ID A0A1W2TJU7_ROSNE Unreviewed; 306 AA.
AC A0A1W2TJU7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMD00023353_1701370 {ECO:0000313|EMBL:GAP88506.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP88506.1};
RN [1] {ECO:0000313|EMBL:GAP88506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP88506.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) 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};
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DR EMBL; DF977462; GAP88506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TJU7; -.
DR STRING; 77044.A0A1W2TJU7; -.
DR OMA; RKPIESW; -.
DR OrthoDB; 217676at2759; -.
DR Proteomes; UP000054516; 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:UP000054516}.
FT ACT_SITE 27
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 29
FT /note="Proton donor"
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 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 306 AA; 33375 MW; FB4527D5F41537E8 CRC64;
MGQSKYLTGN SAAIAEFLDK FDVFLFDCDG VLWSGDHVFE GTVETLELLR SKGKKVVFVT
NNSTKSRQDY QKKLIGMGIP SNIEEIFASA YSSAIYISRI LKLPGPHNKV FVLGESGIEQ
ELRTENVPFI GGTDPSLRRD MTPADFTGLA DGSMLDPDVG IVLAGLDFHV NYLKISMAYQ
YLRRGAVFLA TNLDSTLPMS QTFFPGAGSI SIPLINMIGA KPTALGKPSQ AMMDAVEGKF
HFDRTRTCMV GDRLDTDIQF GIQGGLGGTL AVLTGVTKKE HWEAEEAEFV PAYYVDRLSD
LRGGSS
//