ID A0A218ZG77_9HELO Unreviewed; 304 AA.
AC A0A218ZG77;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ORFNames=B2J93_1204 {ECO:0000313|EMBL:OWP06563.1};
OS Marssonina coronariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Marssonina.
OX NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP06563.1, ECO:0000313|Proteomes:UP000242519};
RN [1] {ECO:0000313|EMBL:OWP06563.1, ECO:0000313|Proteomes:UP000242519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:OWP06563.1,
RC ECO:0000313|Proteomes:UP000242519};
RA Cheng Q.;
RT "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT blotch.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OWP06563.1}.
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DR EMBL; MZNU01000044; OWP06563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218ZG77; -.
DR STRING; 503106.A0A218ZG77; -.
DR InParanoid; A0A218ZG77; -.
DR OrthoDB; 217676at2759; -.
DR Proteomes; UP000242519; 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:UP000242519}.
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 30
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 304 AA; 33187 MW; 3D7E000FAEF4810A CRC64;
MATLPRCLSG DSAAINEFID KFDIFLFDCD GVLWSGDHLF PGTVETLELL RSKGKKIVFV
TNNSTKSRPD YQKKLTSMGI PSNVDEIFAS AYSSAIYISR ILKLPGPKNK VFVLGEKGIE
TELKSEGIEF IGGTDPTFRR DITPEDFTGI ADGSLLDDNV GIVLAGLDFH VNYLKLSHAY
HYIRRGAVFL ATNLDSTLPS NHSFFPGAGS IVIPLINMSG RDPIALGKPS QAMMDSIEGK
FQFDRTKACM VGDRLNTDIK FGVDGKLGGT LAVLTGVSKK EDWEAKNTIA VPAYYVDKLS
DLRG
//