ID   A0A401KFX1_ASPAW        Unreviewed;       320 AA.
AC   A0A401KFX1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
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=AAWM_00977 {ECO:0000313|EMBL:GCB18092.1};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB18092.1, ECO:0000313|Proteomes:UP000286921};
RN   [1] {ECO:0000313|EMBL:GCB18092.1, ECO:0000313|Proteomes:UP000286921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB18092.1,
RC   ECO:0000313|Proteomes:UP000286921};
RA   Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT   "Aspergillus awamori IFM 58123T.";
RL   Submitted (SEP-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};
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:GCB18092.1}.
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DR   EMBL; BDHI01000001; GCB18092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401KFX1; -.
DR   STRING; 105351.A0A401KFX1; -.
DR   Proteomes; UP000286921; 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:UP000286921}.
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         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   320 AA;  35003 MW;  F61CFF16BCC63ABA CRC64;
     MATSAPSSEY PASTHTPRYL TGDAAGIQEF LDKFDVFLFD CDGVLWSGDH LFPGTNETLE
     MLRRKGKQVV FVTNNSTKSR ADYNKKLTAL GIPSNTEEIF SSSYSASIYI SRILSLPPNK
     RKVFVIGETG IEQELASENV PFIGGTDPAY RREITPEDYK DIAKGDSSTL LDPEVGVVLV
     GLDFHINYFK LALAYHYIRR GAVFLATNID STLPNSGTLF PGAGSMSAPL IMMLGKEPTS
     LGKPNQAMMD AIEGKFRFDR SRACMVGDRA NTDIRFGIEG RLGGTLGVLT GVSSKEEFVE
     GDIRPAVYLD RLADLLVVDQ
//