ID   PPA1_PICPA              Reviewed;         468 AA.
AC   P52291;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Acid phosphatase PHO1;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PHO1;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7557473; DOI=10.1016/0378-1119(95)00379-k;
RA   Payne W.E., Gannon P.M., Kaiser C.A.;
RT   "An inducible acid phosphatase from the yeast Pichia pastoris:
RT   characterization of the gene and its product.";
RL   Gene 163:19-26(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC   -!- INDUCTION: By phosphate starvation.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; U28658; AAA85503.1; -; Genomic_DNA.
DR   PIR; JC4285; JC4285.
DR   AlphaFoldDB; P52291; -.
DR   SMR; P52291; -.
DR   BRENDA; 3.1.3.2; 4827.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Signal; Stress response.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..468
FT                   /note="Acid phosphatase PHO1"
FT                   /id="PRO_0000023959"
FT   ACT_SITE        84
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        346
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   468 AA;  52691 MW;  AE555B8E27718C2C CRC64;
     MFSPILSLEI ILALATLQSV FAVELQHVLG VNDRPYPQRT DDQYNILRHL GGLGPYIGYN
     GWGIAAESEI ESCTIDQAHL LMRHGERYPS TNVGKQLEAL YQKLLDADVE VPTGPLSFFQ
     DYDYFVSDAA WYEQETTKGF YSGLNTAFDF GTTLRERYDH LINTSEEGKK LSVWAGSQER
     VVDTAKYFAQ GFMKSNYTDM VEVVALEEEK SQGLNSLTAR ISCPNYNSHI YKDGDFPNDI
     AEREADRLNT LSPGFNITAD DIPTIALYCG FELNVRGESS FCDVLSREAL LYTAYLRDLG
     WYYNVGNGNP LGKTIGYVYA NATRQLLENT EADPRDYPLY FSFSHDTDLL QVFTSLGLFN
     VTDLPLDQIQ FQTSFKSTEI VPMGARLLTE RLLCTVEGEE KYYVRTILND AVFPLSDCSS
     GPGFSCPLND YVSRLEALNE DSDFAENCGV PKNASYPLEL SFFWDDLS