA.
AC   A0A2C5XKS4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=4-nitrophenylphosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE            Short=PNPPase {ECO:0000256|PIRNR:PIRNR000915};
DE            EC=3.1.3.41 {ECO:0000256|PIRNR:PIRNR000915};
GN   Name=pho2 {ECO:0000313|EMBL:PHH56133.1};
GN   ORFNames=CFIMG_002699RA {ECO:0000313|EMBL:PHH56133.1};
OS   Ceratocystis fimbriata CBS 114723.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH56133.1, ECO:0000313|Proteomes:UP000222788};
RN   [1] {ECO:0000313|EMBL:PHH56133.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH56133.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA   Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT   "Analysis of microsatellite markers in the genome of the plant pathogen
RT   Ceratocystis fimbriata.";
RL   Fungal Biol. 117:545-555(2013).
RN   [2] {ECO:0000313|EMBL:PHH56133.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH56133.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA   Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT   "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT   the plant pathogen, Ceratocystis fimbriata.";
RL   IMA Fungus 4:357-358(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) +
CC         phosphate; Xref=Rhea:RHEA:21664, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57917,
CC         ChEBI:CHEBI:61146; EC=3.1.3.41;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000915};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC       Note=Divalent metal ions. Mg(2+) is the most effective.
CC       {ECO:0000256|PIRSR:PIRSR000915-3};
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:PHH56133.1}.
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DR   EMBL; APWK03000002; PHH56133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5XKS4; -.
DR   STRING; 1035309.A0A2C5XKS4; -.
DR   OrthoDB; 217676at2759; -.
DR   Proteomes; UP000222788; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006349; PGP_euk.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   NCBIfam; TIGR01452; PGP_euk; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000915};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222788}.
FT   ACT_SITE        27
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   304 AA;  33262 MW;  62D8E012994B24C8 CRC64;
     MSQPQFISGN PAAIDKFLEG FDTFLFDCVL WSGDSVYENI PETLNMLKAK GKKIVFVTNN
     STKSRNDYQK KLTKMGIQCE LDEVFCSSYS ASIYISRMLQ LPEGKHKVFA IGESGMKEEL
     ESEGLVVVGG PADTYNRNIE PEDYQAMADK TALDPEVGVV LVGLDRKINY LKLSMAFHYI
     RNGAKFLATN IDSTLPSHHT FFPGAGACSI PLVHMTGETP LALGKPGQAM MDAIEGKFQL
     DRDRTCMVGD RLNTDIKFGI DGKLGGTLMV LTGVNQKADF EAKDAVAVPA FYANKLSDLL
     AASK
//
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