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Database: UniProt
Entry: A0A1B9GZZ6_9TREE
LinkDB: A0A1B9GZZ6_9TREE
Original site: A0A1B9GZZ6_9TREE 
ID   A0A1B9GZZ6_9TREE        Unreviewed;       303 AA.
AC   A0A1B9GZZ6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-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=I316_01844 {ECO:0000313|EMBL:OCF36593.1};
OS   Kwoniella heveanensis BCC8398.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF36593.1, ECO:0000313|Proteomes:UP000092666};
RN   [1] {ECO:0000313|EMBL:OCF36593.1, ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|EMBL:OCF36593.1,
RC   ECO:0000313|Proteomes:UP000092666};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) 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; KI669495; OCF36593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9GZZ6; -.
DR   STRING; 1296120.A0A1B9GZZ6; -.
DR   Proteomes; UP000092666; 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:UP000092666}.
FT   ACT_SITE        25
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        27
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         25
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   303 AA;  33422 MW;  84BC5C9F8519A3D3 CRC64;
     MAPPFLKTRE EYQRLVDSVD TFLLDCDGVI YHGPKVVEGV KTVLDMFRAA GKKVIFVTNN
     GTKSRRKLCD TLNKLDLGAT IEECFGSAYA SAVYLAEVMN FPKDKKVYVV GEEGLEEELD
     EFGILHCGGS DPEDRNFKPP IIWDDFKPDP TVGAVVCAFD SWINYKKMAK AMSYLRDDPN
     VVLIQTNTDP TFPTHGTVYP GSGSLSIGIV NASKREPLVI GKPNKHMMDA VLAHHKFDPS
     RALMVGDNLL TDIEFGLNSN IRTLLVMGGV TKHEQIYGEN PSKTVPDLVI ESFGNFAVLA
     DKA
//
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