ID   PPA1_ASPNG              Reviewed;         436 AA.
AC   P20584;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Phosphate-repressible acid phosphatase;
DE            EC=3.1.3.2;
DE   AltName: Full=Acid phosphatase PII;
DE   Flags: Precursor;
GN   Name=pacA; Synonyms=aphA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46951;
RX   PubMed=3224828; DOI=10.1016/0378-1119(88)90051-0;
RA   Macrae W.D., Buxton F.P., Sibley S., Garven S., Gwynne D.I., Davies R.W.,
RA   Arst H.N. Jr.;
RT   "A phosphate-repressible acid phosphatase gene from Aspergillus niger: its
RT   cloning, sequencing and transcriptional analysis.";
RL   Gene 71:339-348(1988).
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   -!- SUBUNIT: Monomer.
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DR   EMBL; M23540; AAA32700.1; -; Genomic_DNA.
DR   PIR; JT0386; JT0386.
DR   AlphaFoldDB; P20584; -.
DR   VEuPathDB; FungiDB:An13g01750; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1181574; -.
DR   VEuPathDB; FungiDB:ATCC64974_24940; -.
DR   VEuPathDB; FungiDB:M747DRAFT_367247; -.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR014390; Acid_Pase_Asper.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR039331; PPA-like.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   PANTHER; PTHR22953; PTHR22953; 1.
DR   PIRSF; PIRSF000900; Acid_Ptase_Asper; 1.
DR   SUPFAM; SSF49363; SSF49363; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..436
FT                   /note="Phosphate-repressible acid phosphatase"
FT                   /id="PRO_0000023980"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   436 AA;  47995 MW;  852E98ADD2859E15 CRC64;
     MKGTAASALL IALSATAAQA RPVVDERFPY TGPAVPIGDW VDPTINGNGK GFPRLVEPPA
     VKPATANPRN NVNVISLSYI PKGMHIHYQT PFGLGQLPAV RWGKDPRNLK QHGAGLLSHF
     QDWSSGRSPG IVQRRRAERH GLHQRSRNTQ AAGQGCPMRE LPFAWPTEVT ISYADELGII
     LVPTTGRSAT TAPVLLFRVA YSGRVQEALA RGEIPDQGEV VANRRRNFTA YQHPFRMPGP
     ETGGVGNFWY SFDYGLAHFV SIDGETDFAN SPEWNFAEDV TGNETLPSEA ETFITDSGPF
     GNVNGSVHET KSYEQWHLAE AGSGEGRPQQ DPVGLRHEPP PYVQFRLFLY QLHVREAFEG
     LLLSMAWMLT SLGDVCPFFK LVHHPLTLSS ATSTGTSSLS SRATAPSILP PCEQQHLLCP
     QRQVHHPHHQ RHGRQH