ID A0A0S7DL05_9EURO Unreviewed; 318 AA.
AC A0A0S7DL05;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ALT_004055 {ECO:0000313|EMBL:GIM36173.1}, CNMCM8060_006712
GN {ECO:0000313|EMBL:KAF4176008.1}, IFM58399_05307
GN {ECO:0000313|EMBL:GFF38643.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4176008.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:GIM36173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM36173.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4176008.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4176008.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:GFF38643.1, ECO:0000313|Proteomes:UP000465261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58399 {ECO:0000313|EMBL:GFF38643.1,
RC ECO:0000313|Proteomes:UP000465261};
RA Takahashi H., Yaguchi T.;
RT "Draft genome sequence of Aspergillus lentulus IFM 58399.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAF4176008.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4176008.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:KAF4176008.1}.
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DR EMBL; BLKH01000028; GFF38643.1; -; Genomic_DNA.
DR EMBL; BCLY01000004; GIM36173.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000048; KAF4176008.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DL05; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_1954; -.
DR OrthoDB; 217676at2759; -.
DR Proteomes; UP000465261; Unassembled WGS sequence.
DR Proteomes; UP000713487; 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}.
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 42
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 318 AA; 35047 MW; 7DF4692D83E1B0C5 CRC64;
MAPPESPQPY PAMTTVPRYL TGKKEEIKEF LDKFDVFLFD CDGVLWSGDH LFPGTVETLE
MLRSNGKQVV FVTNNSTKSR ADYKKKLEKL GIPSTTEEIF SSSYSASIYI SRILKLPENK
RKVFVIGETG IEQELQTENV PFIGGTDPAY RREVRPDDYK LIAAGDPSLL DPEVGVVLVG
LDFHLNYLKL ALAYHYIKRG AVFLATNIDS TLPNSGTLFP GAGSMSAPLI MMLGEEPVSL
GKPNQAMMDA IEGKFKFDRS RTCMVGDRAN TDIRFGLEGK LGGTLGVLTG VSSKEDFLTG
PIRPSVYLDK LSDLLEAK
//