ID A0A094G8L0_9PEZI Unreviewed; 306 AA.
AC A0A094G8L0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=V498_04973 {ECO:0000313|EMBL:KFY92415.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY92415.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY92415.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY92415.1}.
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DR EMBL; JPKA01001066; KFY92415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094G8L0; -.
DR HOGENOM; CLU_043473_0_0_1; -.
DR Proteomes; UP000029270; 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 30
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 32
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 306 AA; 33367 MW; B20F8D5D0E70BCD5 CRC64;
MATHALPKYL TGDTAAINEF IDKFDVFLFD CDGVLWSGDH VFEGVVDTLE LLRSRGKQTI
FVTNNSTKSR SDYLKKLTAM GIPSNVDEIF ASAYSSAIYI SKIMNLPGPK NKVFVLGEAG
IETELRECGV PFIGGTDPAY RRDITPADYT AMADGSLLDD DVAIVLAGLD FHINYLKLAV
AYQYLRRGAK FLATNTDSTL PSNHTFFPGA GSISIPLVNM TGQQPIALGK PSQAMMDSIE
GKFQFDRSKA CMIGDRLNTD IKFGIEGRLG GTLAVLTGVS KKEEWEVEGA ETVPAYYVDK
LSDIKV
//
